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1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
10-kDa heat shock protein-bound gamma-glutamine + methylamine
10-kDa heat shock protein N5-methylglutamine + NH3
-
-
-
-
?
2-aminobenzoyl-APE(gamma-Cad-2,4-dinitrophenyl)QEA + Gly-OMe
?
-
-
-
?
2-N-benzyloxycarbonyl-L-Lys-NH-CH2-CH2-NH-dansyl + Abeta1-40
?
-
residues 1-40 of beta-amyloid protein
-
-
?
2-N-benzyloxycarbonyl-L-Lys-NH-CH2-CH2-NH-dansyl + N-methyl-casein
?
-
-
-
-
?
5-(biotinamido)pentylamine + N,N-dimethylated casein
? + NH3
-
-
-
?
60-kDa heat shock protein-bound gamma-glutamine + methylamine
60-kDa heat shock protein N5-methylglutamine + NH3
-
-
-
-
?
Ac-PNPQLPF-OH + alkylamine
?
-
-
-
?
Ac-PQLPF-NH2 + putrescine
?
-
-
-
?
actin-bound gamma-glutamine + methylamine
actin N5-methylglutamine + NH3
-
-
-
-
?
Alfa-crystallin B glutamine + pentylamine
Alfa-crystallin B N5-pentylglutamine + NH3
-
-
-
?
alpha-actin-bound gamma-glutamine + methylamine
alpha-actin N5-methylglutamine + NH3
-
-
-
-
?
alpha-casein glutamine + alkylamine
alpha-casein N5-alkylglutamine + NH3
-
-
-
?
alpha-difluoromethylornithine + casein
?
-
-
-
-
?
alpha-difluoroornithine + casein
?
-
suicide substrate
-
-
?
alpha-lactalbumin + carbobenzoxy-L-glutaminylglycine
?
-
-
-
-
?
alpha-lactalbumin + dansylcadaverine
?
-
-
-
-
?
alpha-N-t-butyloxycarbonyl-L-Lys-CH2-CH2-dansyl + N,N-dimethylcasein
?
-
-
-
-
?
alpha-synuclein glutamine + alkylamine
alpha-synuclein N5-alkylglutamine + NH3
-
-
-
?
alpha2 plasmin inhibitor + ?
?
-
-
-
?
alphaB-crystallin + ?
?
-
-
formation of water-insoluble dimers or polymers
-
?
alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl + Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val
?
-
i.e. beta-amyloid protein peptide comprising residues 1-40
-
-
?
alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl + N,N-dimethylated casein
?
-
transpeptidation
-
-
?
ApoE glutamine + alkylamine
ApoE N5-alkylglutamine + NH3
-
-
-
?
apomyoglobin + carbobenzoxy-L-glutaminylglycine
?
-
-
-
-
?
apomyoglobin + dansylcadaverine
?
-
-
-
-
?
benzyloxycarbonyl-L-glutaminglycine + glycine ethyl ester
benzyloxycarbonyl-alpha-L-glutamyl(gamma-glycine ethyl ester)glycine + NH3
-
-
-
r
benzyloxycarbonyl-Pro-Gln-Nle-Phe + H2O
?
-
-
-
-
?
beta-casein + glycine ethylester
?
-
-
-
-
?
beta-casein glutamine + hydroxylamine
beta-casein N5-hydroxylglutamine + NH3
-
-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
betaB2-crystallin + ?
?
-
-
formation of water-insoluble dimers or polymers
-
?
biotinyl-5-pentylamine + N,N'-dimethylcasein
?
-
covalent incorporation of biotinyl-5-pentylamine into N,N'-dimethylcasein
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
biotinyl-HQSYVDPWMLDH + alkylamine
?
biotinylated TVQQEL + calcium binding protein S100A7
?
-
transglutaminase 2
-
-
?
bovine serum albumin glutamine + alkylamine
bovine serum albumin N5-alkylglutamine + NH3
-
-
-
-
?
casein glutamine + alkylamine
casein N5-alkylglutamine + NH3
casein glutamine + hydroxylamine
casein N5-hydroxyglutamine + NH3
-
-
-
-
?
casein glutamine + pentylamine
casein N5-pentylglutamine + NH3
CBP40 + ?
?
-
a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
-
-
?
CBZ-D-Ala-coumarin-7-yl ester + hydroxylamine
?
-
-
-
?
Cbz-Gln-Gly + alkylamine
?
-
-
-
-
?
Cbz-Gln-Gly + alkylamine
Cbz-Glu-Gly + NH3
-
-
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
Cbz-Gln-Gly + hydroxylamine
Cbz-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
CBZ-Gln-Gly-OH + hydroxylamine
CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
CBZ-Gly-coumarin-7-yl ester + hydroxylamine
?
-
-
-
?
CBZ-Gly-GABA-coumarin-7-yl ester + hydroxylamine
7-hydroxycoumarin + ?
-
-
-
?
CBZ-Gly-NH2 + AlaNH2
?
-
-
-
?
CBZ-Gly-NH2 + GlyNH2
?
-
-
-
?
CBZ-Gly-NH2 + L-leucine methyl ester
?
-
-
-
?
CBZ-L-Ala-coumarin-7-yl ester + hydroxylamine
?
-
-
-
?
Cbz-L-Gln-Gly + ?
?
-
-
-
-
?
Cbz-L-Gln-Gly + alkylamine
?
-
-
-
-
?
Cbz-L-Glu(gamma-p-nitrophenyl ester)-Gly + ?
?
Cbz-Phe-GABA umbelliferyl ester + ?
?
-
-
-
-
?
CBZ-Phe-GABA-coumarin-7-yl ester + hydroxylamine
7-hydroxycoumarin + ?
-
-
-
?
clathrin heavy chain-bound gamma-glutamine + methylamine
clathrin heavy chain N5-methylglutamine + NH3
-
-
-
-
?
collagen glutamine + alkylamine
collagen N5-alkylglutamine + NH3
-
-
-
?
cornifin-A glutamine + pentylamine
cornifin-A N5-pentylglutamine + NH3
cornifin-A is SPR1
-
-
?
cytoskeletal 1 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 1 keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 2 epidermal keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 2 epidermal keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 5 keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 5 keratin type II N5-methylglutamine + NH3
-
-
-
-
?
cytoskeletal 6A keratin type II-bound gamma-glutamine + methylamine
cytoskeletal 6A keratin type II N5-methylglutamine + NH3
-
-
-
-
?
dansyl-CAD + casein
?
-
-
-
-
?
dansylcadaverine + N,N-dimethylcasein
?
-
-
-
-
?
DDWDAMDEQIWF + beta-casein
?
-
-
-
-
?
desmoplakin glutamine + pentylamine
desmoplakin N5-pentylglutamine + NH3
-
-
-
?
dimethyl casein glutamine + putrescine
?
-
-
-
?
DQMMLPWPAVAL + spermine
?
-
specific substrate of factor XIII
-
-
?
EAQQIVM + monodansylcadaverine
?
-
liver transglutaminase, peptide derived from the N-terminal sequence of fibronection, first modified residue is mainly Q3
-
-
?
epiplakin glutamine + pentylamine
epiplakin N5-pentylglutamine + NH3
-
-
-
?
exendin 4 + 5-biotinamidopentylamine
?
-
-
modification at residues K12 and K27 of exendin 4
-
?
fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
-
-
-
-
?
fibronectin-bound gamma-glutamine + 5-biotinamidopentylamine
fibronectin N5-biotinamidopentylglutamine + NH3
-
-
-
-
?
fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
-
-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
filamin A-bound gamma-glutamine + methylamine
filamin A N5-methylglutamine + NH3
-
-
-
-
?
fluorescein-4-isothiocyanate-beta-AQG + NK6-AP
fluorescein-4-isothiocyanate-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
?
fluorescein-4-isothiocyanate-epsilon-aminocaproate-QG + NK6-AP
fluorescein-4-isothiocyanate-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
?
galectin-3-bound gamma-glutamine + methylamine
galectin-3 N5-methylglutamine + NH3
-
-
-
-
?
gelatin glutamine + alkylamine
gelatin N5-alkylglutamine + NH3
gliadin glutamine + alkylamine
gliadin N5-alkylglutamine + NH3
-
-
-
?
GTP + H2O
GDP + phosphate
H2A histone type 1-bound gamma-glutamine + methylamine
H2A histone type 1 N5-methylglutamine + NH3
-
-
-
-
?
H2B histone type 1-bound gamma-glutamine + methylamine
H2B histone type 1 N5-methylglutamine + NH3
-
-
-
-
?
H4 histone -bound gamma-glutamine + methylamine
H4 histone N5-methylglutamine + NH3
-
-
-
-
?
histamine + acetyl-alphaS1-casein
?
-
-
-
-
?
histamine + maleyl-bovine serum albumin
?
-
-
-
-
?
hornein glutamine + pentylamine
hornein N5-pentylglutamine + NH3
-
-
-
?
HQSYVDPWMLDH + spermine
?
-
specific substrate of factor XIII
-
-
?
hydroxylamine + carbobenzoxy-Gln-Gly
carbobenzoxy-Gln-Gly-hydroxamate + ?
-
other substrates are carbobenzoxy-Gln-Gln-Gly, carbobenzoxy-Gly-Gln-Gln-Gly, carbobenzoxy-Gly-Gly-Gln-Gly with 38%, 13% and 28% efficiency, respectively
-
?
involucrin + N,N'-dimethyl-casein
?
-
-
-
-
?
involucrin glutamine + pentylamine
involucrin N5-pentylglutamine + NH3
-
-
-
?
junction plakoglobin glutamine + pentylamine
junction plakoglobin N5-pentylglutamine + NH3
-
-
-
?
kallikrein-10 glutamine + pentylamine
kallikrein-10 N5-pentylglutamine + NH3
-
-
-
?
leishmanolysin + alkylamine
?
-
-
-
-
?
LGPQSKVIG + glycine-ethylester
?
-
i.e. K9, an optimized sequence based on beta-casein
-
-
?
LGPQSLVIG + glycine ethylester
?
-
i.e. K9(K7L), a modified optimized sequence based on beta-casein
-
-
?
loricrin + N,N'-dimethyl-casein
?
-
-
-
-
?
loricrin + N,N'-dimethylcasein
?
-
-
-
-
?
methylamine + succinyl-beta-casein
?
-
transglutaminase B
-
-
?
methylamine + succinylated alpha-casein
?
-
-
-
-
?
mono-6-amino-6-deoxy-alpha-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
mono-6-amino-6-deoxy-beta-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
mono-6-amino-6-deoxy-gamma-cyclodextrin + bovine pancreatic trypsin
?
-
-
-
-
?
monodansyl- cadaverine + actin
?
-
-
-
-
?
monodansylcadaverine + N,N'-dimethylated casein
?
Nemipterus sp.
-
-
-
-
?
monodansylcadaverine + N,N-dimethylcasein
?
monodansylcadaverine + succinylated casein
?
-
-
-
-
?
myo-inositol-1-phosphate synthase + alkylamine
?
-
-
-
-
?
N,N'-dimethyl casein glutamine + biotinylated pentylamine
?
the enzymatic activity is determined by measuring the fluorescence of biotinylated pentylamine crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Ala
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Gly-Gly
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Leu
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBZ-Gln-Phe
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Ser
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + CBz-Gln-Val
?
-
-
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
-
-
-
?
N,N-dimethylcasein + putrescine
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
N-(5-aminopentyl)biotinamide + N,N'-dimethylcasein
?
-
-
-
-
?
N-acetyl-PNPQLPF + alkylamine
?
-
-
-
?
N-carbobenzoxy-Gln-Gly + cadaverine
?
-
-
-
?
N-carbobenzoxy-L-glutaminyl-glycine + ovalbumin
?
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
L-glutamic acid-gamma-monohydroxamate + ?
-
specific high-affinity substrate
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + ?
L-glutamic acid gamma-monohydroxamate + ?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
N-Cbz-Gln-Gly + alkylamine
? + NH3
N-CBZ-Gln-Gly + hydroxylamine
?
-
-
-
-
?
N-CBZ-Gln-Gly + hydroxylamine
L-CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
N-Cbz-Glu(gamma-4-nitrophenylester)Gly + alkylamine
4-nitrophenol + ?
-
-
-
?
N-Cbz-Glu(gamma-p-nitrophenyl ester)Gly + ?
?
-
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
?
-
-
-
?
N-methyl-casein + dansylcadaverine
?
N-methyl-casein + O-methyl-Gly
?
Nalpha-benzyloxycarbonyl-L-Gln-Gly + alkylamine
?
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
?
-
-
-
-
?
neuropeptide Y + 5-biotinamidopentylamine
?
-
-
modification at residue Q34 of neuropeptide Y
-
?
NNEQVSPLTLLKLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q2N
-
-
?
NQENVSPLTLLKLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N
-
-
?
NQENVSPLTLLLLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12L
-
-
?
NQENVSPLTLLRLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide with modification Q4N, K12R
-
-
?
NQEQVSPLTLLKLGN + glycine ethylester
?
-
i.e. alpha2-antiplasmin peptide
-
-
?
nucleophosmin-bound gamma-glutamine + methylamine
nucleophosmin N5-methylglutamine + NH3
-
-
-
-
?
orexin B + 5-biotinamidopentylamine
?
-
-
modification at residues Q8 and Q12 of orexin B
-
?
ornithine + casein
?
-
-
-
-
?
p-nitrophenyl acetate + alanine ethylester
N-acetylalanine ethylester + p-nitrophenol
-
-
-
?
p-nitrophenyl trimethylacetate + H2O
p-nitrophenol + trimethylacetate
-
liver transglutaminase, ester hydrolysis in the presence of Ca2+
-
?
peptide glutamine + aminoacetonitrile
?
-
-
-
?
peptide glutamine + N-(biotinyl)cadaverine
?
-
-
-
?
plasminogen activator inhibitor 2 glutamine + pentylamine
plasminogen activator inhibitor 2 N5-pentylglutamine + NH3
-
-
-
?
plugin glutamine + alkylamine
plugin N5-alkylglutamine + NH3
-
preferred substrate
-
-
?
pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
?
-
-
-
-
?
pollen cell-wall protein + N,N-dimethylcasein
?
-
-
-
-
?
PQPQLPYPQPQLPY-NH2 + 5-biotinamidopentylamine
?
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
protein S100A10 glutamine + pentylamine
protein S100A10 N5-pentylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
protein-bound gamma-glutamine + methylamine
protein N5-methylglutamine + NH3
-
-
-
-
?
protein-bound gamma-glutamine + putrescine
?
-
-
-
-
?
putrescine + bovine muscle actin
?
-
preferred substrate
-
-
?
putrescine + fibronectin
?
putrescine + L-glutamine
bis-(glutamyl)-putrescine
-
-
-
-
?
putrescine + light-harvesting complex of photosystem II
?
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
putrescine + N,N-dimethylcasein
?
putrescine-alginate conjugate + dimethylated casein
?
-
putrescine (1,4-diaminobutane) covalently linked to alginate and low-methoxyl pectin, although the latter at higher concentrations, are able to act as effective acyl acceptor transglutaminase substrates in vitro using both dimethylated casein and soy flour proteins as acyl donors
-
-
?
putrescine-pectin conjugate + dimethylated casein
?
-
putrescine (1,4-diaminobutane) covalently linked to alginate and low-methoxyl pectin, although the latter at higher concentrations, are able to act as effective acyl acceptor transglutaminase substrates in vitro using both dimethylated casein and soy flour proteins as acyl donors
-
-
?
putrescine-pectin conjugate + soy flour protein
?
-
-
reacion produces edible films with low water vapor permeability and improved mechanical properties
-
?
QLQPFPQPQLPY + 5-biotinamidopentylamine
?
-
-
-
-
?
small proline-rich protein 3 + N,N'-dimethyl-casein
?
-
-
-
-
?
small proline-rich protein 3 + N,N'-dimethylcasein
?
-
-
-
-
?
spectrin alpha-bound gamma-glutamine + methylamine
spectrin alpha N5-methylglutamine + NH3
-
-
-
-
?
spermidine + L-glutamine
bis-(glutamyl)-spermidine
-
-
-
-
?
spermidine + light-harvesting complex of photosystem II
?
-
-
-
-
?
spermidine + N,N'-dimethylcasein
?
spermidine + N,N-dimethylcasein
?
-
-
-
-
?
spermine + light-harvesting complex of photosystem II
?
-
coupling efficiency in decreasing order: spermine, spermidine, putrescine
-
-
?
spermine + N,N'-dimethylcasein
?
SPR2D glutamine + pentylamine
SPR2D N5-pentylglutamine + NH3
-
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
sulforhodamine-beta-AQG + NK6-AP
sulforhodamine-labeled NK6-AP + ?
NK6-AP, recombinant Escherichia coli alkaline phosphatase with a N-terminal fused acyl-acceptor substrate peptide tag MKHKGS
-
-
?
SVS I + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS II + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS III + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
thermolysin(205-316) + carbobenzoxy-L-glutaminylglycine
?
-
-
-
-
?
thermolysin(205-316) + dansylcadaverine
?
-
-
-
-
?
thylakoid protein + putrescine
?
-
the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
-
-
?
transforming growth factor-beta glutamine + alkylamine
transforming growth factor-beta N5-alkylglutamine + NH3
-
-
-
?
TVQQEL + alkylamine
?
-
-
-
-
?
vimentin + 5-(biotinamido)pentylamine
?
-
transglutaminase 5
-
-
?
vimentin + ?
?
-
-
formation of water-insoluble dimers or polymers
-
?
vimentin-bound gamma-glutamine + methylamine
vimentin N5-methylglutamine + NH3
-
-
-
-
?
YELQRPYHSELP + biotinylated cadaverine
?
-
preferred substrate, acitve even in the peptide form
-
-
?
YELQRPYHSELP-glutathione-S-transferase + biotinylated cadaverine
?
-
preferred substrate
-
-
?
YENHKLPSSWPF + alkylamine
Y-N5-alkylglutaminyl-NHKLPSSWPF + NH3
N-terminally biotinylated peptide substrate
-
-
?
YEQHKLPSSWPF + pentylamine
Y-N5-pentylglutaminyl-QHKLPSSWPF + NH3
N-terminally biotinylated peptide substrate
-
-
?
Z-Gln-Gly + 3-anisidine
?
-
-
-
-
?
Z-Gln-Gly + 3-chloro-4-fluorobenzylamine
?
-
-
-
-
?
Z-Gln-Gly + 4-xylenediamine
?
-
-
-
-
?
Z-Gln-Gly + 5-aminovaleric acid
?
-
-
-
-
?
Z-Gln-Gly + 6-aminocaproic acid
?
-
-
-
-
?
Z-Gln-Gly + alkylamine
?
-
-
-
-
?
Z-Gln-Gly + aminoacetonitrile
?
-
high activity
-
-
?
Z-Gln-Gly + aniline
?
-
-
-
-
?
Z-Gln-Gly + benzylamine
?
-
high activity
-
-
?
Z-Gln-Gly + beta-alanine
?
-
-
-
-
?
Z-Gln-Gly + cadaverine
?
-
high activity
-
-
?
Z-Gln-Gly + cyclohexylamine
?
-
-
-
-
?
Z-Gln-Gly + cyclohexylmethylamine
?
-
-
-
-
?
Z-Gln-Gly + D-serine methyl ester
?
-
-
-
-
?
Z-Gln-Gly + ethylamine azide
?
-
high activity
-
-
?
Z-Gln-Gly + gamma-aminobutyric acid
?
-
-
-
-
?
Z-Gln-Gly + glycine
?
-
-
-
-
?
Z-Gln-Gly + glycine ethyl ester
?
-
high activity
-
-
?
Z-Gln-Gly + hydroxamate
L-glutamic acid gamma-monohydroxamate + NH3
-
high activity
-
-
?
Z-Gln-Gly + hydroxylamine
Z-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Z-Gln-Gly + L-cysteine ethyl ester
?
-
-
-
-
?
Z-Gln-Gly + L-serine methyl ester + hydroxamate
?
-
-
-
-
?
Z-Gln-Gly + L-threonine ethyl ester
?
-
-
-
-
?
Z-Gln-Gly + Nalpha-acetyl-L-lysine methyl ester
?
-
high activity
-
-
?
Z-Gln-Gly + O-benzylhydroxylamine
?
-
-
-
-
?
Z-Gln-Gly + O-methyl-Gly
?
Z-Gln-Gly + propargylamine
Z-Nepsilon-propargyl-Gln-Gly + NH3
-
high activity
-
-
?
Z-Gln-Gly + propylamine azide
?
-
high activity
-
-
?
Z-Gln-Gly + putrescine
?
-
-
-
?
Z-Gln-Gly + tryptophan methyl ester
?
-
-
-
-
?
Z-Glu(HC)-Gly-OH + alkylamine
?
-
-
-
?
Z-Glu(HC)-Gly-OH + H2O
?
-
-
-
?
Z-Glu(HMC)-Gly-OH + alkylamine
?
best substrate
-
-
?
Z-Glu(HMC)-Gly-OH + H2O
?
best substrate
-
-
?
Z-Glu(HMC)-OH + alkylamine
?
-
-
-
?
Z-Glu(HMC)-OH + H2O
?
-
-
-
?
Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin + alkylamine
Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxy-4-methylcoumarin
-
-
-
?
Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin + H2O
Z-Phe-gamma-Abu-OH + 7-hydroxy-4-methylcoumarin
-
-
-
?
Z-Phe-gamma-Abu-7-hydroxycoumarin + alkylamine
Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxycoumarin
-
-
-
?
Z-Phe-gamma-Abu-7-hydroxycoumarin + H2O
Z-Phe-gamma-Abu-OH + 7-hydroxycoumarin
-
-
-
?
Z-Phe-Glu(HC)-Gly-OH + alkylamine
?
-
-
-
?
Z-Phe-Glu(HC)-Gly-OH + H2O
?
-
-
-
?
Z-Phe-Glu(HMC)-Gly-OH + alkylamine
?
-
-
-
?
Z-Phe-Glu(HMC)-Gly-OH + H2O
?
-
-
-
?
Z-Phe-Glu(HMC)-OH + alkylamine
?
-
-
-
?
Z-Phe-Glu(HMC)-OH + H2O
?
-
-
-
?
[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[casein]-L-glutamine + alkylamine
[casein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[casein]-L-glutamine + biotin-labeled pentylamine
? + NH3
-
-
-
?
[osteopontin]-L-glutamine + 5-(biotinamido)pentylamine
?
-
-
-
-
?
[osteopontin]-L-glutamine + biotinyl-TVQQEL-OH
?
-
-
-
-
?
[protein]-gamma-glutamine + 5-(biotinamido) pentylamine
?
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
[T26 protein]-L-glutamine + 5-(biotinamido)-pentylamine
[T26 protein]-N5-pentyl-L-glutamine + biotin
-
-
-
-
?
additional information
?
-
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-carbobenzoxy-lysine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + alpha-S1-casein
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + butylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + ethylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
-
-
-
-
?
1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5'-N',N'-dimethylamino-1'-naphthalenesulfonyl)diamidopentane + propylamine
?
-
fluorescent substrate for detection and characterization of glutamine acceptor compounds
-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
-
-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
beta-crystallin, a major structural protein of the eye lens, is an archetypal TG2 substrate. Its target Gln residue is localized to a peptide sequence denoted A25 (TVQQEL), and is crosslinked to a Lys residue near the C-terminus of the same protein
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-HQSYVDPWMLDH + alkylamine
?
a TG2 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-HQSYVDPWMLDH + alkylamine
?
a TG2 isozyme specific biotinylated peptide substrate
-
-
?
casein glutamine + alkylamine
casein N5-alkylglutamine + NH3
-
-
-
?
casein glutamine + alkylamine
casein N5-alkylglutamine + NH3
-
-
-
-
?
casein glutamine + pentylamine
casein N5-pentylglutamine + NH3
the enzymatic activity of TGase is determined by measuring the fluorescence of MDC cross-linking to N,N'-dimethyl casein upon exposure
-
-
?
casein glutamine + pentylamine
casein N5-pentylglutamine + NH3
the enzymatic activity of TGase is determined by measuring the fluorescence of MDC cross-linking to N,N'-dimethyl casein upon exposure
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + D-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + hydroxylamine
Cbz-N5-hydroxyglutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-Gln-Gly + L-lysine
Cbz-N5-aminocaproyl-glutaminyl-Gly + NH3
-
-
-
?
Cbz-L-Glu(gamma-p-nitrophenyl ester)-Gly + ?
?
-
-
-
?
Cbz-L-Glu(gamma-p-nitrophenyl ester)-Gly + ?
?
-
-
-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
-
-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
the 220 kDa fibronectin monomer harbors multiple Gln residues susceptible to TG2 modification, including sites within its N-terminal collagen/fibrinbinding domain, its central (RGD-containing) integrin-binding domain, and its C-terminal glycosaminoglycan-binding domain. In addition, its N-terminal domain also harbors a high-affinity non-covalent docking site for TG2
-
-
?
gelatin glutamine + alkylamine
gelatin N5-alkylglutamine + NH3
-
-
-
-
?
gelatin glutamine + alkylamine
gelatin N5-alkylglutamine + NH3
-
-
-
?
GTP + H2O
GDP + phosphate
-
intrinsic GTPase activity
-
?
GTP + H2O
GDP + phosphate
-
Mg2+-dependent GTP hydrolytic activity
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
monodansylcadaverine + N,N-dimethylcasein
?
-
-
-
-
?
monodansylcadaverine + N,N-dimethylcasein
?
-
-
-
-
?
monodansylcadaverine + N,N-dimethylcasein
?
-
-
-
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
-
the enzymatic activity is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein (DMC) exposure. Fluorescence intensity of MDC incorporated into DMC is measured at excitation and emission wavelengths of 350 and 480 nm, respectively
-
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
the enzymatic activity of AcTG-1 is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N,N'-dimethyl casein glutamine + monodansylcadaverine
?
the enzymatic activity of TG2 is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein upon exposure
-
-
?
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
?
-
-
-
-
?
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
-
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + casein
?
-
trivial name dansylcadaverine, casein can be replaced by various synthetic peptide acceptors
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
-
trivial name dansylcadaverine
-
-
?
N-(5-aminopentyl)-5-dimethylamino-1-naphthalenesulfonamide + F-actin
?
-
trivial name dansylcadaverine
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
-
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
hydroxamic acid + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + ?
L-glutamic acid gamma-monohydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + ?
L-glutamic acid gamma-monohydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminyl-glycine + hydroxylamine
hydroxamate + ?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
-
-
-
-
?
N-Cbz-Gln-Gly + alkylamine
? + NH3
-
-
-
?
N-Cbz-Gln-Gly + alkylamine
? + NH3
-
-
-
?
N-CBZ-Gln-Gly + hydroxylamine
L-CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
-
?
N-CBZ-Gln-Gly + hydroxylamine
L-CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Gln-Gly + hydroxylamine
L-CBZ-Gln(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
?
N-CBZ-Glu-Gly + hydroxylamine
CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
-
-
-
?
N-methyl-casein + dansylcadaverine
?
-
-
-
-
?
N-methyl-casein + dansylcadaverine
?
-
-
-
-
?
N-methyl-casein + O-methyl-Gly
?
-
-
-
-
?
N-methyl-casein + O-methyl-Gly
?
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
immunohistochemic detection of 5-HT
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
immunohistochemic detection of 5-HT
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
immunohistochemic detection of 5-HT
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl)lysine bonds between appropriate substrates
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl)lysine bonds between appropriate substrates
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
lens transglutaminase, endogenous substrate beta-crystallin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase is probably involved in cell death program
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
aliphatic amine donors incorporated into benzyloxycarbonyl-L-Gln-Gly: hydroxylamine, methylamine, ethylamine, n-propylamine, n-butylamine, n-pentylamine, n-hexylamine, amino acids incorporated: L-lysine and D-lysine, amino acid esters incorporated: Gly, Ala, Val, and Met ethyl esters, Lys-analogs incorporated: L-ornithine, aliphatic amines with omega-carboxyl groups incorporated: 5-aminovaleric acid, epsilon-amino-n-caproic acid, 7-aminoheptanoic acid, omega-aminocaprylic acid, amines with functional groups incorporated: carbonyl, phosphate, sulfo groups and saccharides
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
H2O acts as substrate in the absence of amine acceptors
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
hydrolysis and aminolysis of certain aliphatic amides and active esters e.g. p-nitrophenyl esters and thiolesters
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
hydrolysis and aminolysis of certain aliphatic amides and active esters e.g. p-nitrophenyl esters and thiolesters
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate carbobenzoxy-L-Gln-Gly
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transglutaminase, amine donors: putrescine, phenylethylamine, glycinamide, histamine, methylamine, ethanolamine, amonia
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transaminase catalyzes also the hydrolysis and aminolysis of certain aliphatic amides and of active and some inactive esters
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
liver transglutaminase: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with benzyloxycarbonyl-L-glutaminylglycine, benzyloxycarbonyl-alpha-L-glutamyl(gamma-p-nitrophenyl ester) glycine, guinea pig hair follicle enzyme
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no amine donors are tyrosinamide, glycine, Gly-Leu, gamma-aminobutyric acid
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are acetylated B-chains of oxidized insulin
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
mediates membrane-structural changes
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
acyl-transfer reaction
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates of recombinant full-length transglutaminase 5: loricrin, small proline rich proteins 1, 2 and 3, and involucrin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are membrane-associated erythrocyte proteins
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are coagulation factor V, alpha2-macroglobulin, platelet myosin, actin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates of transglutaminase I and II: EF-hand-containing calcium binding proteins S100A11, S100A10 and S100A07
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
synthetic peptide acceptors for factor XIIIa in descending order of affinity: pyroglutamic acidEAQQIV, tert-butyloxycarbonylAQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
amine donors: primary amines
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
H2O acts as substrate in the absence of amine acceptors
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
recombinant factor XIIIa: substrate plasminogen-activator inhibitor type-2
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
donors: gamma-carboxamide groups of protein-bound glutamine, acceptors: epsilon-amino groups of protein-bound lysine
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
broad specificity towards amine acceptor
peptide bound glutamic acid with H2O as acceptor
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no amine donors are tyrosinamide, glycine, Gly-Leu, gamma-aminobutyric acid
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
dimerization of fibrin gamma chains, cross-linking of alpha2-plasmin inhibitor to fibrin alpha-chain and cross-linking of fibronectin to fibrin alpha-chains by factor XIIIa
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
endogenous substrates: cellular proteins e.g. aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphorylase kinase, crystallins, gluthathione S-transferase, actin, myosin, troponin, beta-tubulin, tau, Rho A, histone, alpha-oxoglutarate dehydrogenase, cytochromes, erythrocyte band III, CD38, acetylcholine esterase, collagen, fibronectin, fibrinogen, vitronectin, osteopontin, nidogen, laminin, LTBP-1, osteonectin, osteocalcin, substance P, phospholipase A2, midkine, exogenous substrates: wheat gliadin, whey proteins, soy proteins, pea legumin, Candida albicans surface proteins, HIV envelope glycoproteins gp120 and gp41, HIV aspartyl proteinase, hepatitis C virus core protein
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
lens transglutaminase, crosslinking of beta-crystallin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
synthetic peptide acceptors for transglutaminase in descending order: tert-butyloxycarbonylQQIV, tert-butyloxycarbonylAQQIV, pyroglutamic acidQQIV
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
crosslinking of Hammersten casein, crosslinking between Ac-IB and Bz-Gly-Lys
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
actin is probably the major endogenous substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
amine donors: diamines and polyamines
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are pepsin, thrombin, cellulase, creatine kinase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with catalase
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrates are fibrinogen, beta-lactoglobulin, casein, insulin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
chondrosarcoma transglutaminase B, no activity with type I collagen and fibronectin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase B: simultaneously gamma-polymer and alpha-polymer formation
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
aliphatic amine donors incorporated into benzyloxycarbonyl-L-Gln-Gly: hydroxylamine, methylamine, ethylamine, n-propylamine, n-butylamine, n-pentylamine, n-hexylamine, amino acids incorporated: L-lysine and D-lysine, amino acid esters incorporated: Gly, Ala, Val, and Met ethyl esters, Lys-analogs incorporated: L-ornithine, aliphatic amines with omega-carboxyl groups incorporated: 5-aminovaleric acid, epsilon-amino-n-caproic acid, 7-aminoheptanoic acid, omega-aminocaprylic acid, amines with functional groups incorporated: carbonyl, phosphate, sulfo groups and saccharides
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with native bovine serum albumin
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
no activity with bovine myosin, histone mixture, human serum fibronectin, spinach ribulose 1,5-diphosphate carboxylase-oxygenase, carbobenzoxyglutamine, carbobenzoxy-Asn-Gly
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
identification of natural protein substrates
-
?
putrescine + casein
?
-
-
-
-
?
putrescine + casein
?
-
alpha- or beta-casein
-
-
?
putrescine + casein
?
-
in vitro acceptor
-
-
?
putrescine + casein
?
-
-
-
-
?
putrescine + casein
?
-
alpha- or beta-casein
-
-
?
putrescine + casein
?
-
-
-
-
?
putrescine + casein
?
-
-
-
-
?
putrescine + casein
?
-
-
-
-
?
putrescine + fibronectin
?
-
in vivo acceptor
-
-
?
putrescine + fibronectin
?
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermine and spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
-
transglutaminase 5
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
diaminopropane and cadaverine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
spermidine can replace putrescine
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
putrescine + N,N'-dimethylcasein
?
-
-
-
-
?
putrescine + N,N-dimethylcasein
?
-
-
-
-
?
putrescine + N,N-dimethylcasein
?
-
-
-
?
spermidine + N,N'-dimethylcasein
?
-
-
-
-
?
spermidine + N,N'-dimethylcasein
?
-
-
-
-
?
spermine + N,N'-dimethylcasein
?
-
-
-
-
?
spermine + N,N'-dimethylcasein
?
-
-
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
-
TGase mediated biotinylation
-
-
?
Streptomyces subtilisin and TAMEP inhibitor (SSTI) + N-lauroylsarcosine
?
-
TGase mediated biotinylation
-
-
?
Z-Gln-Gly + H2O
?
-
-
-
-
?
Z-Gln-Gly + H2O
?
-
-
-
-
?
Z-Gln-Gly + O-methyl-Gly
?
-
-
-
-
?
Z-Gln-Gly + O-methyl-Gly
?
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
additional information
?
-
-
screening of a M13 phage display random peptide library to elucidate primary structures surrounding reactive glutamine residues that are preferred by transglutaminase. Enzyme prefers a sequence like Q-nonconserved amino acid-P-hydrophobic amino acid-D(P), Q-nonconserved amino acid-P-hydrophobic amino acid, or Q-nonconserved amino acid-nonconserved amino acid-hydrophobic amino acid-DP
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.530 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Bothamyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase-induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
?
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
additional information
?
-
synthesis and kinetic characterisation of water-soluble fluorogenic acyl donors for transglutaminase 2, overview. Development of a fluorimetric TGase 2 activity assay with release of 7-hydroxycoumarin (HC) by TGase 2-catalysed hydrolysis or aminolysis of Z-Phe-gamma-Abu-HC resulting in a measureable increase in fluorescence. No activity with Z-Phe-gamma-Abu-7-amido-4-methylcoumarin and Z-Glu(AMC)-Gly-OH. Because the assay of TGase 2 requires the presence of an antioxidant to prevent oxidation of the active-site cysteine residue, both DTT and tris(2-carboxyethyl)phosphine (TCEP) are employed for investigations into the spontaneous reactivity of the compounds at a concentration of 0.5 mM. C-terminal extension with glycine results in kobs values that are increased by a factor of approximately four
-
-
-
additional information
?
-
wild-type TG2 can catalyze synthesis of CBZ-protected dipeptides. Its donor substrate specificity is narrow, aromatic ester derivatives of Gly and D-Ala serve as donor substrates. A hydrophobic cavity formed by Trp332 and Phe334 dictates substrate specificity. TG2 enzymes exhibit broad specificity towards the acyl-acceptor substrate. Guinea pig liver transglutaminase (gTG2) catalyzes the cross-linking of peptides and proteins via the formation of gamma-glutamyl-epsilon-lysyl isopeptide bonds. gTG2-catalyzed peptide bond formation between various amino acid-derived donor and acceptor substrates is analyzed. gTG2 forms Gly-Xaa and D-Ala-Gly dipeptide products, confirming that the enzyme's natural transamidation activity can be co-opted for peptide synthesis, LC-MS analysis. An aromatic ester of Gly is the most efficient acyl-donor substrate tested, aromatic esters of D-Ala and L-Ala show 50fold lower reactivity or no reactivity, respectively. The native acyl-acceptor substrate is generally a lysine-containing protein or peptide, many nonnatural primary amines, such as glycinamide, and anilines, such as N,N-dimethyl-1,4-phenylenediamine, can also react. TG2 displays narrow specificity for its acyl-donor substrates. The side chain of a protein or peptide-bound L-Gln residue is the native substrate while the side chain of the similar amino acid L-Asn is not reactive. In addition to amides, gamma-glutamyl aromatic ester derivatives of L-Glu, such as Ncarbobenzyloxy-L-glutamyl(gamma-p-nitrophenyl ester)glycine, have also been shown to be acyl-donor substrates of TG2 and are used to measure the enzyme's activity. N-Carbobenzyloxyglycyl-coumarin-7-yl ester (CBZ-Gly-7HC), is also a donor substrate of TG2. Construction of acyl-enzyme intermediates, structure analysis, and structural basis, overview
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additional information
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the recombinant transglutaminase crosslinks casein, collagen and gelatin
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additional information
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the recombinant transglutaminase crosslinks casein, collagen and gelatin
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additional information
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enzyme as well as enzyme peptide BH3 interact with pro-apoptotic Bcl-2 family member Bax
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additional information
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enzyme is involved in the control of dynamic adhesion formation in cell spreading and migration via regulation of phospholipase C activity
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?
additional information
?
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enzyme may be involved in cataractogenesis
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?
additional information
?
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surface tissue transglutaminase amplifies integrin-mediated signaling to RhoA/Rho-associated coiled-coil containing serine/threonine protein kinase ROCK via integrin clustering and down.regulation of the Src-p190RhoGAP regulatory pathway
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?
additional information
?
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screening of a M13 phage display random peptide library to elucidate primary structures surrounding reactive glutamine residues that are preferred by transglutaminase. Enzyme prefers a sequence like or Q-nonconserved amino acid-nonconserved amino acid-hydrophobic amino acid-WP
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additional information
?
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study of enzyme specificity with Q-containing substrates based on beta-casein, K9-peptide and alpha2-antiplasmin. Factor XIIIa preferentially selects the Q2 residue for carrying out crosslinking processes.The E3 and Q4 provide supporting role in binding. When reaction occurs at Q2, then Q4 is sterically blocked. Deamidation of Q2 to E2 allows observation of reactivity at Q4. K12 position provides an additional favorable site of interaction with factor XIIIa surface
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additional information
?
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functions of TG2: wound healing, macrophage phagocytosis, TGF-beta activation, protein kinase activity, association with calreticulin, and association with G-protein coupled receptor GPR56. The majority of these functions are independent of the enzymatic transamidation activity of the protein. Transglutaminase 2 is involved in the pathogenesis of a number of diseases, such as celiac sprue, neurodegenerative disorders, diabetes, liver cirrhosis and fibrosis, renal scarring, and certain types of cancer. It is the enzymatic function of TG2 that is thought to contribute to the pathology or etiology of most of the aforementioned diseases
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?
additional information
?
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pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
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additional information
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TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
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?
additional information
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transglutaminase catalyses the crosslinking of proteins by formation of an isopeptide bond between a glutamyl carboxamide in one protein and a lysyl epsilon-amino group of another protein
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additional information
?
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type I transglutaminase catalyzes the formation of epsilon-(gamma-glutamyl)lysine bonds and is the key protein responsible for generation of the crosslinks. Tazarotene-induced gene 3 (TIG3) regulates TG1 activity
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?
additional information
?
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vimentin is a major arterial substrate for transglutaminase, transglutaminase-mediated vimentin dimerization produces a novel unifying pathway by which vasodilatory and remodeling responses may be regulated
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?
additional information
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enzyme preferably uses those glutamine and lysine residues that are in intrinsically disordered regions. To explain the complex physicochemical interaction between TG2 and its substrates spatial features must be considered as well
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?
additional information
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certain gluten peptides are excellent TG2 substrates, prompting analysis of the enzyme's substrate specificity. The most favorable substrates appear to harbor a reactive Gln within a Q-X-P motif, whereas sequences containing Q-P, Q-G, Q-X-X-P, or Q-X-X-G motifs are not recognized (X denotes any amino acid). A random 7-mer peptide library yields GQQQTPY, GLQQASV and WQTPMNS as preferred substrates of TG2
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additional information
?
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certain gluten peptides are excellent TG2 substrates, prompting analysis of the enzyme's substrate specificity. The most favorable substrates appear to harbor a reactive Gln within a Q-X-P motif, whereas sequences containing Q-P, Q-G, Q-X-X-P, or Q-X-X-G motifs are not recognized (X denotes any amino acid). A random 7-mer peptide library yields GQQQTPY, GLQQASV and WQTPMNS as preferred substrates of TG2
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additional information
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several substrate candidates of TG1 that may be essential for cornified envelope formation are identified and characterized
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additional information
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enzyme transglutaminase 2 (TG2) can catalyze deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. It is also known to harbor other enzymatic properties, including protein disulfide isomerase, GTP-dependent signal transduction, and ATP dependent protein kinase activity
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additional information
?
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enzyme transglutaminase 2 (TG2) can catalyze deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. It is also known to harbor other enzymatic properties, including protein disulfide isomerase, GTP-dependent signal transduction, and ATP dependent protein kinase activity
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additional information
?
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measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
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additional information
?
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measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
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additional information
?
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measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
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additional information
?
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measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
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additional information
?
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measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
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additional information
?
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
?
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
?
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
?
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protein 4.2 has ATPase activity. Noncatalytic structural role of protein 4.2
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additional information
?
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significant differences in the 15(V/K) KIEs on NH3 release determined for the deamidation (0.2%) and the transamidation (2.3%) of Z-Gln-Gly suggest the rate-limiting steps of TG2 active site acylation are dependent on the presence of the acyl acceptor. Substrate-induced conformational changes may play a role in promoting catalysis, mechanism, overview
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additional information
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microbial transglutaminase, MTG, from Kutzneria albida (KalbTG) exhibits no cross-reactivity with known MTG substrates or commonly used target proteins, such as antibodies. The motifs YRYRQ and RYESK are the best Gln and Lys substrates of KalbTG, respectively. Substrate specificity analysis, overview
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additional information
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microbial transglutaminase, MTG, from Kutzneria albida (KalbTG) exhibits no cross-reactivity with known MTG substrates or commonly used target proteins, such as antibodies. The motifs YRYRQ and RYESK are the best Gln and Lys substrates of KalbTG, respectively. Substrate specificity analysis, overview
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additional information
?
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microbial transglutaminase, MTG, from Kutzneria albida (KalbTG) exhibits no cross-reactivity with known MTG substrates or commonly used target proteins, such as antibodies. The motifs YRYRQ and RYESK are the best Gln and Lys substrates of KalbTG, respectively. Substrate specificity analysis, overview
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additional information
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major substrates of enzyme are in the range of 50-75 kDA
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additional information
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TG2 knockout mice are protected against the development of renal interstitial fibrosis, which is associated with a lesser activation of TGF-beta1 and reduced interstitial inflammation. TG2 plays an important role in the development of renal fibrosis
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?
additional information
?
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tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers. Transglutaminase-mediated oligomerization of soluble ephrin potentially represents a novel mechanism of forward signaling through Eph receptors and may extend the influence of A-type ephrins beyond cell contact mediated signaling
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additional information
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mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
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?
additional information
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mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
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?
additional information
?
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the enzyme uses pepT26-bound gamma-glutamine, vimentin-bound gamma-glutamine, actin-bound gamma-glutamine, heat shock protein 71-bound gamma-glutamine, heat shock protein 90-bound gamma-glutamine, beta-actin-like protein 2-bound gamma-glutamine, serpin H1-bound gamma-glutamine, heat shock protein 60-bound gamma-glutamine, lysozyme C1-bound gamma-glutamine, endoplasmin-bound gamma-glutamine, collagen alpha-1(III) chain-bound gamma-glutamine, elongation factor 1-alpha1-bound gamma-glutamine as substrates
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?
additional information
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no activity with PPPYSFYNSRWV
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?
additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
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-
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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the formation of intermolecular cross-links of casein and bovine serum albumin polymerized by MsTGase in the presence of DTT is observed
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additional information
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Nemipterus sp.
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enzyme catalyzes the cross-linking of the myosin heavy chains of Nemipterus sp.
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additional information
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possible role of TGase activity in the defense against a viral plant pathogen
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additional information
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no substrate: Boc-Gln-Gly
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additional information
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hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
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additional information
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transglutaminase reactions function in response to mechanical injury. Among the substrates are actin, 40 kDa Ca2+-binding protein CBP40, and a 33 kDa protein highly homologous to the eukaryotic adenine nucleotide translocator
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additional information
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enzyme is related with the first wave of spermatogenesis
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additional information
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TG2 is related to cell growth at an early stage of liver regeneration after partial hepatectomy, and regulates the growth capacity through down-regulation of the EGF receptor
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additional information
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evaluation of cross-reactivity of biotinylated peptides. TG-isoform-specific enzyme activity on rat brain tissue, overview. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
?
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evaluation of cross-reactivity of biotinylated peptides. TG-isoform-specific enzyme activity on rat brain tissue, overview. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
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additional information
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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transglutaminase (TGase) is an enzyme that exhibits several catalytic activities: the crosslinking of proteins by forming Nepsilon-(gamma-glutamyl) lysine bonds, the incorporation of polyamines into protein, and the deamidation of protein-bound glutamines
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additional information
?
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transglutaminase (TGase) is an enzyme that exhibits several catalytic activities: the crosslinking of proteins by forming Nepsilon-(gamma-glutamyl) lysine bonds, the incorporation of polyamines into protein, and the deamidation of protein-bound glutamines
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additional information
?
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transglutaminase (TGase) is an enzyme that exhibits several catalytic activities: the crosslinking of proteins by forming Nepsilon-(gamma-glutamyl) lysine bonds, the incorporation of polyamines into protein, and the deamidation of protein-bound glutamines
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additional information
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MTG can accept diverse fluorophores such asdansyl, fluorescein, and rhodamine derivatives in place of the benzyloxycarbonyl moiety when linked via a beta-alanine or epsilon-aminocaproic acid linker
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additional information
?
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posttranslational dimerization and multimerization of Camelidae anti-human TNF single domain antibodies in vitro catalyzed by microbial transglutaminases. Ribonuclease S-tag-peptide acts as a peptidyl substrate in covalent protein cross-linking reactions catalyzed by MTG. C-terminally fusion of the S-tag sequence to the anti-hTNF-variable heavy chain-domain results in fusion proteins that are efficiently dimerized and multimerized by MTG whereas anti-hTNF-variable heavy chain domain is not susceptible to protein crosslinking
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additional information
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no activity with carbamic acid, thiamine, 2-bromoethylamine, N-ethylmethylamine, sarcosine, butanol, butanethiol, or L-isoleucine methyl ester
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?
additional information
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transglutaminase catalyzes the acyl transfer reaction between gamma-carboxyamide groups (acyl donor) and primary amines (acyl acceptor). In proteins, it is able to crosslink the gamma-carboxyamide of glutamine and the primary epsilon-amine in lysine
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additional information
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crosslinking activity and IgG reactivity after digestion with cow and horse milk proteins, detailed overview
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additional information
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microbial transglutaminase (MTG) is a practical tool to enzymatically form isopeptide bonds between peptide or protein substrates. Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements. MTG can react readily with glutamines in alpha-helical, beta-sheet, and unstructured loop elements and does not favor one type of secondary structure. Building of a GB1 library where each variant contains a single glutamine at positions covering all secondary structure elements, detailed overview. The most reactive and selective variants display an over 100fold increase in incorporation compared to another developed aminated benzo[a]imidazo[2,1,5-cd]indolizine-type fluorophore, relative to native GB1
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additional information
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site-specific conjugation to native and engineered lysines in human immunoglobulins by microbial transglutaminase, overview. ESI-MS analysis of antibodies incubated with an acyl donor substrate and enzyme MTG, performed by incubation with ZQG-biotin and MTG at 37°C overnight followed by digestion with IdeS to generate Fab'2 and Fc fragments. A positive-control peptide with two known lysine acyl acceptor sites (GGSTKHKIPGGS) is genetically fused to the C-terminus of mAb1 HC or LC (HC-KTag or LC-KTag, respectively) and analyzed for transamidation. The addition of the KTag to the HC C-terminus blocks removal of Lys447, thereby allowing MTG to utilize Lys447 as an acyl acceptor site. Effect of single C-terminal amino acids on transamidation of HC Lys447, and analysis of transamidation of single lysine substitutions in gamma, iota, kappa, and lambda constant regions, overview. Optimal transamidation of an LC C-terminal lysine requires a spacer between Cys214 and the lysine. Analysis of transamidation of select single lysine substitutions, conducted by incubating samples with ZQG-biotin and MTG at 37°C overnight. Mutational analysis of binding sites
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additional information
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site-specific transglutaminase-mediated conjugation of interferon alpha-2b at glutamine or lysine residues. Reactivity of IFN alpha-2b to microbial transglutaminase (TGase) allows site-specific conjugation of this protein drug. Production of two monoderivatized isomers of IFN with high yields, mass spectrometry analysis of the two conjugates indicating that they are exclusively modified at the level of Gln101 if the protein is reacted in the presence of an amino-containing ligand (i.e. dansylcadaverine) or at the level of Lys164 if a glutamine-containing molecule is used (i.e. carbobenzoxy-L-glutaminyl-glycine, ZQG). The enzyme is absolutely specific, among the 10 Lys and 12 Gln residues of the protein, only Gln101 and Lys164 are located in highly flexible protein regions
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additional information
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SM-TAP procession of the pro-form zymogen is not essential for activity as TAMEP-treated and fully processed enzyme and the zymogen exhibit similar catalytic activity
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additional information
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SM-TAP procession of the pro-form zymogen is not essential for activity as TAMEP-treated and fully processed enzyme and the zymogen exhibit similar catalytic activity
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additional information
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
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the enzymatic transamidation reaction between a gamma-glutamyl donor (Z-Gln-Gly) and hydroxylamine releasing ammonia is coupled to the glutamate dehydrogenase (GDH)-catalyzed reductive amination of 2-oxoglutarate. The activity of GDH is dependent on NADH as a cofactor, whose disappearance can be monitored at 340 nm. NADH concentration was calculated based on a calibration curve, which in turn is used to calculate activity of mTG
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additional information
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the enzyme also catalyzes the deamination of amines. Glutamine is recognised as the acyl donor substrate by TGases due to the gamma-carboxyamide group. N-Benzyloxycarbonyl-L-glutaminylglycine (CBZ-Gln-Gly) is the standard glutamine peptide substrate used for TGases. Acyl acceptor substrates and acyl donor substrates, overview. The mTGase enzyme was reported to recognise L-isomer of lysine slightly more than its D-isomer when incorporated into a Z-Gln-Gly motif
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additional information
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TGase activity on the productivity of crosslinking peptide with tryptic casein, substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
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additional information
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coupling of mono- and bis-polyamines is catalysed in equal amounts, reaction only occurs in the light
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Alfa-crystallin B glutamine + pentylamine
Alfa-crystallin B N5-pentylglutamine + NH3
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?
alpha-casein glutamine + alkylamine
alpha-casein N5-alkylglutamine + NH3
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-
-
?
alpha-synuclein glutamine + alkylamine
alpha-synuclein N5-alkylglutamine + NH3
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-
-
?
ApoE glutamine + alkylamine
ApoE N5-alkylglutamine + NH3
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-
-
?
beta-crystallin glutamine + alkylamine
beta-crystallin N5-alkylglutamine + NH3
beta-crystallin, a major structural protein of the eye lens, is an archetypal TG2 substrate. Its target Gln residue is localized to a peptide sequence denoted A25 (TVQQEL), and is crosslinked to a Lys residue near the C-terminus of the same protein
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casein glutamine + alkylamine
casein N5-alkylglutamine + NH3
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?
CBP40 + ?
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a 40 kDa Ca2+-binding protein accumulating most significantly around injured areas
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?
Cbz-Gln-Gly + alkylamine
Cbz-Glu-Gly + NH3
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?
Cbz-L-Gln-Gly + alkylamine
?
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-
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-
?
collagen glutamine + alkylamine
collagen N5-alkylglutamine + NH3
-
-
-
?
cornifin-A glutamine + pentylamine
cornifin-A N5-pentylglutamine + NH3
cornifin-A is SPR1
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-
?
desmoplakin glutamine + pentylamine
desmoplakin N5-pentylglutamine + NH3
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-
-
?
epiplakin glutamine + pentylamine
epiplakin N5-pentylglutamine + NH3
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-
-
?
fibrinogen-bound gamma-glutamine + 5-(biotinamido)pentylamine
fibrinogen N5-(biotinamido)pentyl-glutamine + NH3
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-
-
-
?
fibronectin-bound gamma-glutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
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-
-
?
fibronectinglutamine + alkylamine
fibronectin N5-alkylglutamine + NH3
the 220 kDa fibronectin monomer harbors multiple Gln residues susceptible to TG2 modification, including sites within its N-terminal collagen/fibrinbinding domain, its central (RGD-containing) integrin-binding domain, and its C-terminal glycosaminoglycan-binding domain. In addition, its N-terminal domain also harbors a high-affinity non-covalent docking site for TG2
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?
gelatin glutamine + alkylamine
gelatin N5-alkylglutamine + NH3
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-
?
gliadin glutamine + alkylamine
gliadin N5-alkylglutamine + NH3
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-
-
?
hornein glutamine + pentylamine
hornein N5-pentylglutamine + NH3
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-
-
?
involucrin glutamine + pentylamine
involucrin N5-pentylglutamine + NH3
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-
-
?
junction plakoglobin glutamine + pentylamine
junction plakoglobin N5-pentylglutamine + NH3
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-
-
?
kallikrein-10 glutamine + pentylamine
kallikrein-10 N5-pentylglutamine + NH3
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-
-
?
leishmanolysin + alkylamine
?
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-
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-
?
myo-inositol-1-phosphate synthase + alkylamine
?
-
-
-
-
?
N,N-dimethylated casein-bound gamma-glutamine + dansyl-labeled amine nucleophile
?
-
-
-
?
N,N-dimethylcasein + putrescine
?
-
-
-
-
?
N-acetyl-PNPQLPF + alkylamine
?
-
-
-
?
N-carbobenzoxy-L-glutaminylglycine + NH2OH
L-glutamic acid-gamma-monohydroxamate + ?
-
specific high-affinity substrate
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
N-Cbz-L-glutaminyl(gamma-4-nitrophenylester)glycine + alkylamine
?
-
-
-
?
Nalpha-benzyloxycarbonyl-L-glutaminylglycine + hydroxylamine
?
-
-
-
-
?
plasminogen activator inhibitor 2 glutamine + pentylamine
plasminogen activator inhibitor 2 N5-pentylglutamine + NH3
-
-
-
?
plugin glutamine + alkylamine
plugin N5-alkylglutamine + NH3
-
preferred substrate
-
-
?
pollen cell-wall protein + histidine-tagged Xpr-green fluorescent protein
?
-
-
-
-
?
pollen cell-wall protein + N,N-dimethylcasein
?
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
protein S100A10 glutamine + pentylamine
protein S100A10 N5-pentylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
protein-bound gamma-glutamine + putrescine
?
-
-
-
-
?
SPR2D glutamine + pentylamine
SPR2D N5-pentylglutamine + NH3
-
-
-
?
thylakoid protein + putrescine
?
-
the incorporation of putrescine by the recombinant protein are 100fold greater using light-grown than dark-grown thylakoid protein extracts
-
-
?
transforming growth factor-beta glutamine + alkylamine
transforming growth factor-beta N5-alkylglutamine + NH3
-
-
-
?
[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
additional information
?
-
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
-
-
-
-
?
N-carboxybenzoyl-L-glutaminylglycine + alkylamine
?
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
?
protein glutamine + 5-hydroxytryptamine
protein N5-(5-hydroxy)tryptaminyl-glutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
transglutaminase is probably involved in cell death program
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
production of vaginal plug by postejaculatory clotting of rodent seminal plasma, formation of chemically resistant envelope of the stratum
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
mediates membrane-structural changes
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
dimerization of fibrin gamma chains, cross-linking of alpha2-plasmin inhibitor to fibrin alpha-chain and cross-linking of fibronectin to fibrin alpha-chains by factor XIIIa
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
involved in a wide variety of cellular processes, including growth, differentiation, stabilization of cytoskeleton
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
last enzyme in blood coagulation forming intermolecular gamma-glutamyl-epsilon-lysine crosslinks between fibrin molecules
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
plasmodia-specific 40000 Da protein LAV1-2 is the preferred in situ substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
actin is probably the major endogenous substrate
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.530 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
?
additional information
?
-
-
enzyme as well as enzyme peptide BH3 interact with pro-apoptotic Bcl-2 family member Bax
-
-
?
additional information
?
-
-
enzyme is involved in the control of dynamic adhesion formation in cell spreading and migration via regulation of phospholipase C activity
-
-
?
additional information
?
-
-
enzyme may be involved in cataractogenesis
-
-
?
additional information
?
-
-
surface tissue transglutaminase amplifies integrin-mediated signaling to RhoA/Rho-associated coiled-coil containing serine/threonine protein kinase ROCK via integrin clustering and down.regulation of the Src-p190RhoGAP regulatory pathway
-
-
?
additional information
?
-
-
functions of TG2: wound healing, macrophage phagocytosis, TGF-beta activation, protein kinase activity, association with calreticulin, and association with G-protein coupled receptor GPR56. The majority of these functions are independent of the enzymatic transamidation activity of the protein. Transglutaminase 2 is involved in the pathogenesis of a number of diseases, such as celiac sprue, neurodegenerative disorders, diabetes, liver cirrhosis and fibrosis, renal scarring, and certain types of cancer. It is the enzymatic function of TG2 that is thought to contribute to the pathology or etiology of most of the aforementioned diseases
-
-
?
additional information
?
-
-
pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
-
-
?
additional information
?
-
-
TGase induces rapid aggregation of amyloid beta-protein within 0.5-30 min, which is not observed with chemical cross-linkers. Both amyloid beta-protein40 and amyloid beta-protein42 are good substrates for TGase but show different aggregation patterns. Guinea pig and human TGase induced similar amyloid beta-protein aggregation patterns, and oligomerization is observed with amyloid beta-protein40 concentrations as low as 50 nM. The formed amyloid beta-protein40 species ranges from 5 to 6 nm spheres to curvilinear structures of the same width, but up to 100 nm in length. TGase-induced amyloid beta-protein40 assemblies are resistant to a 1 h incubation with either neprilysin or insulin degrading enzyme, whereas the monomer is rapidly degraded by both proteases
-
-
?
additional information
?
-
-
transglutaminase catalyses the crosslinking of proteins by formation of an isopeptide bond between a glutamyl carboxamide in one protein and a lysyl epsilon-amino group of another protein
-
-
?
additional information
?
-
-
type I transglutaminase catalyzes the formation of epsilon-(gamma-glutamyl)lysine bonds and is the key protein responsible for generation of the crosslinks. Tazarotene-induced gene 3 (TIG3) regulates TG1 activity
-
-
?
additional information
?
-
-
vimentin is a major arterial substrate for transglutaminase, transglutaminase-mediated vimentin dimerization produces a novel unifying pathway by which vasodilatory and remodeling responses may be regulated
-
-
?
additional information
?
-
certain gluten peptides are excellent TG2 substrates, prompting analysis of the enzyme's substrate specificity. The most favorable substrates appear to harbor a reactive Gln within a Q-X-P motif, whereas sequences containing Q-P, Q-G, Q-X-X-P, or Q-X-X-G motifs are not recognized (X denotes any amino acid). A random 7-mer peptide library yields GQQQTPY, GLQQASV and WQTPMNS as preferred substrates of TG2
-
-
-
additional information
?
-
-
certain gluten peptides are excellent TG2 substrates, prompting analysis of the enzyme's substrate specificity. The most favorable substrates appear to harbor a reactive Gln within a Q-X-P motif, whereas sequences containing Q-P, Q-G, Q-X-X-P, or Q-X-X-G motifs are not recognized (X denotes any amino acid). A random 7-mer peptide library yields GQQQTPY, GLQQASV and WQTPMNS as preferred substrates of TG2
-
-
-
additional information
?
-
several substrate candidates of TG1 that may be essential for cornified envelope formation are identified and characterized
-
-
-
additional information
?
-
-
major substrates of enzyme are in the range of 50-75 kDA
-
-
?
additional information
?
-
-
TG2 knockout mice are protected against the development of renal interstitial fibrosis, which is associated with a lesser activation of TGF-beta1 and reduced interstitial inflammation. TG2 plays an important role in the development of renal fibrosis
-
-
?
additional information
?
-
-
tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers. Transglutaminase-mediated oligomerization of soluble ephrin potentially represents a novel mechanism of forward signaling through Eph receptors and may extend the influence of A-type ephrins beyond cell contact mediated signaling
-
-
?
additional information
?
-
-
hemocyte enzyme may be activated upon injury to stop the bleeding by crosslinking proteins
-
-
?
additional information
?
-
-
transglutaminase reactions function in response to mechanical injury. Among the substrates are actin, 40 kDa Ca2+-binding protein CBP40, and a 33 kDa protein highly homologous to the eukaryotic adenine nucleotide translocator
-
-
?
additional information
?
-
-
enzyme is related with the first wave of spermatogenesis
-
-
?
additional information
?
-
-
TG2 is related to cell growth at an early stage of liver regeneration after partial hepatectomy, and regulates the growth capacity through down-regulation of the EGF receptor
-
-
?
additional information
?
-
transglutaminase catalyzes the acyl transfer reaction between gamma-carboxyamide groups (acyl donor) and primary amines (acyl acceptor). In proteins, it is able to crosslink the gamma-carboxyamide of glutamine and the primary epsilon-amine in lysine
-
-
-
additional information
?
-
-
tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins
-
-
?
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(1Z)-2-{[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl}ethanehydrazonic acid
-
-
(2-tert-butoxy-2-oxoethyl)(dimethyl)sulfonium
-
-
(2-[[(1R)-3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-1-carboxy-3-oxopropyl]amino]-2-oxoethyl)(dimethyl)sulfanium bromide
-
-
(2-[[4-(methoxycarbonyl)benzyl]oxy]-2-oxoethyl)(dimethyl)sulfonium
-
-
(2-[[6-(methoxycarbonyl)naphthalen-2-yl]methoxy]-2-oxoethyl)(dimethyl)sulfonium
-
-
(2E)-3-(4-nitrophenyl)-1-(pyridin-3-yl)prop-2-en-1-one
-
reversible, competitive with the acyl donor substrate
(2S)-2-[[(benzyloxy)carbonyl]amino]-4-[(prop-2-enoyl)amino]butanoic acid
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(2-hydroxybenzamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(3-hydroxybenzamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(4-hydroxybenzamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(nicotinamido)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(prop-2-yn-1-yloxy)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(pyrazine-2-carboxamido)-pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-fluoropyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-hydroxypyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-methoxypyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-phenylpyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-(benzyloxy)-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-amino-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-benzamido-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4R)-quinolin-3-ylmethyl 4-benzyl-2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(2-hydroxyphenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(3-chlorophenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(3-hydroxyphenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(4-chlorophenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(4-hydroxyphenyl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-(5-fluoro-1H-indol-3-yl)pyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-fluoropyrrolidine-1-carboxylate
-
-
(2S,4S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-4-phenylpyrrolidine-1-carboxylate
-
-
(3E)-1-benzyl-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-(2-oxopropylidene)-6-(trifluoromethoxy)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-(3-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-(4-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-(5-bromopyridin-3-yl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
-
-
(3E)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-1-(2-methylpropyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-1-(cyclohexylmethyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-1-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(2-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(3-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(3-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(4-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(4-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-(6-methoxypyridin-3-yl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-2-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(2-phenylethyl)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(3-phenylpropyl)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(propan-2-yl)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-phenyl-1,3-dihydro-2H-indol-2-one
-
-
(3E)-4-chloro-3-[2-oxo-2-(pyridin-4-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-5-nitro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-6-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-6-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-6-fluoro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-7-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(3E)-7-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
-
(3E)-7-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
-
(4R)-1-[(benzyloxy)carbonyl]-4-hydroxy-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
(5-bromothiophen-2-yl)(4-methyl-1H-pyrazol-1-yl)methanone
-
(E)-1-(1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-(3-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-(cyclohexylmethyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(E)-1-(1-benzyl-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
-
(naphthalen-2-yl)methyl 4-(N-acryloylglycyl)piperazine-1-carboxylate
-
-
(naphthalen-2-yl)methyl 4-[N-(bromoacetyl)glycyl]piperazine-1-carboxylate
-
-
(R)-quinolin-3-ylmethyl 3-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(1-methyl-1H-benzo[d]imidazol-2-yl)methyl 2-((((S)-3-bromo-4,5-dihydro-isoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(1H-benzo[d]imidazol-2-yl)methyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(R)-1-(naphthalen-2-yl)ethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(R)-1-(quinolin-3-yl)ethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-(S)-1-(naphthalen-2-yl)ethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-2,3-dimethoxybenzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-3-(benzyloxy)benzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-3-fluorobenzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-4-ethynylbenzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-benzyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-N-(((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-2-(1-(dimethylamino)naphthalene-5-sulfonamido)-3-(1H-indol-3-yl)propanamide
-
the majority of cellular TG2 cannot be inhibited in intact cells. The inhibitor potently inhibits cell lysate TG2 activity in the presence of calcium
(S)-N-(((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)pyrrolidine-2-carboxamide
-
-
(S)-prop-2-yn-1-yl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-pyridin-2-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-pyridin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-pyridin-4-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)-methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)-4-phenyl-2,5-dihydro-1H-pyrrole-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)-2-methylpyrrolidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)azetidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)piperidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 2-(2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)amino)-2-oxoethyl)pyrrolidine-1-carboxylate
-
-
(S)-quinolin-3-ylmethyl 3-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)-3,4-dihydro-1H-pyrido[3,4-b]indole-2(9H)-carboxylate
-
-
(S)-quinolin-4-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-quinoxalin-2-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
-
-
(S)-tert-butyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)pyrrolidine-1-carboxylate
-
-
1,1'-methanediylbis(1H-indole-2,3-dione)
-
-
1,1'-[(2,5-dimethylbenzene-1,4-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
-
-
1,1'-[(4,6-dimethylbenzene-1,3-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
-
-
1,3-dimethyl-2-[(2-oxopropyl)thio]-1H-imidazol-3-ium
-
-
1,3-dimethyl-2-[(2-oxopropyl)thio]imidazolium
-
pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
1-(((3R,5S)-5-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-carbamoyl)-1-((quinolin-3-ylmethoxy)carbonyl)pyrrolidin-3-yl)-carbamoyl)cyclobutanecarboxylic acid
-
-
1-(1-benzothiophen-2-yl)-3-[benzyl(tert-butyl)amino]propan-1-one
-
-
1-(6-methylpyridin-2-yl)piperazine
1-(6-nitropyridin-3-yl)piperazine
1-(ethenylsulfonyl)tricyclo[3.3.1.13,7]decane
-
-
1-(furan-2-yl)-3-[(2-hydroxyethyl)(propan-2-yl)amino]propan-1-one
-
-
1-(tricyclo[3.3.1.13,7]dec-1-yl)prop-2-en-1-one
-
-
1-acetyl-L-prolyl-6-imino-5-oxo-L-norleucyl-L-leucyl-L-prolyl-L-phenylalaninamide
-
1-ethyl-3-(4-methoxyphenyl)-6-methylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
-
1-[(2E)-3-(4-nitrophenyl)prop-2-enoyl]-3H-[1,2,3]triazolo[4,5-b]pyridin-1-ium-3-olate
-
reversible, competitive with the acyl donor substrate
1-[(benzyloxy)carbonyl]-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
2,3-dibromonaphthoquinone
-
0.015 mM, 41.5% inhibition
2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl prop-2-enoate
-
-
2-([2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl]sulfanyl)-1,3,4,5-tetramethyl-1H-imidazol-3-ium bromide
-
-
2-([3-(2-chlorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0015 mM, standard format
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
2-([3-(2-methoxyphenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00082 mM, standard format, at 0.00047 mM, full progress curve
2-([3-(3-chlorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0018 mM, standard format
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00045 mM, full progress curve
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
2-([3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-5-(2-hydroxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0008 mM, standard format, at 0.00025 mM, full progress curve
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-5-(3-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0014 mM, standard format
2-([3-(3-fluorophenyl)-5-methyl-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0002 mM, full progress curve
2-([3-(3-fluorophenyl)-5-phenyl-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00093 mM, standard format, at 0.00071 mM, full progress curve
2-([3-(3-fluorophenyl)-7-methyl-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00053 mM, full progress curve
2-([3-(3-methoxyphenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0021 mM, standard format
2-([3-(4-chlorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0005 mM, standard format, at 0.00016 mM, full progress curve
2-([3-(4-methoxyphenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0018 mM, standard format
2-([5-(4-fluorophenyl)-4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.0008 mM, standard format, at 0.00029 mM, full progress curve
2-aminonaphthoquinone
-
0.015 mM, 33.4% inhibition
2-bromo-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
-
-
2-bromo-3-hydroxynaphthoquinone
-
0.015 mM, 35.4% inhibition
2-chloro-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
-
-
2-[(2-hydrazinoethyl)thio]-3,5-diphenylthieno[2,3-d]pyrimidin-4(3H)-one
-
i.e. LDN-27219, reversible, slow-binding inhibitor that binds at the enzymes GTP site or a site that regulates binding of GTP
2-[(3-amino-2-oxopropyl)thio]-3-(3-fluorophenyl)-5-phenylthieno[2,3-d]pyrimidin-4(3H)-one
-
50% inhibition at 0.0053 mM, standard format
2-[(3-benzyl-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0012 mM, standard format, at 0.00048 mM, full progress curve
2-[(3-methyl-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0023 mM, standard format
2-[(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]-N,N-dimethylacetamide
-
-
2-[(4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)amino]acetohydrazide
-
50% inhibition at 0.0037 mM, full progress curve
2-[(4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)oxy]acetohydrazide
-
50% inhibition at 0.0045 mM, standard format
2-[(4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0008 mM, standard format, at 0.00025 mM, full progress curve
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
-
-
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
-
2-[(4-oxo-5-phenyl-3-pyridin-3-yl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.002 mM, standard format
2-[(6-methyl-4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
50% inhibition at 0.0015 mM, standard format, at 0.00016 mM, full progress curve
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
-
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
-
-
2-[[5-benzyl-3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
-
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
-
3-(3-methyl-3H-diaziren-3-yl)-N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]propanamide
-
reversible inhibitor and photolabel. In labeling experiments, specific labeling of residue C230
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
-
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
-
3-iodo-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
3-[(2E)-3-(3-nitrophenyl)prop-2-enoyl]-1H-benzotriazol-3-ium-1-olate
-
reversible, competitive with the acyl donor substrate
3-[(6-methyl-4-oxo-3,5-diphenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]propanohydrazide
-
50% inhibition at 0.0013 mM, standard format
3-[benzyl(ethyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
-
3-[benzyl(propan-2-yl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
-
3-[benzyl(propan-2-yl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(4-nitrophenyl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
3-[benzyl(tert-butyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(thiophen-2-yl)propan-1-one
-
-
3-[bis(2-hydroxyethyl)amino]-1-(furan-2-yl)propan-1-one
-
-
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(3-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid benzyl ester
-
4-(4-acryloylamino-2-chlorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-fluorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-methoxybenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-methylbenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylamino-2-trifluoromethylbenzenesulfonyl)-piperazine-1-carboxylic acid benzyl ester
-
4-(4-acryloylamino-3-fluorobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-chlorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-methylbenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-trifluoromethylbenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 3,5-difluorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid cyclopentyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid methyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-1-ylmethyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-2-ylmethyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 2,3-difluorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 4-fluorobenzyl ester
-
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid ethyl ester
-
4-(4-acryloylaminobenzenesulfonyl)[1,4]diazepane-1-carboxylicacid benzyl ester
-
4-(4-acryloylaminobenzenesulfonylamino)piperidine-1-carboxylic acid benzyl ester
-
4-(4-but-2-enoylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(4-cyanobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid benzyl ester
-
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
-
4-fluoro-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
4-fluoro-N-[(2S)-1-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
4-hydroxymercuribenzoate
-
99% inactivation
4-[(4-acryloylaminobenzenesulfonylamino)methyl]-piperidine-1-carboxylic acid benzyl ester
-
4-[4-(1-oxobut-2-ynylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-cyanoacetylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-ethoxycarbonylvinyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(2-fluoroacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-methylacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-methylbut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(2-oxopropionylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-(E)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-(Z)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-cyanomethylureido)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(3-diazo-2-oxopropyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(3-ethoxycarbonylallyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(4,4,4-trifluoro-3-methylbut-2-enoylamino)-benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(4,4,4-trifluorobut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(4-diazo-3-oxobutyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
4-[4-(acryloylmethyl-amino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-(ethoxycarbonylmethylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
-
4-[4-acryloylamino-3-(isobutylmethylamino)-benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
-
5,5'-dithiobis (2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
5,5'-methanediylbis(1H-indole-2,3-dione)
-
-
5,5'-oxybis(1H-indole-2,3-dione)
-
-
5-(4-acryloylaminobenzenesulfonyl)-2,5-diazabicyclo-[2.2.1]heptane-2-carboxylic acid tert-butyl ester
-
5-(4-acryloylaminobenzenesulfonyl)hexahydropyrrolo[3,4-c]pyrrole-2-carboxylic acid benzyl ester
-
5-(biotinamido)pentylamine
-
-
5-biotinamido pentylamine
5BP, 5BP is widely used in chromogenic TG2 assays, based on the ability of streptavidin conjugates to recognize its biotin substituent with high specificity
5-hydroxynaphthoquinone
-
0.015 mM, 46.1% inhibition
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxamide
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylic acid
6,6'-oxybis(1H-indole-2,3-dione)
-
-
6-diazo-5-oxo-L-norleucine
DON
Ac-P(6-diazo-5-oxo-L-norleucine)LPF-NH2
high-affinity irreversible inhibitor of TG2. The inhibitor stabilizes TG2 in an extended conformation that is dramatically different from earlier transglutaminase structures. The active site is exposed, revealing that catalysis takes place in a tunnel, bridged by two tryptophan residues that separate acyl-donor from acyl-acceptor and stabilize the tetrahedral reaction intermediates
acetonitrile
48% residual activity at 5% (v/v)
acrylonitrile
68 and 48% residual activity at 2.5 and 5.0 mM, respectively
alpha-difluoromethylornithine
-
2.6 mM, 50% inhibition of putrescine transfer to casein, suicide substrate, irreversible, competitive to putrescine or fibrinonectin
ammonium
a natural inhibitor of the enzyme, prevents cross-linking activity
AMP
-
weak inhibition of liver transglutaminase
benzyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
-
benzyl 4-[3-(acryloylamino)-2-oxopropanoyl]piperazine-1-carboxylate
-
-
benzyl 4-[3-[(ethenylsulfonyl)amino]-2-oxopropanoyl]piperazine-1-carboxylate
-
-
benzyl [(1R)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(methylamino)-2-oxoethyl]carbamate
-
irreversible
benzyl [(2S)-1-(4-acetylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-(4-benzoylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-(morpholin-4-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-1-[4-(phenylacetyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-1-[4-(phenylmethanesulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-1-[4-(propane-2-sulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(pyridine-2-carbonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(pyridine-3-carbonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(pyridine-4-carbonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(thiophene-2-sulfonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[(2-aminoethyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[(3-aminopropyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[(4-aminobutyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(2-chlorophenyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(7-hydroxy-2-oxo-2H-1-benzopyran-3-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
i.e. VA5
benzyl [(2S)-1-[4-(benzenesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(cyclohexanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(ethanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(methanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-1-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-1-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-2-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-(naphthalene-2-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-5-[(prop-2-enoyl)amino]pentan-2-yl]carbamate
-
-
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
-
benzyl [(9S)-19-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-3,10-dioxo-14,17-dioxa-4,11-diazanonadec-1-en-9-yl]carbamate
-
-
beta-mercaptoethanolamine
-
mechanism of inhibition, mercapto group significantly influences substrate behaviour
beta-selenoethanolamine
-
-
Boc-DON-Gln-Ile-Val-OMe
-
-
BOC-DON-QIV-OMe
-
0.1 mM and 1 mM for normal skin and keloid scar, respectively
Ce3+
-
not reversible by Ca2+
CP30a
reversible inhibitor
CP4d
reversible inhibitor
cystamine dihydrochloride
-
1 mM and 10 mM for normal skin and keloid scar, respectively
cysteamine
-
50% inhibition at 0.178 mM
cysteine
-
85% inhibition
diethyl dicarbonate
-
not without Ca2+
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]sulfonium
-
-
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-ylmethoxy)ethyl]sulfonium
-
-
dimethyl[2-oxo-2-[2-(tricyclo[3.3.1.13,7]dec-1-yl)ethoxy]ethyl]sulfonium
-
-
dithiothreitol
-
1.5 mM, 42% inhibition, 16.5 mM, 40% inhibition
DMF
90% residual activity at 2.5 and 5% (v/v)
ERW1069
-
i.e. ((S)-1-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)amino)-3-(5-fluoro-1H-indol-3-yl)-1-oxopropan-2-yl)carbamate
ethenesulfonic acid (4-bromophenyl)amide
-
ethyl [(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]acetate
-
-
fluorenylmethyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
-
reversible, competitive with the acyl donor substrate
Gd3+
-
not reversible by Ca2+
glucosamine
-
the TGase 2 inhibitor, might be an attractive novel target for treatment of malignant cancers
GMP
-
at low levels of Ca2
GSSG
-
reversible inactivation, activity can be restored by treatment with dithiothreitol
HgCl2
-
5 mM, 96% inhibition in the presence of 10 mM Ca2+
hydroxylamine
-
100 mM, complete inhibition
isatin
-
weak, reversible inhibitor
K+
-
1 mM, 41% inhibition
La3+
-
not reversible by Ca2+
Li+
-
10 mM, complete inhibition
lysine
-
1 mM, 43% inhibition of DEAE-unabsorbed transglutaminase, 90% inhibition of DEAE-absorbed transglutaminase
menadione
-
0.015 mM, 97% inhibition
methyl 3-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
-
-
methyl 4-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
-
-
methyl 4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]benzoate
-
reversible, competitive with the acyl donor substrate
methyl 4-[(acryloyloxy)methyl]benzoate
-
-
methyl 4-[[(bromoacetyl)oxy]methyl]benzoate
-
-
methyl 5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylate
methyl 6-[(acryloyloxy)methyl]naphthalene-2-carboxylate
-
-
methyl 6-[[(bromoacetyl)oxy]methyl]naphthalene-2-carboxylate
-
-
methyl 6-[[(chloroacetyl)oxy]methyl]naphthalene-2-carboxylate
-
-
methyl N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucinate bromide
-
-
methyl N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycinate
-
-
MgCl2
-
5 mM, 88% inhibition, 30% inhibition in the presence of 10 mM Ca2+
Monoiodoacetic acid
Nemipterus sp.
-
-
N,N-dimethyl-5-(piperazine-1-sulfonyl)naphthalen-1-amine
N-(2-aminoethyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
-
N-(2-bromophenyl)acrylamide
-
N-(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)prop-2-enamide
-
-
N-(3-aminopropyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
-
N-(3-bromophenyl)acrylamide
-
N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycine
-
irreversible, ratio kinact to Ki 0.33 micromol per min
N-(4-aminobutyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
-
N-(4-bromobenzyl)acrylamide
-
N-(4-bromophenyl)acrylamide
-
N-(4-bromophenyl)propionamide
-
N-(4-fluorophenyl)acrylamide
-
N-(4-[4-[2-(2-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
N-(4-[4-[2-(3-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
N-(4-[4-[2-(4-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]- phenyl)acrylamide
-
N-(4-[4-[2-(4-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
-
N-(phenylcarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-(tert-butoxycarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-acetyl-P(6-diazo-5-oxo-L-norleucine)LPF-NH2
-
active-site inhibitor
N-benzyloxycarbonyl-L-glutaminyl-6-(dimethylsulfonio)-5-oxo-L-norleucine
-
pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
N-carbobenzyloxy-L-phenylalanine 2-(acrylamido)ethylamide
-
-
N-carbobenzyloxy-L-phenylalanine 4-(acrylamido)butylamide
-
-
N-carbobenzyloxy-L-phenylalanine 4-(chloroacetylamido)butylamide
-
-
N-carbobenzyloxy-L-phenylalanine 6-(acrylamido)hexylamide
-
-
N-carbobenzyloxy-L-phenylalanine 6-(chloroacetylamido)hexylamide
-
-
N-carbobenzyloxy-L-phenylalanine 8-(acrylamido)octylamide
-
-
N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
-
0.01 mM, 91% and 92% inhibition of chondrosarcoma transglutaminases B and C respectively
N-[(2-phenylethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(2S)-4-[(3-methoxy-1,2,4-thiadiazol-5-yl)amino]-2-[(phenoxycarbonyl)amino]butanoyl]glycine
-
irreversible, ratio kinact to Ki 0.71 micromol per min
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]tryptophanamide
-
-
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(2-phenylethoxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(naphthalen-2-yloxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-3-ylmethoxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-4-ylmethoxy)carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-5-hydroxy-L-tryptophanamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-L-tyrosinamide
-
irreversible
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[5-(dimethylamino)naphthalen-2-yl]sulfonyl]-L-tyrosinamide
-
study on pharmacokinetics, pharmacodynamics, and bioavailability
N-[(5S)-5-(2-cyclohexylacetamido)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(3-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(4-bromophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(4-chlorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(4-iodophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[2-(4-methylphenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[[(4-fluorophenyl)carbamothioyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[[(4-fluorophenyl)carbamoyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[[(4-fluorophenyl)methyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-5-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-(4-phenylpiperazin-1-yl)hexyl]prop-2-enamide
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-3-yl)piperazin-1-yl]hexyl]prop-2-enamide
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-4-yl)piperazin-1-yl]hexyl]prop-2-enamide
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-[6-(trifluoromethyl)pyridin-3-yl]piperazin-1-yl]hexyl]prop-2-enamide
N-[(5S)-6-oxo-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]-5-(2,2,2-trifluoroacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(3-methylphenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(4-fluorobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(4-nitrobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(4-nitrophenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-bromopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-chloropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-chloropyridine-2-carbonyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-fluoropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-fluoropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-iodopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamothioyl)amino]hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylmethanesulfonyl)amino]hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(pyridin-2-yl)acetamido]hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-2-yl)acetamido]hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-3-yl)acetamido]hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
N-[(5S)-6-[4-(6-tert-butylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-[(4-fluorophenyl)methyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(5S)-6-[4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
N-[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]glycine
-
-
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-3-[(prop-2-enoyl)amino]-L-alanine
-
-
N-[(benzyloxy)carbonyl]-L-alanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-alpha-aspartyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-isoleucyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-5-oxo-6-[(1,3,4,5-tetramethyl-1H-imidazol-3-ium-2-yl)sulfanyl]-L-norleucine
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(diethylsulfonio)-5-oxo-L-norleucine
-
-
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]-L-tryptophyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[(benzyloxy)carbonyl]glycyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N-[4-(4-cyclopentanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
-
N-[4-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
-
N-[4-(4-phenylpiperazine-1-sulfonyl)phenyl]acrylamide
-
N-[4-(4-pyridin-2-ylpiperazine-1-sulfonyl)phenyl]acrylamide
-
N-[4-(aminomethyl)benzyl]-3-(5-[[[[(E)-2-phenylethenyl]sulfonyl](pyridin-2-ylmethyl)amino]methyl]-1,2,4-oxadiazol-3-yl)benzamide
-
N-[4-(piperazine-1-sulfonyl)phenyl]acrylamide
-
N-[4-(pyrrolidine-1-sulfonyl)phenyl]acrylamide
-
N-[4-methanesulfonylphenyl]acrylamide
-
N-[4-methoxyphenyl]acrylamide
-
N-[4-nitrophenyl]acrylamide
-
N-[4-phenoxyphenyl]acrylamide
-
N-[4-trifluoromethylphenyl]acrylamide
-
N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]acetamide
-
reversible, competitive with the acyl donor substrate
N-[4-[4-(2-phenylcyclopropanecarbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(2-trifluoromethylphenyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[4-[4-(3-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(3-phenylpropionyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(3-phenylpropyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(3-trifluoromethylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(4,4-difluoropiperidine-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(4-phenylbutyl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(6-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
-
N-[4-[4-(6-trifluoromethylpyridin-3-yl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[4-[4-(octahydroisoquinoline-2-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(octahydroquinoline-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
-
N-[4-[4-(piperidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[4-[4-(pyrrolidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
-
N-[5-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-pyridin-2-yl]acrylamide
-
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyridin-2-yl]acrylamide
-
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyrimidin-2-yl]acrylamide
-
N-[[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
N-{[(5S)-3-bromo-4,5-dihydro-1,2-oxazol-5-yl]methyl}-5-fluoro-Nalpha-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
N2-[(benzyloxy)carbonyl]-L-lysyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
-
-
N2-[(benzyloxy)carbonyl]-N5-prop-2-enoyl-L-ornithine
-
-
N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycine
-
-
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysinamide
-
-
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysine
-
-
N5-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-ornithylglycine
-
irreversible, ratio kinact to Ki 0.55 micromol per min
N6-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-lysylglycine
-
irreversible, ratio kinact to Ki 0.72 micromol per min
Na+
-
1 mM, 57% inhibition
Na-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluorotryptophanamide
-
-
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
naphthoquinone
-
0.015 mM, complete inhibition
NC-I052
irreversible inhibitor
NC9
potent inhibitor, NC9 inhibiting osteoclastogenesis, also inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect ofNC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected; potent inhibitor, NC9 inhibiting osteoclastogenesis, also inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect ofNC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected; potent inhibitor, NC9 inhibiting osteoclastogenesis, also inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect ofNC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected
NEM
-
34.38% activity remaining at 10 mM
o-phenanthroline
-
not reversible by Ca2+
ornithine
-
weak, suicide substrate in the presence of casein
Pb(CH3COO)2
-
1 mM, 56% inhibition
Pb2+
-
5 mM Pb(CH3COO)2, 80% inhibition
PCMB
-
1.62% activity remaining at 10 mM
phenyl methyl sulfonyl fluoride
-
10 mM, complete inhibition
PMSF
-
40.79% activity remaining at 10 mM
pyrrolidine-1-carboxylic acid (4-acryloylaminophenyl)-amide
-
quinolin-3-ylmethyl [(1S)-2-([[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]amino)-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
quinolin-3-ylmethyl [(1S)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
R281
irreversible inhibitor
-
S-nitroso-N-acetylpenicillamine
-
NO-donor, 8-16 mM, almost complete inhibition of transglutaminases 1 and 3, weak inhibition of transglutaminase 3
Sodium citrate
-
above 10 mM, complete inactivation
SQAETYR
-
noncompetitive inhibition
SYAETYR
-
noncompetitive inhibition
Tb3+
-
noncompetitive inhibition of factor XIIIa, at high Ca2+-levels, not reversed by Ca2+
tert-butyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
-
tert-butyl 4-(4-fluorobenzoyl)piperazine-1-carboxylate
tert-butyl 4-(4-nitrobenzoyl)piperazine-1-carboxylate
tert-butyl 4-(6-chloropyridine-2-carbonyl)piperazine-1-carboxylate
tert-butyl 4-(6-fluoropyridin-2-yl)piperazine-1-carboxylate
tert-butyl 4-(6-fluoropyridin-3-yl)piperazine-1-carboxylate
tert-butyl 4-(6-iodopyridin-2-yl)piperazine-1-carboxylate
tert-butyl 4-(6-nitropyridin-2-yl)piperazine-1-carboxylate
tert-butyl 4-(6-phenylpyridin-2-yl)piperazine-1-carboxylate
tert-butyl 4-(6-tert-butylpyridin-2-yl)piperazine-1-carboxylate
tert-butyl 4-(pyridin-3-yl)piperazine-1-carboxylate
tert-butyl 4-[(4-fluorophenyl)methyl]piperazine-1-carboxylate
tert-butyl 4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazine-1-carboxylate
tert-butyl 4-[6-(methoxycarbonyl)pyridin-3-yl]piperazine-1-carboxylate
tert-butyl 4-[6-(trifluoromethyl)pyridin-3-yl]piperazine-1-carboxylate
tert-butyl N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycinate
-
irreversible, ratio kinact to Ki 0.78 micromol per min
tert-butyl N6-acryloyl-N2-[(benzyloxy)carbonyl]-L-lysylglycinate
-
tert-butyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
-
reversible, competitive with the acyl donor substrate
tetrathionate
-
inactivation, not reversible by dithiothreitol
tricyclo[3.3.1.13,7]dec-1-ylmethyl bromoacetate
-
-
tricyclo[3.3.1.13,7]dec-1-ylmethyl prop-2-enoate
-
-
UTP
-
50% as effective as ATP
VA4
-
the inhibitor also inhibits epidermal cancer stem cell invasion with an EC50 of 0.0039 mM
vitamin K1
-
0.015 mM, 10% inhibition
vitamin K2
-
0.015 mM, 75% inhibition
Z-DON-Val-Pro-Leu-OMe
-
irreversible inhibitor
ZED1227
an irreversible peptidomimetic TG2-selective inhibitor
[(2-[[(benzyloxy)carbonyl]amino]-4-[5-(formylamino)-1,2,4-thiadiazol-3-yl]butanoyl)amino]acetic acid
-
-
[(4-[3-(aminocarbonyl)oxiran-2-yl]-2-[[(benzyloxy)carbonyl]amino]butanoyl)amino]acetic acid
-
-
[(5R,8S)-8-{[(benzyloxy)carbonyl]amino}-5-(methoxycarbonyl)-2,7-dioxo-9-phenylnonyl](dimethyl)sulfonium bromide
-
[([3-(aminocarbonyl)oxiran-2-yl][[(benzyloxy)carbonyl]amino]acetyl)amino]acetic acid
-
-
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-ylmethyl]-carbamic acid benzyl ester
-
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-yl]-carbamic acid benzyl ester
-
[2-[(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)amino]-2-oxoethyl](dimethyl)sulfanium
-
-
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](diethyl)sulfanium bromide
-
-
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](dimethyl)sulfanium bromide
-
-
[2-[(4-acryloylaminobenzenesulfonyl)methylamino]ethyl]-methylcarbamic acid benzyl ester
-
[4-(4-acryloylpiperazine-1-sulfonyl)phenyl]carbamic acid benzyl ester
-
[4-[(4-aminophenyl)sulfonyl]piperazin-1-yl](cyclopropyl)methanone
-
[[(4E)-6-amino-2-[[(benzyloxy)carbonyl]amino]-6-oxohex-4-enoyl]amino]acetic acid
-
-
[[(5E)-7-amino-2-[[(benzyloxy)carbonyl]amino]-7-oxohept-5-enoyl]amino]acetic acid
-
-
[[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]amino]acetic acid
-
-
(NH4)2SO4
-
65.58% activity remaining at 10 mM
(NH4)2SO4
Nemipterus sp.
-
-
1-(6-methylpyridin-2-yl)piperazine
-
1-(6-methylpyridin-2-yl)piperazine
-
1-(6-nitropyridin-3-yl)piperazine
-
1-(6-nitropyridin-3-yl)piperazine
-
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00025 mM, standard format, at 0.00018 mM, full progress curve
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
-
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
50% inhibition at 0.00021 mM, standard format, at 0.00014 mM, full progress curve
3-iodo-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
3-iodo-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
-
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
-
4-fluoro-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
4-fluoro-N-[(2S)-1-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
4-fluoro-N-[(2S)-1-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
4-fluoro-N-[(2S)-1-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]benzamide
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mol per mol enzyme, 85% inactivation, not reversed by glutathione
5,5'-dithiobis(2-nitrobenzoic acid)
-
irreversible, carbobenzoxy-Phe protects
5,5'-dithiobis(2-nitrobenzoic acid)
-
reversed by dithiothreitol
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxamide
-
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxamide
-
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylic acid
-
5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylic acid
-
ADP
-
complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
ADP
-
complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
ATP
-
3 mM, complete inhibition of rat liver and human brain tissue-type transglutaminase, reversible; 3 mM, complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
ATP
-
0.5 mM, approx. 60% inhibition of recombinant tranglutaminase
ATP
-
3 mM, complete inhibition of rat liver and human brain tissue-type transglutaminase, reversible; 3 mM, complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
ATP
-
2 mM, 27% inhibition
Ba2+
-
22.55% activity remaining at 10 mM
Ba2+
-
10 mM, complete inhibition
cadaverine
-
complete inhibition at 0.15 mM
cadaverine
-
strong, putrescine as substrate
cadaverine
-
2 mM, 70% inhibition
chlorpromazine
-
reverses calmodulin enzyme stimulation
chlorpromazine
-
reverses calmodulin enzyme stimulation
CTP
-
3 mM, complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
CTP
-
3 mM, complete inhibition of rat liver and human brain transglutaminase, reversible, non-competitive to putrescine
Cu2+
-
-
Cu2+
-
KCN or dithiothreitol restore activity; mechanism
Cu2+
-
19.78% activity remaining at 10 mM
Cu2+
-
strong inactivation
Cu2+
-
10 mM, complete inhibition
Cu2+
-
trace amounts, 0.45 mM diethyldithiocarbamate stimulates crude preparation
Cu2+
-
5 mM CuSO4, 91% inhibition
Cu2+
-
1 mM, complete inhibition
cystamine
-
50% inhibition at 0.022 mM
cystamine
-
transglutaminase inhibitor cystamine alleviates the abnormality in liver from NZB/W F1 mice
cystamine
-
significant reduction in TG2 activity in NZB/W F1 mice following cystamine administration
cystamine
-
2 mM, 58% inhibition
cystamine
-
ameliorates liver fibrosis induced by carbon tetrachloride via inhibition of tissue transglutaminase
Dansylcadaverine
-
0.0019 mM, 50% inhibition
Dansylcadaverine
-
0.0019 mM, 50% inhibition
EDTA
-
-
EDTA
complete inhibition at 10 mM
EDTA
complete inhibition at 10 mM
EDTA
the enzyme is inhibited at 10 mM
EDTA
-
10 mM, complete inhibition
EDTA
complete inhibition at 10 mM
EDTA
-
1 mM, stable in absence of NaCl, inactivation in presence of NaCl
EDTA
-
10 mM, no residual activity
EDTA
-
complete inactivation above 10 mM
EDTA
-
5 mM; 5 mM, complete inhibition
EGTA
-
2.5 mM, 94% inhibition
EGTA
-
42.93% activity remaining at 10 mM
EGTA
-
10 mM, complete inhibition
EGTA
-
2 mM, irreversible
EGTA
-
weak, reversible by Ca2+
EGTA
-
5 mM, 100% inhibition
ERW1041E
-
i.e. (S)-quinolin-3-ylmethyl 2-((((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)carbamoyl)pyrrolidine-1-carboxylate
Fe2+
-
-
GDP
-
inhibits hydrolysis of GTP
GDP
-
inhibits hydrolysis of GTP
GDP
-
at low levels of Ca2+
GTP
-
weak inhibition in the millimolar range
GTP
-
inhibition of tissue transglutaminase
GTP
-
inhibition of tissue transglutaminase
GTP
-
0.1 mM, complete inhibition at suboptimal Ca2+-levels
GTP
-
50% as effective as ATP
GTP
-
0.02-0.1 mM, inhibition of transglutaminases 2 and 3
GTP
-
causes significant shifts in electrophoretic mobility of the protein under native conditions
GTP
the protein transamidase activity of TG2 is positively regulated by calcium and negatively regulated by GTP
GTP
-
inhibition of tissue transglutaminase
GTP
-
0.005 mM, complete inhibition
GTP
-
0.05 mM, 50% inhibition of lens transglutaminase, 0.5 mM, complete inhibition in the presence of 0.5 mM Ca2+, increasing the Ca2+ concentration to 3 mM reverses inhibition
GTP
-
0.5 mM, almost complete inhibition of recombinant transglutaminase in the presence of 0.5 mM Ca2+, no inhibition in the presence of 2 mM Ca2+
GTP
-
inhibition of tissue transglutaminase
GTP
-
50% as effective as ATP
GTP
-
2 mM, 80% inhibition
GTP-gamma-S
-
inhibition of GTP-hydrolysis
GTP-gamma-S
-
inhibition of GTP-hydrolysis
GTP-gamma-S
1 mM, 60% inhibition of transglutaminase activity in presence of 0.5 mM Ca2+, 0.1 mM, 50% inhibition of GTPase activity
Hg2+
-
-
Hg2+
-
5 mM HgCl2, 94% inhibition
iodoacetamide
-
complete inhibition at 50 mM
iodoacetamide
-
10 mM, 62% inhibition in the presence of 10 mM Ca2+
iodoacetamide
-
0.1 mM, pH 6.8, in the presence of Ca2+, complete inhibition, irreversible, incorporation of 1 mol carbamidomethyl/mol enzyme, substrate protects
iodoacetamide
-
0.1 mM, pH 6.8, in the presence of Ca2+, complete inhibition, irreversible, incorporation of 1 mol carbamidomethyl/mol enzyme, substrate protects; mechanism
iodoacetamide
irreversible inhibition
iodoacetamide
-
factor XIIIa; not inhibited in the absence of Ca2+, calmodulin regulated transglutaminases is not inhibited
iodoacetamide
-
factor XIIIa; not inhibited in the absence of Ca2+, calmodulin regulated transglutaminases is not inhibited
iodoacetamide
-
0.1 mM and 1 mM for normal skin and keloid scar, respectively
iodoacetamide
-
1 mM, 89% inhibition of DEAE-absorbed transglutaminase
iodoacetamide
-
86% and 91% inhibition of chondrosarcoma transglutaminase B and C respectively
iodoacetic acid
-
28.75% activity remaining at 10 mM
iodoacetic acid
-
10 mM, complete inhibition
KCC009
-
inhibition of enzyme and subsequent block of fibronectin assembly in the extracellular matrix of glioblastoma cells
KCC009
-
dihydroisoxazole TG2 inhibitor
KCC009
a specific tTG inhibitor
KCC009
-
inhibition of enzyme and subsequent block of fibronectin assembly in the extracellular matrix of glioblastoma cells in vitro and in vivo. KCC009 treatment in mice harboring orthotopic glioblastomas sensitizes the tumors to N,N-bis(2-chloroethyl)-N-nitrosourea chemotherapy
KCl
-
45% activity at 400 mM
LDN-27219
-
reversible, slow-binding inhibitor that appears not to bind at the enzymes active site but rather at the enzymes GTP site, or a site that regulates binding of GTP. The potency and kinetics of inhibition are dependent on substrate structure and suggest a novel mechanism of inhibition that involves differential binding of LDN-27219 to multiple conformational states of this enzyme
methyl 5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylate
-
methyl 5-[4-[N2-(phenylacetyl)-N6-(prop-2-enoyl)-L-lysyl]piperazin-1-yl]pyridine-2-carboxylate
-
methylamine
-
1.8 mM, 50% inhibition
methylamine
-
1.8 mM, 50% inhibition
Mg2+
-
53.52% activity remaining at 10 mM
Mg2+
-
significant inhibition
Mg2+
-
1 mM, complete inhibition
Mn2+
-
30.65% activity remaining at 10 mM
monodansyl cadaverine
MDC
monodansyl cadaverine
-
-
Monodansylcadaverine
-
-
Monodansylcadaverine
treatment of proximal renal tublule cells with inhibitor monodansylcadaverine or siRNA results in decreased proliferation accompanied by activation of signal transducer and activator of transcription, Akt and Stat-3. Treatment with monodansylcadaverine or TGase-1 siRNA decreases Stat-3 but not Akt phosphorylation. TGase-1 interacts with Janus-activated kinase JAK2, and this interaction is inhibited by monodansylcadaverine
Monodansylcadaverine
-
partial inhibition above 0.5 mM
Monodansylcadaverine
-
2 mM, 97% inhibition
Monodansylcadaverine
-
inhibition of glutamyl transfer to putrescine-pectin and putrescine-alginate
monoiodoacetate
-
1 mM, 97% inhibition
monoiodoacetate
-
1 mM, 93% inhibition of DEAE-unabsorbed transglutaminase, 85% inhibition of DEAE-absorbed transglutaminase
monoiodoacetate
-
1 mM, 24% inhibition
monoiodoacetate
-
1 mM, 94% inhibition
N,N-dimethyl-5-(piperazine-1-sulfonyl)naphthalen-1-amine
-
N,N-dimethyl-5-(piperazine-1-sulfonyl)naphthalen-1-amine
-
-
N,N-dimethyl-5-(piperazine-1-sulfonyl)naphthalen-1-amine
-
N-ethylmaleimide
-
3.6 mol per mol enzyme, 91% inhibition in the presence of Ca2+, not inhibited in the absence of Ca2+, substrate protects
N-ethylmaleimide
-
1 mM, 75% inhibition
N-ethylmaleimide
-
0.1 mM, 60% inhibition
N-ethylmaleimide
-
strong inactivation in the presence of Ca2+, not inhibited in the absence of Ca2+
N-ethylmaleimide
-
strong inactivation
N-ethylmaleimide
Nemipterus sp.
-
-
N-ethylmaleimide
-
10 mM, complete inhibition
N-ethylmaleimide
-
1 mM, complete inhibition of DEAE-unabsorbed transglutaminase, 93% inhibition of DEAE-absorbed transglutaminase
N-ethylmaleimide
-
0.1 mM
N-ethylmaleimide
-
irreversible inhibition, inhibition increases with increasing Ca2+ concentrations, 50% inhibition at 1 mM Ca2+
N-ethylmaleimide
-
79% inactivation
N-ethylmaleimide
-
5 mM, strong
N-ethylmaleimide
strong inhibition
N-ethylmaleimide
-
1 mM, 90% inhibition
N-ethylmaleimide
-
1 mM, 98% inhibition
N-[(5S)-5-(2-cyclohexylacetamido)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-(2-cyclohexylacetamido)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(2-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(3-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(3-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-bromophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-bromophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-chlorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-chlorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-fluorophenyl)acetamido]-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-iodophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-iodophenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-methylphenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[2-(4-methylphenyl)acetamido]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)carbamothioyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)carbamothioyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)carbamoyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)carbamoyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)methyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[(4-fluorophenyl)methyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-5-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxohexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-(4-phenylpiperazin-1-yl)hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-(4-phenylpiperazin-1-yl)hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-3-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-3-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-4-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-4-yl)piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-[6-(trifluoromethyl)pyridin-3-yl]piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-[6-(trifluoromethyl)pyridin-3-yl]piperazin-1-yl]hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]-5-(2,2,2-trifluoroacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-oxo-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]-5-(2,2,2-trifluoroacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(3-methylphenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(3-methylphenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-fluorobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-fluorobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-nitrobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-nitrobenzoyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-nitrophenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(4-nitrophenyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-bromopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-bromopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-chloropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-chloropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-chloropyridine-2-carbonyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-chloropyridine-2-carbonyl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-fluoropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
determination of the thermodynamic solubility of the compound
N-[(5S)-6-[4-(6-fluoropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
determination of the thermodynamic solubility of the compound
N-[(5S)-6-[4-(6-fluoropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-fluoropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-iodopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-iodopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
an selective Nepsilon-acryloyllysine derivative, irreversible inhibition
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
reversible inhibitor
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
reversible inhibitor
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamothioyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamothioyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylmethanesulfonyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[(phenylmethanesulfonyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(pyridin-2-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(pyridin-2-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-2-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-2-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-3-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-[2-(thiophen-3-yl)acetamido]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
determination of the thermodynamic solubility of the compound
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
determination of the thermodynamic solubility of the compound
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
reversible inhibitor
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
reversible inhibitor
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-[(phenylcarbamoyl)amino]hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-tert-butylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-tert-butylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[(4-fluorophenyl)methyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[(4-fluorophenyl)methyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
NaCl
-
20% inhibition at 15 mM
NaCl
-
500 mM, 2 h at 20°C in the absence of substrate, 86% inhibition, reversible to some extent by dilution
NaCl
Nemipterus sp.
-
1.2 M, 25% inhibition
NaCl
-
500 mM, 58% inhibition
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
-
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
study on pharmacokinetics, pharmacodynamics, and bioavailability
NH4+
-
5 mM, 36% inhibition
NH4+
-
complete inhibition of coagulating gland transglutaminase with more than 1 mM NH4Cl or 20 mM (NH4)2SO4
p-chloromercuribenzoate
-
reversible by glutathione
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
1 mM, 98% inhibition
p-chloromercuribenzoate
-
strong inactivation
p-chloromercuribenzoate
-
10 mM, complete inhibition
p-chloromercuribenzoate
-
0.1 mM
p-chloromercuribenzoate
-
21% inhibition of chondrosarcoma transglutaminase B
p-chloromercuribenzoate
-
1 mM, 44% inhibition
putrescine
-
-
putrescine
-
pan-transglutaminase inhibition inhibits terminal differentiation of keratinocytes, leading to a hyperproliferative epidermis with parakeratosis and enhanced expression of involucrin and cytokeratins 6 and 16. Expression of the differentiation-associated cytokeratin, cytokeratin 10, is reduced. Basement membrane integrity is also lost as a result of transglutaminase inhibition
putrescine
-
0.1-0.2 mM, substrate inhibition
putrescine
-
2 mM, 75% inhibition
R283
irreversible inhibitor
R283
-
specific inhibitor, i.e. 1,3-dimethyl-2-[(2-oxopropyl)thio]imidazolium chloride, complete inhibition at 0.25 mM
spermidine
-
-
spermidine
-
0.1-0.2 mM, substrate inhibition
spermidine
-
2 mM, 70% inhibition
spermine
-
0.17 mM, 50% inhibition
spermine
-
0.1-0.2 mM, substrate inhibition
spermine
-
0.17 mM, 50% inhibition
spermine
-
2 mM, 68% inhibition
tert-butyl 4-(4-fluorobenzoyl)piperazine-1-carboxylate
-
tert-butyl 4-(4-fluorobenzoyl)piperazine-1-carboxylate
-
tert-butyl 4-(4-nitrobenzoyl)piperazine-1-carboxylate
-
tert-butyl 4-(4-nitrobenzoyl)piperazine-1-carboxylate
-
tert-butyl 4-(6-chloropyridine-2-carbonyl)piperazine-1-carboxylate
-
tert-butyl 4-(6-chloropyridine-2-carbonyl)piperazine-1-carboxylate
-
tert-butyl 4-(6-fluoropyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-fluoropyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-fluoropyridin-3-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-fluoropyridin-3-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-iodopyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-iodopyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-nitropyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-nitropyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-phenylpyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-phenylpyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-tert-butylpyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(6-tert-butylpyridin-2-yl)piperazine-1-carboxylate
-
tert-butyl 4-(pyridin-3-yl)piperazine-1-carboxylate
-
tert-butyl 4-(pyridin-3-yl)piperazine-1-carboxylate
-
tert-butyl 4-[(4-fluorophenyl)methyl]piperazine-1-carboxylate
-
tert-butyl 4-[(4-fluorophenyl)methyl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(methoxycarbonyl)pyridin-3-yl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(methoxycarbonyl)pyridin-3-yl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(trifluoromethyl)pyridin-3-yl]piperazine-1-carboxylate
-
tert-butyl 4-[6-(trifluoromethyl)pyridin-3-yl]piperazine-1-carboxylate
-
Zn2+
-
-
Zn2+
-
20.12% activity remaining at 10 mM
Zn2+
-
10 mM, complete inhibition
Zn2+
-
5 mM ZnSO4, 95% inhibition
Zn2+
-
1 mM, 89% inhibition
ZnCl2
-
5 mM, 97.5% inhibition, 43% inhibition in the presence of 10 mM Ca2+
additional information
-
not inhibited by mono- and dimethylated dansylcadaverine
-
additional information
-
-
-
additional information
-
-
-
additional information
-
rapid degradation of liver tissue transglutaminase in the presence of micro-calpain, GTP-gamma-S inhibits degradation
-
additional information
-
not inhibitory: beta-mercaptoethanol
-
additional information
-
not inhibitory: N-carbobenzyloxy-L-phenylalanine 2-(chloroacetylamido)ethylamide
-
additional information
-
beta-aminoethyl ketones strongly inhibit TGase, alpha- and gamma-aminoalkyl ketones show very weak TGase inhibition
-
additional information
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2, synthesis, structure-activity relationships, and pharmacokinetic profiling, overview. No inhibition by N-[(5R)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
additional information
-
rapid inactivatin of factor XIIIa by trypsin and thrombin in the absence of metal ions
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
transglutaminase 1, not inhibited by GTP
-
additional information
-
inhibitory activity in decreasing order: cystamine, spermidine, spermine, putrescine, cysteamine
-
additional information
peptide harboring Gln mimics, e.g. 6-diazo-5-oxo-L-norleucine, have the potential to show considerably higher specificity for TG2 than the amine inhibitors. Non-hydrolyzable GTP analogs (e.g. 5'-guanylyl imidodiphosphate) are also inhibitors of TG2 activity. Because of the tight coupling between the GTP binding site and the transamidase/deamidase active site of TG2, these ligands act as competitive inhibitors of both the GTPase and transglutaminase activities of this enzyme
-
additional information
-
peptide harboring Gln mimics, e.g. 6-diazo-5-oxo-L-norleucine, have the potential to show considerably higher specificity for TG2 than the amine inhibitors. Non-hydrolyzable GTP analogs (e.g. 5'-guanylyl imidodiphosphate) are also inhibitors of TG2 activity. Because of the tight coupling between the GTP binding site and the transamidase/deamidase active site of TG2, these ligands act as competitive inhibitors of both the GTPase and transglutaminase activities of this enzyme
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
-
poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor; poor inhibition by ZED1227, an irreversible peptidomimetic TG2-selective inhibitor
-
additional information
-
efficient site-specific antibody-drug conjugation by engineering a nature-derived recognition tag for microbial transglutaminase, overview. Synthesis and evaluation of series of targeted covalent inhibitors (TCIs) whose structure is based on a Cbz-Lys scaffold, the irreversible inhibitors block both the transamidation and GTP-binding activities of hTG2, structure-activity relationship (SAR) study and docking study using crystal structure PDB ID 2Q3Z. Isozyme selectivity. No inhibition by benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-3-[(prop-2-enoyl)amino]propan-2-yl]carbamate and benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-4-[(prop-2-enoyl)amino]butan-2-yl]carbamate
-
additional information
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2, synthesis, structure-activity relationships, and pharmacokinetic profiling, overview. No inhibition by N-[(5R)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
additional information
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2, synthesis, structure-activity relationships, and pharmacokinetic profiling, overview. No inhibition by N-[(5R)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
additional information
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2, synthesis, structure-activity relationships, and pharmacokinetic profiling, overview. No inhibition by N-[(5R)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
additional information
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2, synthesis, structure-activity relationships, and pharmacokinetic profiling, overview. No inhibition by N-[(5R)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
additional information
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2, synthesis, structure-activity relationships, and pharmacokinetic profiling, overview. No inhibition by N-[(5R)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
additional information
-
not inhibitory: didansylcadaverine
-
additional information
-
not inhibited by GDP
-
additional information
-
not inhibited by adenosine or adenine
-
additional information
-
not inhibited by mono- and dimethylated dansylcadaverine
-
additional information
-
not inhibited by diisopropylfluorophosphate; not inhibited by PMSF; not inhibited by sulfhydryl-reagents in the absence of Ca2+
-
additional information
-
transglutaminase of coagulating gland, not inhibited by GTP
-
additional information
-
the enzyme is not inhibited by ethylenediaminetetraacetic acid, Na+, K+, Ca2+, Mg2+, Ba2+, Mn2+ and Co2+
-
additional information
the amount of ammonia produced by cross-linking casein with the mutant MTG in the presence of 20% ethanol is less than the control
-
additional information
-
not inhibitory: Ba2+, Ca2+, Co2+, Cu2+, Fe2+, Fe3+, Mg2+, Mn2+, Na+, phenylmethylsulfonyl fluoride, EDTA
-
additional information
-
enzyme precursor protein is inhibitory to mature enzyme, even after heat treatment. Precursor is secreted to culture medium; heat-treated pro-enzyme acts effectively as inhibitor of mature form
-
additional information
isozyme MTG-TX is not inhibited by Li+, Na+, K+, Ca2+, Mg2+, Ba2+, Mn2+, or the inhibitor phenylmethanesulfonyl fluoride (PMSF)
-
additional information
-
not inhibited by Ba2+, Co2+, Fe3+, K+, Mg2+, Mn2+, Na+, Ni2+, Sr2+
-
additional information
-
not inhibited by diisopropylfluorophosphate
-
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0.00041
(3E)-1-benzyl-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.012
(3E)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0004
(3E)-4-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.004
(3E)-4-chloro-1-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0007
(3E)-4-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0033
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.003
(3E)-5-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0009
(3E)-5-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0053
(3E)-6-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.0054
(3E)-6-fluoro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
-
pH and temperature not specified in the publication
0.01
1,1'-methanediylbis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.011
1,1'-[(4,6-dimethylbenzene-1,3-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.00016 - 0.045
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.0071 - 0.11
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.00018 - 0.041
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.0015
2-([3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.00014 - 0.019
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
0.00061 - 0.21
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
1.04
2-Aminophenol
-
pH 8.0, 37°C
0.16
2-Aminothiophenol
-
pH 8.0, 37°C
0.000075
2-Iodoacetamide
-
-
0.006 - 0.5
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
0.00025 - 0.039
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
0.00016 - 0.045
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.0071 - 0.22
2-[[3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.00017 - 0.01
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
0.00018 - 0.041
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.0015 - 0.18
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
0.00014 - 0.019
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
0.0011 - 0.19
2-[[5-benzyl-3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
0.00061 - 0.21
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
1.91
3-Aminophenol
-
pH 8.0, 37°C
0.16
3-aminothiophenol
-
pH 8.0, 37°C
1.09
4-Aminophenol
-
pH 8.0, 37°C
0.63
4-aminothiophenol
-
pH 8.0, 37°C
0.015
5,5'-methanediylbis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.003
5,5'-oxybis(1H-indole-2,3-dione)
-
pH and temperature not specified in the publication
0.00006
Ac-P(6-diazo-5-oxo-L-norleucine)LPF-NH2
-
2.28
alpha-difluoromethylornithine
-
-
0.0011 - 0.09
benzyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
0.11
benzyl [(1R)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(methylamino)-2-oxoethyl]carbamate
-
pH 9.0, 37°C
0.0521
benzyl [(2S)-1-(4-acetylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0366
benzyl [(2S)-1-(4-benzoylpiperazin-1-yl)-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.02
benzyl [(2S)-1-oxo-1-[4-(phenylacetyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0147
benzyl [(2S)-1-oxo-1-[4-(phenylmethanesulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0091
benzyl [(2S)-1-oxo-1-[4-(propane-2-sulfonyl)piperazin-1-yl]-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0401
benzyl [(2S)-1-oxo-6-[(prop-2-enoyl)amino]-1-[4-(thiophene-2-sulfonyl)piperazin-1-yl]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0235
benzyl [(2S)-1-[(2-aminoethyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0305
benzyl [(2S)-1-[(3-aminopropyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0271
benzyl [(2S)-1-[(4-aminobutyl)[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0088
benzyl [(2S)-1-[4-(benzenesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.011
benzyl [(2S)-1-[4-(cyclohexanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.036
benzyl [(2S)-1-[4-(ethanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0064
benzyl [(2S)-1-[4-(methanesulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0089
benzyl [(2S)-1-[4-(naphthalene-1-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0104
benzyl [(2S)-1-[4-(naphthalene-1-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0134
benzyl [(2S)-1-[4-(naphthalene-2-carbonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0067
benzyl [(2S)-1-[4-(naphthalene-2-sulfonyl)piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0477
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-5-[(prop-2-enoyl)amino]pentan-2-yl]carbamate
-
pH 6.5, 25°C
0.0129
benzyl [(2S)-1-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-1-oxo-6-[(prop-2-enoyl)amino]hexan-2-yl]carbamate
-
pH 6.5, 25°C
0.0339
benzyl [(9S)-19-[[5-(dimethylamino)naphthalene-1-sulfonyl]amino]-3,10-dioxo-14,17-dioxa-4,11-diazanonadec-1-en-9-yl]carbamate
-
pH 6.5, 25°C
0.147
beta-mercaptoethanolamine
-
pH 8.0, 37°C
5.14
beta-selenoethanolamine
-
pH 8.0, 37°C
0.28
butanolamine
-
pH 8.0, 37°C
2.2 - 9
ethanolamine
-
pH 8.0, 37°C
0.041
isoindigotin
-
pH and temperature not specified in the publication
0.01
methyl ketone
-
pH and temperature not specified in the publication
0.04
methyl N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycinate
-
pH 6.5, 25°C
0.014
N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycine
-
-
0.009
N-carbobenzyloxy-L-phenylalanine 2-(acrylamido)ethylamide
-
-
0.0045
N-carbobenzyloxy-L-phenylalanine 4-(acrylamido)butylamide
-
-
0.073
N-carbobenzyloxy-L-phenylalanine 4-(chloroacetylamido)butylamide
-
-
0.013
N-carbobenzyloxy-L-phenylalanine 6-(acrylamido)hexylamide
-
-
0.006
N-carbobenzyloxy-L-phenylalanine 6-(chloroacetylamido)hexylamide
-
-
0.0035
N-carbobenzyloxy-L-phenylalanine 8-(acrylamido)octylamide
-
-
0.0013
N-[(2S)-4-[(3-methoxy-1,2,4-thiadiazol-5-yl)amino]-2-[(phenoxycarbonyl)amino]butanoyl]glycine
-
-
0.004
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
0.018
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]tryptophanamide
-
-
0.061
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(2-phenylethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.043
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(naphthalen-2-yloxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.078
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-3-ylmethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.081
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[(pyridin-4-ylmethoxy)carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.079
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-5-hydroxy-L-tryptophanamide
-
pH 9.0, 37°C
0.087
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.11
N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-Nalpha-[[5-(dimethylamino)naphthalen-2-yl]sulfonyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.00573
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
pH 6.5, 30°C, with/versus substrate Z-Glu(HMC)-Gly-OH
0.0011
N-[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]glycine
-
-
0.0013
N-[[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]-5-fluoro-Na-[(quinolin-3-ylmethoxy)carbonyl]-L-tryptophanamide
-
-
0.0481
N2-[(benzyloxy)carbonyl]-N6-(prop-2-enoyl)-L-lysylglycine
-
pH 6.5, 25°C
0.0351
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysinamide
-
pH 6.5, 25°C
0.0603
N2-[(benzyloxy)carbonyl]-N6-prop-2-enoyl-L-lysine
-
pH 6.5, 25°C
0.0023
N5-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-ornithylglycine
-
-
0.0017
N6-(3-methoxy-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-lysylglycine
-
-
0.019
Na-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-5-fluorotryptophanamide
-
-
0.42
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
2.05
propanolamine
-
pH 8.0, 37°C
0.03
quinolin-3-ylmethyl [(1S)-2-([[(5S)-3-bromo-4,5-dihydroisoxazol-5-yl]methyl]amino)-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
0.041
quinolin-3-ylmethyl [(1S)-2-[[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]amino]-1-(4-hydroxybenzyl)-2-oxoethyl]carbamate
-
-
0.0011 - 0.2
tert-butyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
0.0013
tert-butyl N-(3-methyl-1,2,4-thiadiazol-5-yl)-N2-(phenoxycarbonyl)-L-glutaminylglycinate
-
-
0.014
[(2-[[(benzyloxy)carbonyl]amino]-4-[5-(formylamino)-1,2,4-thiadiazol-3-yl]butanoyl)amino]acetic acid
-
-
0.00123
[(4-[3-(aminocarbonyl)oxiran-2-yl]-2-[[(benzyloxy)carbonyl]amino]butanoyl)amino]acetic acid
-
-
0.00056
[([3-(aminocarbonyl)oxiran-2-yl][[(benzyloxy)carbonyl]amino]acetyl)amino]acetic acid
-
-
0.00275
[[(4E)-6-amino-2-[[(benzyloxy)carbonyl]amino]-6-oxohex-4-enoyl]amino]acetic acid
-
-
0.00048
[[(5E)-7-amino-2-[[(benzyloxy)carbonyl]amino]-7-oxohept-5-enoyl]amino]acetic acid
-
-
0.00028
[[(6Z)-8-amino-2-[[(benzyloxy)carbonyl]amino]-8-oxooct-6-enoyl]amino]acetic acid
-
-
additional information
additional information
-
0.00016
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.045
2-([3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.0071
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.11
2-([3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.00018
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.041
2-([3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.00014
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.019
2-([3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.00061
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate N-methylcasein
0.21
2-([3-(3-fluorophenyl)-5-(3-diethylaminopropoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio)acetohydrazide
-
substrate Abeta1-40
0.006
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
-
substrate N-methylcasein
0.006
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.5
2-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00025
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
substrate N-methylcasein
0.00025
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0073
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.039
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
substrate Abeta1-40
0.039
2-[(4-oxo-3-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl)thio]acetohydrazide
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.00016
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0082
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.045
2-[[3-(2-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0071
2-[[3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.11
2-[[3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.22
2-[[3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00017
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
substrate N-methylcasein
0.00017
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.005
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
substrate Abeta1-40
0.005
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.01
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00018
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.01
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.041
2-[[3-(3-fluorophenyl)-4-oxo-5-phenyl-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0015
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.18
2-[[3-(3-fluorophenyl)-4-oxo-6-phenyl-3,4-dihydroquinazolin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00014
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0042
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.019
2-[[3-(3-fluorophenyl)-5-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]thio]acetohydrazide
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0011
2-[[5-benzyl-3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
substrate N-methylcasein
0.0011
2-[[5-benzyl-3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.19
2-[[5-benzyl-3-(3-fluorophenyl)-4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.00061
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.05
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
0.21
2-[[5-[2-[3-(diethylamino)propoxy]phenyl]-3-(3-fluorophenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-2-yl]sulfanyl]acetohydrazide
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.0011
benzyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
substrate N-methylcasein
0.09
benzyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
substrate Abeta1-40
0.004
CP30a
at pH 7.0 and 25°C
0.004
CP30a
0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25°C
0.001
CP4d
at pH 7.0 and 25°C
0.001
CP4d
0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25°C
0.42
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
-
0.42
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
pH 9.0, 37°C
0.019
NC-I052
at pH 7.0 and 25°C
0.019
NC-I052
0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25°C
0.0011
tert-butyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
transpeptidation of N,N-dimethylated casein by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.09
tert-butyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
transpeptidation of Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val by alphaN-Boc-Lys-NH-CH2-CH2-NH-dansyl
0.2
tert-butyl 3-(3-fluorophenyl)-2-[(2-hydrazino-2-oxoethyl)sulfanyl]-4-oxo-3,5,6,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-7(4H)-carboxylate
-
hydrolysis of benzyloxycarbonyl-Pro-Gln-Nle-Phe
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics
-
additional information
additional information
-
inhibition kinetic analysis
-
additional information
additional information
inhibition kinetics, irreversible enzyme inactivation usually results in steady-state rates that are equal to zero independent of inhibitor concentration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000273
(2-tert-butoxy-2-oxoethyl)(dimethyl)sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0007
(2-[[(1R)-3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-1-carboxy-3-oxopropyl]amino]-2-oxoethyl)(dimethyl)sulfanium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0033
(2-[[4-(methoxycarbonyl)benzyl]oxy]-2-oxoethyl)(dimethyl)sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0015
(2-[[6-(methoxycarbonyl)naphthalen-2-yl]methoxy]-2-oxoethyl)(dimethyl)sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.021
(2E)-3-(4-nitrophenyl)-1-(pyridin-3-yl)prop-2-en-1-one
Cavia porcellus
-
pH 7.0, 25
0.0015
(3E)-1-benzyl-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0036
(3E)-3-(2-oxopropylidene)-6-(trifluoromethoxy)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-3-[2-(3-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
(3E)-3-[2-(4-aminophenyl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-3-[2-(5-bromopyridin-3-yl)-2-oxoethylidene]-4-chloro-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.022
(3E)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
(3E)-4-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.001
(3E)-4-chloro-1-(2-methylpropyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
(3E)-4-chloro-1-(cyclohexylmethyl)-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.004
(3E)-4-chloro-1-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0028
(3E)-4-chloro-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(3E)-4-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
(3E)-4-chloro-3-[2-(2-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
(3E)-4-chloro-3-[2-(3-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.001
(3E)-4-chloro-3-[2-(3-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
(3E)-4-chloro-3-[2-(4-chlorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
(3E)-4-chloro-3-[2-(4-methoxyphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-4-chloro-3-[2-(6-methoxypyridin-3-yl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
(3E)-4-chloro-3-[2-oxo-2-(pyridin-2-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(2-phenylethyl)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(3-phenylpropyl)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-(propan-2-yl)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
(3E)-4-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1-phenyl-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
(3E)-4-chloro-3-[2-oxo-2-(pyridin-4-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0048
(3E)-5-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0043
(3E)-5-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.006
(3E)-5-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0063
(3E)-5-methyl-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0079
(3E)-5-nitro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(3E)-6-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
(3E)-6-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.011
(3E)-6-fluoro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0029
(3E)-7-bromo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
(3E)-7-chloro-3-(2-oxopropylidene)-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0073
(3E)-7-chloro-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.018
(4R)-1-[(benzyloxy)carbonyl]-4-hydroxy-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.0069
(5-bromothiophen-2-yl)(4-methyl-1H-pyrazol-1-yl)methanone
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0107
(E)-1-(1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
Cavia cutleri
25°C, pH 7.0
0.0094
(E)-1-(1-(3-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
Cavia cutleri
25°C, pH 7.0
0.0021
(E)-1-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
Cavia cutleri
25°C, pH 7.0
0.011
(E)-1-(1-(cyclohexylmethyl)-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
Cavia cutleri
25°C, pH 7.0
0.0043
(E)-1-(1-benzyl-1H-1,2,3-triazol-4-yl)-3-(4-nitrophenyl)prop-2-en-1-one
Cavia cutleri
25°C, pH 7.0
0.00044 - 0.00107
(naphthalen-2-yl)methyl 4-(N-acryloylglycyl)piperazine-1-carboxylate
0.000029
(naphthalen-2-yl)methyl 4-[N-(bromoacetyl)glycyl]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.018
1,1'-methanediylbis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.25
1,1'-[(2,5-dimethylbenzene-1,4-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
Homo sapiens
-
IC50 above 0.25 mM, pH and temperature not specified in the publication
0.04
1,1'-[(4,6-dimethylbenzene-1,3-diyl)dimethanediyl]bis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.004
1,3-dimethyl-2-[(2-oxopropyl)thio]-1H-imidazol-3-ium
Homo sapiens
-
-
0.00021
1-(1-benzothiophen-2-yl)-3-[benzyl(tert-butyl)amino]propan-1-one
Cavia porcellus
-
pH 7.5
0.000875
1-(ethenylsulfonyl)tricyclo[3.3.1.13,7]decane
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00012
1-(furan-2-yl)-3-[(2-hydroxyethyl)(propan-2-yl)amino]propan-1-one
Cavia porcellus
-
pH 7.5
0.000125
1-(tricyclo[3.3.1.13,7]dec-1-yl)prop-2-en-1-one
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000025
1-ethyl-3-(4-methoxyphenyl)-6-methylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.033
1-[(2E)-3-(4-nitrophenyl)prop-2-enoyl]-3H-[1,2,3]triazolo[4,5-b]pyridin-1-ium-3-olate
Cavia porcellus
-
pH 7.0, 25
0.005
1-[(benzyloxy)carbonyl]-L-prolyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.0009
2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl prop-2-enoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.1
2-([2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl]sulfanyl)-1,3,4,5-tetramethyl-1H-imidazol-3-ium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0000039
2-bromo-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00000875
2-chloro-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethanone
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0055
2-[(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]-N,N-dimethylacetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.028
3-(3-methyl-3H-diaziren-3-yl)-N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]propanamide
Cavia porcellus
-
pH 7.0, 25°C
0.0005 - 0.00058
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
0.000096 - 0.00052
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
0.024
3-[(2E)-3-(3-nitrophenyl)prop-2-enoyl]-1H-benzotriazol-3-ium-1-olate
Cavia porcellus
-
pH 7.0, 25
0.00042
3-[benzyl(ethyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
Cavia porcellus
-
pH 7.5
0.00019
3-[benzyl(propan-2-yl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
Cavia porcellus
-
pH 7.5
0.00023
3-[benzyl(propan-2-yl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
Cavia porcellus
-
pH 7.5
0.00017
3-[benzyl(tert-butyl)amino]-1-(4-nitrophenyl)propan-1-one
Cavia porcellus
-
pH 7.5
0.000081
3-[benzyl(tert-butyl)amino]-1-(5-bromothiophen-2-yl)propan-1-one
Cavia porcellus
-
pH 7.5
0.0001
3-[benzyl(tert-butyl)amino]-1-(5-chlorothiophen-2-yl)propan-1-one
Cavia porcellus
-
pH 7.5
0.00044
3-[benzyl(tert-butyl)amino]-1-(thiophen-2-yl)propan-1-one
Cavia porcellus
-
pH 7.5
0.00036
3-[bis(2-hydroxyethyl)amino]-1-(furan-2-yl)propan-1-one
Cavia porcellus
-
pH 7.5
0.000069
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000026
4-(2-acryloylaminopyrimidine-5-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00035
4-(3-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
4-(4-acryloylamino-2-chlorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00019
4-(4-acryloylamino-2-fluorobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0025
4-(4-acryloylamino-2-methoxybenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00091
4-(4-acryloylamino-2-methylbenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00018
4-(4-acryloylamino-2-trifluoromethylbenzenesulfonyl)-piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.013
4-(4-acryloylamino-3-fluorobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000094
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-chlorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00007
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-methylbenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 2-trifluoromethylbenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00007
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid 3,5-difluorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00012
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000044
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid cyclopentyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid methyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0000821
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-1-ylmethyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00022
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid naphthalen-2-ylmethyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0012
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000046
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 2,3-difluorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000054
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid 4-fluorobenzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000072
4-(4-acryloylaminobenzenesulfonyl)piperazine-1-carboxylicacid ethyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00046
4-(4-acryloylaminobenzenesulfonyl)[1,4]diazepane-1-carboxylicacid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00045
4-(4-acryloylaminobenzenesulfonylamino)piperidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0028
4-(4-but-2-enoylaminobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-(4-cyanobenzenesulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000078
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000097
4-(6-acryloylaminopyridine-3-sulfonyl)piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00038
4-[(4-acryloylaminobenzenesulfonylamino)methyl]-piperidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0014
4-[4-(1-oxobut-2-ynylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-cyanoacetylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-ethoxycarbonylvinyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0023
4-[4-(2-fluoroacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-methylacryloylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-methylbut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(2-oxopropionylamino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0068
4-[4-(3-(E)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00014
4-[4-(3-(Z)-chloroacryloylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(3-cyanomethylureido)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.016
4-[4-(3-diazo-2-oxopropyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.091
4-[4-(3-ethoxycarbonylallyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.01
4-[4-(4,4,4-trifluoro-3-methylbut-2-enoylamino)-benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.01 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.01
4-[4-(4,4,4-trifluorobut-2-enoylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.01 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.004
4-[4-(4-diazo-3-oxobutyl)benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0045
4-[4-(acryloylmethyl-amino)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.028 - 0.08
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
0.08
4-[4-(ethoxycarbonylmethylamino)benzenesulfonyl]-piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.076
4-[4-acryloylamino-3-(isobutylmethylamino)-benzenesulfonyl]piperazine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.03
5,5'-methanediylbis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.025
5,5'-oxybis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
5-(4-acryloylaminobenzenesulfonyl)-2,5-diazabicyclo-[2.2.1]heptane-2-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00014
5-(4-acryloylaminobenzenesulfonyl)hexahydropyrrolo[3,4-c]pyrrole-2-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.03 - 0.04
6,6'-oxybis(1H-indole-2,3-dione)
Homo sapiens
-
pH and temperature not specified in the publication
0.005925
benzyl 4-[3-(acryloylamino)-2-oxopropanoyl]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.001725
benzyl 4-[3-[(ethenylsulfonyl)amino]-2-oxopropanoyl]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000889
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000775
dimethyl[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-ylmethoxy)ethyl]sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00315
dimethyl[2-oxo-2-[2-(tricyclo[3.3.1.13,7]dec-1-yl)ethoxy]ethyl]sulfonium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.016
ethenesulfonic acid (4-bromophenyl)amide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0018
ethyl [(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.025
fluorenylmethyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
Cavia porcellus
-
pH 7.0, 25
0.009
GTP
Homo sapiens
-
-
0.1
indirubin
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.008
isoindigotin
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
methyl 3-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
methyl 4-([(3E)-4-chloro-2-oxo-3-[2-oxo-2-(pyridin-3-yl)ethylidene]-2,3-dihydro-1H-indol-1-yl]methyl)benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.027
methyl 4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]benzoate
Cavia porcellus
-
pH 7.0, 25
0.0063
methyl 4-[(acryloyloxy)methyl]benzoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0000021
methyl 4-[[(bromoacetyl)oxy]methyl]benzoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0021
methyl 6-[(acryloyloxy)methyl]naphthalene-2-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.000015
methyl 6-[[(bromoacetyl)oxy]methyl]naphthalene-2-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00000665
methyl 6-[[(chloroacetyl)oxy]methyl]naphthalene-2-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.011
methyl ketone
Homo sapiens
-
pH and temperature not specified in the publication
0.005
methyl N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucinate bromide
Homo sapiens
-
-
0.08
N-(2-bromophenyl)acrylamide
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0000061
N-(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)prop-2-enamide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.003
N-(3-bromophenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.043
N-(4-bromobenzyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0033
N-(4-bromophenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
N-(4-bromophenyl)propionamide
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.029
N-(4-fluorophenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00013
N-(4-[4-[2-(2-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000054
N-(4-[4-[2-(3-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00006
N-(4-[4-[2-(4-phenoxyphenyl)acetyl]piperazine-1-sulfonyl]-phenyl)acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.11
N-(phenylcarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.3
N-(tert-butoxycarbonyl)-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.043
N-phenylacrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.008
N-[(2-phenylethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.0002
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(6-phenylpyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00034
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-2-yl)piperazin-1-yl]hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00009
N-[(5S)-6-oxo-5-(2-phenylacetamido)-6-[4-(pyridin-3-yl)piperazin-1-yl]hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00022
N-[(5S)-6-[4-(6-bromopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00018
N-[(5S)-6-[4-(6-chloropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00011
N-[(5S)-6-[4-(6-fluoropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00014
N-[(5S)-6-[4-(6-iodopyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00031
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.0001
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00017
N-[(5S)-6-[4-(6-tert-butylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.00039
N-[(5S)-6-[4-[6-(2-fluoroethoxy)pyridin-2-yl]piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
Homo sapiens
pH 6.5, 30°C
0.03
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.02
N-[(benzyloxy)carbonyl]-L-alanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.028
N-[(benzyloxy)carbonyl]-L-alpha-aspartyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.35
N-[(benzyloxy)carbonyl]-L-isoleucyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.003
N-[(benzyloxy)carbonyl]-L-phenylalanyl-5-oxo-6-[(1,3,4,5-tetramethyl-1H-imidazol-3-ium-2-yl)sulfanyl]-L-norleucine
Homo sapiens
-
-
0.02
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(diethylsulfonio)-5-oxo-L-norleucine
Homo sapiens
-
-
0.01
N-[(benzyloxy)carbonyl]-L-phenylalanyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.012
N-[(benzyloxy)carbonyl]-L-tryptophyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.008
N-[(benzyloxy)carbonyl]glycyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.000032
N-[4-(4-cyclopentanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00011
N-[4-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00018
N-[4-(4-phenylpiperazine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000055
N-[4-(4-pyridin-2-ylpiperazine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0057
N-[4-(aminomethyl)benzyl]-3-(5-[[[[(E)-2-phenylethenyl]sulfonyl](pyridin-2-ylmethyl)amino]methyl]-1,2,4-oxadiazol-3-yl)benzamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0013
N-[4-(piperazine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0019
N-[4-(pyrrolidine-1-sulfonyl)phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.005
N-[4-methanesulfonylphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.058
N-[4-methoxyphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00067
N-[4-nitrophenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.026
N-[4-phenoxyphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.045
N-[4-toluyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0038
N-[4-trifluoromethylphenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.028
N-[4-[(1E)-3-oxo-3-(pyridin-3-yl)prop-1-en-1-yl]phenyl]acetamide
Cavia porcellus
-
pH 7.0, 25
0.000034
N-[4-[4-(2-phenylcyclopropanecarbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00019
N-[4-[4-(2-trifluoromethylphenyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000025
N-[4-[4-(3-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00016
N-[4-[4-(3-phenylpropionyl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00038
N-[4-[4-(3-phenylpropyl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000052
N-[4-[4-(3-trifluoromethylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000041
N-[4-[4-(4,4-difluoropiperidine-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00031
N-[4-[4-(4-phenylbutyl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000035
N-[4-[4-(6-methylpyridin-2-yl)piperazine-1-sulfonyl]phenyl]-acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000076
N-[4-[4-(6-trifluoromethylpyridin-3-yl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00001
N-[4-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00002
N-[4-[4-(octahydroisoquinoline-2-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000026
N-[4-[4-(octahydroquinoline-1-carbonyl)piperazine-1-sulfonyl]phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000037
N-[4-[4-(piperidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000057
N-[4-[4-(pyrrolidine-1-carbonyl)piperazine-1-sulfonyl]-phenyl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00018
N-[5-(4-cyclopropanecarbonylpiperazine-1-sulfonyl)-pyridin-2-yl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000015
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyridin-2-yl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000014
N-[5-[4-(adamantane-1-carbonyl)piperazine-1-sulfonyl]-pyrimidin-2-yl]acrylamide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.15
N2-[(benzyloxy)carbonyl]-L-lysyl-6-(dimethylsulfonio)-5-oxo-L-norleucine bromide
Homo sapiens
-
-
0.03
pyrrolidine-1-carboxylic acid (4-acryloylaminophenyl)-amide
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.65
SQAETYR
Streptomyces mobaraensis
-
in 250 mM Tris acetate buffer (pH 8.0), at 37°C
0.75
SYAETYR
Streptomyces mobaraensis
-
in 250 mM Tris acetate buffer (pH 8.0), at 37°C
0.018
tert-butyl [4-[(1E)-3-(1H-benzotriazol-1-yl)-3-oxoprop-1-en-1-yl]phenyl]carbamate
Cavia porcellus
-
pH 7.0, 25
0.00000629
tricyclo[3.3.1.13,7]dec-1-ylmethyl bromoacetate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.001625
tricyclo[3.3.1.13,7]dec-1-ylmethyl prop-2-enoate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00021
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-ylmethyl]-carbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00022
[1-(4-acryloylaminobenzenesulfonyl)piperidin-4-yl]-carbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00038
[2-[(2-[4-[5-(dimethylamino)naphthalene-1-sulfonyl]piperazin-1-yl]-2-oxoethyl)amino]-2-oxoethyl](dimethyl)sulfanium
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00185
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](diethyl)sulfanium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0014
[2-[(3-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-2,3-dioxopropyl)amino]-2-oxoethyl](dimethyl)sulfanium bromide
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0015
[2-[(4-acryloylaminobenzenesulfonyl)methylamino]ethyl]-methylcarbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.0029
[4-(4-acryloylpiperazine-1-sulfonyl)phenyl]carbamic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
[4-[(4-aminophenyl)sulfonyl]piperazin-1-yl](cyclopropyl)methanone
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00044
(naphthalen-2-yl)methyl 4-(N-acryloylglycyl)piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.00107
(naphthalen-2-yl)methyl 4-(N-acryloylglycyl)piperazine-1-carboxylate
Homo sapiens
-
at pH 7.1, temperature not specified in the publication
0.0005
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00058
3-(4-acryloylaminobenzenesulfonylamino)-(R)-pyrrolidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.000096
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.00052
3-(4-acryloylaminobenzenesulfonylamino)-(S)-pyrrolidine-1-carboxylic acid benzyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.028
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
0.08
4-[4-(cyanomethylcarbamoyl)benzenesulfonyl]piperazine-1-carboxylic acid tert-butyl ester
Homo sapiens
IC50 above 0.08 mM, in 25 mM HEPES, pH 7.4, 250 mM NaCl, 2 mM MgCl2, 10 mM CaCl2, 0.2 mM dithiothreitol, and 0.05% (v/v) Pluronic F-127 at 37°C
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evolution
as a member of the transglutaminase family, transglutaminase 2 (TG2) can catalyze deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. Redox regulation unique to TG2 and evolved relatively recently, TG2 homologues in other vertebrates appear to lack this structure feature
evolution
crayfish TGase is adapted to have significant activity at low temperatures since crayfish are living in quite cold waters
evolution
transglutaminase 2 (TG2) is a ubiquitously expressed multifunctional member of the transglutaminase enzyme family
evolution
transglutaminase is an enzyme family responsible for post-translational modification such as protein cross-linking and the attachment of primary amine and/or deamidation of glutamine-residue in proteins. The medaka orthologue of human tissue-type transglutaminase (OlTGT), identified in the established model fish, has similar functions compared to mammalian enzyme
malfunction
-
transglutaminase 2 (TG2) mutations are associated with diabetes type 2. Lack of TG2 reduces glucose-stimulated insulin secretion from the pancreatic islets
malfunction
enzyme inactivation significantly reduces the virulence of Streptococcus suis serotype 2 in a pig infection model and impairs its antiphagocytosis in human blood
malfunction
double-TG1/TG2 knockout mice show epidermal features similar to TG1 knockout mice. Double-FXIII-A/TG2 knockout mice exhibit only a transient delay in bone mineral density and growth relative to wild-type mice
malfunction
effective inhibition of renal interstitial fibrosis by TG inhibitors but only partial reduction of fibrosis in TG2 knockout mice
malfunction
failure in the regulation of TG2 activities is associated with many human diseases, including inflammatory disease, celiac disease, neurodegenerative disease, diabetes, tissue fibrosis, and cancers. Comparison of wild-type with G224V mutant enzyme structrue and actives sites, overview. Since the active site cysteine (C277)-containing alpha-helix, whose location may be important for TG2 activity, is interacted with a neighboring intramolecular alpha-helix, which contains residue 224, replacement of G with V will have an effect on the transamidase activity of TG2. Decreased activity of G224 may be due to the higher chance of location shift on active site cysteine (C277) because of the loss of the hydrophobic cluster anchored by V224
malfunction
loss of TG1 and TG5 cross linking leads to defects in epidermal cornification in lamellar ichthyosis and acral peeling skin syndrome, respectively. Homozygous missense mutations in the gene encoding TG5 are found to correlate with acral peeling skin syndrome, which is characterized by continual shedding of the outer epidermis of the dorsa of the hands and feet from birth and throughout life
malfunction
loss of TG1 and TG5 cross linking leads to defects in epidermal cornification in lamellar ichthyosis and acral peeling skin syndrome, respectively. Lamellar ichthyosis is apparent at birth, with newborns encased in a shiny, waxy layer of skin (collodion babies) that sheds to reveal scaling and shedding of the outer epidermis and a severely compromised skin barrier. It is an autosomal-recessive disease, with mutations in the gene encoding TG1 accounting for about 90% of cases. Lamellar ichthyosis is an orphan disease. TG1 and TG2 are the most abundantly expressed TGs in normal kidney, and renal disease progression correlates with increases in activity of intracellular TG1 in renal tubular epithelium and of TG2 in the extracellular matrix
malfunction
loss of TG3 crosslinking in hair-cuticle formation leads to uncombable hair syndrome. A homozygous nonsense mutation of TG3 correlates with uncombable hair syndrome and the absence of TG3-mediated crosslinks between trichohyalin and keratin intermediate filaments
malfunction
loss of TG6 crosslinking leads to spinocerebellar ataxia-35
malfunction
loss of the structural erythrocyte membrane protein, protein 4.2, leads to hereditary spherocytosis type 5 associated with abnormally shaped, osmotically fragile erythrocytes
malfunction
specific tTG inhibitors, such as KCC009, can block alpha-synuclein aggregation in SH-SY5Y neuroblastoma cells
malfunction
TG1 and TG2 are the most abundantly expressed TGs in normal kidney, and renal disease progression correlates with increases in activity of intracellular TG1 in renal tubular epithelium and of TG2 in the extracellular matrix. Yet no diseases have been correlated with TG2 deficiency. TG2 deletion does not improve motor, cognitive, molecular, histologic, or lifespan phenotypes and is thus not an important factor in Huntington's disease pathology
malfunction
TG1 knockout mice show defective epidermal maturation late in embryonic development, resulting in a drastic increase in skin permeability, but unlike human patients, TG1 knockout mice die from dehydration within a few hours of birth. Double-TG1/TG2 knockout mice show epidermal features similar to TG1 knockout mice
malfunction
the removal of the pro-sequence region using proteases results in the active site of the mature enzyme to be revealed to initiate the reaction
malfunction
transglutaminase (TG) inhibitors are capable of blocking the entire osteoclastogenesis process. The most potent of the inhibitors, NC9 when added to cultures at different phases of osteoclastogenesis, inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect of NC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected
malfunction
transglutaminase (TG) inhibitors are capable of blocking the entire osteoclastogenesis process. The most potent of the inhibitors, NC9 when added to cultures at different phases of osteoclastogenesis, inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect ofNC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected
metabolism
-
the enzyme activates PI3-kinase
metabolism
in general, TG-catalyzed crosslinking is the primary mechanism by which TGs promote disease progression
metabolism
regulation of human TG2, overview. Redox regulation unique to this isozyme
metabolism
transglutaminase 2 (TG2) is a ubiquitously expressed multifunctional member of the transglutaminase enzyme family. It is implicated to have roles in many physiological and pathological processes such as differentiation, apoptosis, signal transduction, adhesion and migration, wound healing and inflammation. TG2 has various intra- and extra-cellular interacting partners, which contribute to these processes. The molecular co-chaperone, DNAJA1, is an interacting partner of human isozyme TG2. DNAJA1 and TG2 are reported to regulate common pathological conditions such as neurodegenerative disorders and cancer
physiological function
complete knock-down by RNAi results in changed cell morphology, and cells start to spread intensely. After addition of astakine, a cytokine involved in hematopoiesis, cells start to spread and adopt a morphology similar to that observed after RNAi of TGase. Astakine has no effect on TGase expression, but after a prolonged incubation for one week, TGase activity inside and outside the cells is completely lost
physiological function
-
hypoxia induces TG2 expression through an HIF-1 dependent pathway and concurrently activates intracellular TG2. The hypoxiccells overexpressing TG2 show resistance to apoptosis. Hypoxic cells treated with either TG2 inhibitor or small interfering RNA become sensitive to apoptosis. Activation of TG2 in response to hypoxic stress inhibits caspase-3 activity by forming crosslinked multimer, resulting in insoluble aggregates. TG2 also activates nuclear factor kappaB pathway after hypoxic stress, and thereby induces the expression of cellular inhibitor of apoptosis 2
physiological function
-
inhibition of TGase activity with monodansylcadervine, or knockdown of TGase-1 with small interference RNA enhances apoptosis and decreased cell survival in hydrogen peroxide-treated renal proximal tubule cells. Overexpression of TGase-1 renders renal proximal tubule cells more resistant to hydrogen peroxide toxicity and monodansylcadaverine treatment blocks this response. Concurrent with renal proximal tubule cells apoptosis, phosphorylation of AKT, signal transducer and activator of transcription-3, and glucogen synthase kinase-3 are observed. Pretreatment of cells with monodansylcadervine or TGase-1 siRNA inhibits phosphorylation of all these molecules
physiological function
presence of bacterial lipopolysaccharide increases the level of TG2 on the surface of maturing dendritic cells
physiological function
-
TG2 binds to the Rac-binding pocket in the GTPase-activating domains of regulator proteins Bcr and Abr, blocks Bcr activity and, through this mechanism, increases levels of active GTP-bound Rac and EGF-stimulated membraneruffling. Bcr exhibits preferential binding to the non-compacted conformation of TG2, in which its catalytic domain is exposed, but transamidation is not needed for the interaction
physiological function
-
TG2 regulates the expression and function of matrix metalloproteinase MMP-2. TG2 knockdown down-regulates MMP-2 protein and mRNA expression in SKOV-3, IGROV-1, MDA-MB-436, and PC-3 cancer cells. TG2 knockdown or inhibition of TG2 activity using KCC009 decreases MMP-2 gelatinase activity in cancer cells. MMP-2 expression and function are regulated by TG2 at transcriptional level. Binding of CREB to the MMP-2 promoter is diminished in cells that express decreased TG2 levels. TG2 knockdown decreases CREB phosphorylation, and CREB knockdown decreases MMP-2 expression. The effect of TG2 on CREB activity and MMP-2 transcription is mediated by TG2-dependent degradation of protein phosphatase PP2A-alpha. PP2A-alpha complexes with and is targeted for degradation by TG2
physiological function
-
TGase 2 has a role as a biological glue to consolidate various micro-structural components of tissues and biomaterials
physiological function
treatment of proximal renal tublule cells with inhibitor monodansylcadaverine or siRNA results in decreased proliferation accompanied by activation of signal transducer and activator of transcription, Akt and Stat-3. Treatment with monodansylcadaverine or TGase-1 siRNA decreases Stat-3 but not Akt phosphorylation. Janus-activated kinase JAK2 mediates phosphorylation of Stat-3, and knockdown of either JAK2 or Stat-3 by siRNA decreases cell proliferation. Inhibition of TGase-1 decreases phosphorylation of Stat-3 but not JAK2. JAK2 is indispensable for TGase-1 to induce Stat-3 phosphorylation and TGase-1 potentiates JAK2-induced Stat-3 phosphorylation. Inhibition of TGase-1 and the JAK2-Stat-3 signaling pathway decreases the transcriptional activity of Stat-3 and expression of the Stat-3-targeted genes, cyclin D1 and cyclin E. TGase-1 interacts with JAK2, and this interaction is inhibited by monodansylcadaverine
physiological function
-
phosphorylation of transglutaminase 2 at Ser216 plays a role in transglutaminase 2-mediated activation of nuclear factor-kappaB, Akt and in the downregulation of phosphatase and tensin homologue deleted on chromosome 10
physiological function
-
phosphorylation of transglutaminase 2 at Ser216 plays a role in transglutaminase 2-mediated activation of nuclear factor-kappaB, Akt and in the downregulation of phosphatase and tensin homologue deleted on chromosome 10
physiological function
-
the enzyme is involved in the apical growth of apple pollen tube
physiological function
-
the enzyme reduces the pore diameter and inhibits the activity of transient receptor potential vanilloid 5 in an N-glycosylation-dependent manner
physiological function
-
tissue transglutaminase activity protects from cutaneous melanoma metastatic dissemination. The number of melanoma lung foci is more markedly reduced by enzyme overexpression than the metastatic size
physiological function
-
tissue transglutaminase activity protects from cutaneous melanoma metastatic dissemination. The number of melanoma lung foci is more markedly reduced by enzyme overexpression than the metastatic size
physiological function
major and functional transglutaminas of Macrobrachium rosenbergii for haemolymph coagulation and also in spread of infection
physiological function
-
the enzyme has an intrinsic capability to promote cell survival and contributes to oncogenesis
physiological function
the enzyme is a virulence factor in Streptococcus suis serotype 2 with antiphagocytic activity
physiological function
-
the enzyme is associated with amyloid-beta deposits and lesion-associated astrocytes in Alzheimer's disease
physiological function
-
transglutaminase 2 is involved in homocysteine-induced activation of human THP-1 monocytes
physiological function
DNAJA1 interacts with the open form of TG2 and regulates its transamidation activity under both in vitro and in situ conditions. DNAJA1 and TG2 are reported to regulate common pathological conditions such as neurodegenerative disorders and cancer, molecular mechanisms, overview
physiological function
enzyme transglutaminase 2 (TG2) catalyzes deamidation or alternatively transamidation of selected Gln residues in proteins and peptides. As TG2 is natively inactive, TRX is able to reduce the vicinal disulfide bond between C370-C371 to activate TG2, and ERp57 can oxidize the disulfide between C230 and C370 to catalytically inactivate the enzyme. Redox regulation of human TG2, overview. The 220 kDa fibronectin monomer harbors multiple Gln residues susceptible to TG2 modification, including sites within its N-terminal collagen/fibrinbinding domain, its central (RGD-containing) integrin-binding domain, and its C-terminal glycosaminoglycan-binding domain. In addition, its N-terminal domain also harbors a high-affinity non-covalent docking site for TG2. Remarkably, the biogenic amine serotonin can serve as an effective nucleophile in TG2-catalyzed modification of fibronectin; this post-translational modification of fibronectin appears to be a biomarker of pulmonary hypertension in humans as well as cellular and animal models of the disease. Like fibronectin, a number of other proteins comprising the extracellular matrix have been shown to harbor TG2-reactive sites. Amongst these, TG2-catalyzed crosslinking of the amino-propeptide of type III collagen onto the mature collagen fibril and the oligomerization of osteonectin in the matrix of differentiating cartilage represent especially intriguing examples, notwithstanding very limited insight into their biological relevance. TG2 catalyzes an early step in the activation of transforming growth factor-beta (TGF-beta) by crosslinking latent TGF-beta binding protein (LTBP) to the extracellular matrix. Two classes of non-physiological substrates of TG2 warrant attention. The first includes peptides derived from dietary gluten
physiological function
essential role for membrane-bound TG1 in cornified envelope assembly
physiological function
-
human tissue transglutaminase (hTG2) is a multifunctional enzyme. It is primarily known for its calcium-dependent transamidation activity that leads to formation of an isopeptide bond between glutamine and lysine residues found on the surface of proteins, but it is also a GTP binding protein. hTG2 function is tightly regulated by the presence of specific allosteric and redox regulators. Enzyme hTG2 is allosterically modulated by calcium ions and redox proteins to primarily exist in an open or extended conformation that is catalytically active when specific disulfide bonds are reduced. Intracellularly, hTG2 is regulated by guanidine-containing nucleotides, such as GTP that bind hTG2 at a site remote from the catalytic active site. The enzyme is implicated in several disease processes
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. Essential role for membrane-bound TG1 in cornified envelope assembly. TG1 may contribute to intracellular crosslinking processes. Intracellular TG1 activity is unlikely to contribute extracellularly to extracellular matrix crosslinking
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. TG3 is an autoantigen, causing autoantibody production, in dermatitis herpetiformis
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. TG4 is an autoantigen, causing autoantibody production, in autoimmume polyglandular syndrome type 1. Role of TG4 in cancer
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. TG5 is not an autoantigen and does not cause autoantibody production. Role for the cytoplasmic TG5 in epidermal cornification
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. TG6 is an autoantigen, causing autoantibody production, in gluten axonal neuropathy and gluten ataxia
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. TG7 is not an autoantigen and does not cause autoantibody production
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. The enzymatic activity of TG2 is involved in the exacerbation of celiac disease. TG2 has been identified as the principal autoantigen recognized by disease-specific autoantibodies in the serum of patientswith active celiac disease. And TGS is involved in at least one case of hemoglobinopathy, characterized by shortened erythrocyte lifespan. TG2-mediated formation of crosslinked supramolecular membrane proteins and the resultant stiffening of the erythrocyte membrane by these polymers contribute to the extra-rapid clearing of erythrocytes from the circulation and hence, the shortened lifespan of Hb-Koeln erythrocytes, from 120 to 31 days. TG2 might contribute to neurologic diseases by affecting transcription, cellular differentiation, or cell migration and adhesion. TG2 is implicated in Huntington's disease pathogenesis. TG2 is implicated in extracellular collagen crosslinking. TG2 has been reported to enhance cancer cellmotility through induction of epithelial-to-mesenchymal transition, and TG2 enzymatic activity has been reported to be required for the development and survival of cancer stem cells. TG2 is an autoantigen, causing autoantibody production, in celiac disease
physiological function
in humans, 9 members of the transglutaminase (TG) family have been identified, of which eight (factor XIII (FXIII) A and TG1-TG7) catalyze posttranslational protein-modifying reactions, and one (protein 4.2) does not. The TG enzymatic activities considered for human disease include deamidation of glutamine (Gln) residues, amine incorporation into Gln residues, and protein crosslinking. The noncatalytic structural role of protein 4.2 is clearly important for erythrocyte membrane integrity
physiological function
mammalian transglutaminases (TGs) catalyze irreversible posttranslational modifications of proteins, the most prominent of which is the calcium-dependent formation of covalent acyl transfers between the gamma-carboxamide group of glutamine and the epsilon-amino-group of lysine (GGEL-linkage)
physiological function
mammalian transglutaminases (TGs) catalyze irreversible posttranslational modifications of proteins, the most prominent of which is the calcium-dependent formation of covalent acyl transfers between the gamma-carboxamide group of glutamine and the epsilon-amino-group of lysine (GGEL-linkage)
physiological function
microbial transglutaminase (mTG) is a robust enzyme catalyzing the formation of an isopeptide bond between glutamine and lysine residues. Transglutaminase catalyzes the acyl transfer reaction between gamma-carboxyamide groups (acyl donor) and primary amines (acyl acceptor). In proteins, it is able to crosslink the gamma-carboxyamide of glutamine and the primary epsilon-amine in lysine
physiological function
microbial transglutaminase alters the immunogenic potential and cross-reactivity of horse and cow milk proteins. The effect of TG on immunoreactivity depends on enzyme quantity and milk protein type. Determination of immunoreactivity of milk proteins by competitive ELISA
physiological function
-
serotonin (5-hydroxytryptamine, 5-HT) is a key player in many physiological processes in both the adult organism and developing embryo. One of the mechanisms for 5-HT-mediated effects is covalent binding of 5-HT to the target proteins catalyzed by transglutaminases (serotonylation). In some cases, protein serotonylation (or generally monoaminylation) may lead to the formation of an active or inactive molecule that remains stable until its proteolytic degradation
physiological function
serotonin (5-hydroxytryptamine, 5-HT) is a key player in many physiological processes in both the adult organism and developing embryo. One of the mechanisms for 5-HT-mediated effects is covalent binding of 5-HT to the target proteins catalyzed by transglutaminases (serotonylation). In some cases, protein serotonylation (or generally monoaminylation) may lead to the formation of an active or inactive molecule that remains stable until its proteolytic degradation
physiological function
-
serotonin (5-hydroxytryptamine, 5-HT) is a key player in many physiological processes in both the adult organism and developing embryo. One of the mechanisms for 5-HT-mediated effects is covalent binding of 5-HT to the target proteins catalyzed by transglutaminases (serotonylation). In some cases, protein serotonylation (or generally monoaminylation) may lead to the formation of an active or inactive molecule that remains stable until its proteolytic degradation
physiological function
TG2 is involved in extracellular collagen crosslinking
physiological function
the Ca2+-dependent deamidation and transamidation activities of transglutaminase 2 are important to numerous physiological and pathological processes
physiological function
tissue transglutaminase (t-TG) is a multifunctional protein involved in the healing of gastric erosions and ulcers in animal models. Determination of increased gastric t-TG activity in patients with dyspepsia according to Helicobacter pylori infection and cytotoxin-associated gene A (cagA) and vacuolating cytotoxin (vacA) subtype status. t-TG activity is significantly greater in gastritis associated with Helicobacter pylori infection, suggesting that this enzyme is induced by inflammation and may have an important role in the natural history of human gastritis. Tissue-TG is expressed at sites of inflammation, and can act as a modulator of inflammation, exerting both pro- and anti-inflammatory effects. The enzyme covalently cross-links a variety of proteins in the extracellular matrix, increasing fibrosis in order to favor wound healing by increasing resistance to chemical, enzymatic, and physical disruption
physiological function
tissue transglutaminase (TG2) catalyzes the Ca2+-dependent cross-linking of peptides and proteins via the formation of gamma-glutamyl-epsilon-lysyl isopeptide bonds
physiological function
transglutaminase (TG) activity regulates differentiation, migration, and fusion of osteoclasts via affecting actin dynamics. TG activity regulates actin dynamics in pre-osteoclasts. Increased osteoclast activity is responsible for bone destruction in diseases such as osteoporosis, periodontitis and rheumatoid arthritis. Analysis of the role of TG activity in osteoclastogenesis in vitro, overview. TG activity is required for pre-osteoclast migration
physiological function
-
transglutaminase (TGase) catalyzes post-translational modification of proteins by gamma-glutamyl-epsilon-lysine chain links, covalent conjugation of polyamines, and deamidation. Analysis of cross-linking effect of recombinant TGZ on the properties of acid-induced milk protein concentrate (MPC) gel
physiological function
transglutaminase (TGase) catalyzes protein cross-linking reactions essential for several biological processes. In differentiating keratinocytes, TG1 (keratinocyte-type) is crucial for the cross-linking of substrate proteins required for the complete formation of the cornified envelope, a proteinaceous supermolecule located in the outermost layer of the epidermis
physiological function
transglutaminase 2 (TG2) is a multi-functional protein that possesses various biological activities, including protein cross-linking activity, GTPase activity, protein disulfide isomerase activity, kinase activity, and scaffold activity. Because of its various functions, TG2 is involved in many important cellular processes, including apoptosis, angiogenesis, wound healing, neuronal regeneration, and bone development. Isozyme TG2 function differs according to its location in the cell. In the cytosol, TG2 acts as a signal transfer molecule that transmits a receptor signal to an intracellular effector through GTP hydrolysis. When it is secreted into the extracellular environment, TG2 functions as a cross-linking enzyme in the matrix. This protein transamidase activity of TG2 is positively regulated by calcium and negatively regulated by GTP
physiological function
transglutaminase 2 (TGase 2)-catalyzed transamidation represents an important post-translational mechanism for protein modification with implications in physiological and pathophysiological conditions, including fibrotic and neoplastic processes
physiological function
transglutaminase 2 (TGase 2)-catalyzed transamidation represents an important post-translational mechanism for protein modification with implications in physiological and pathophysiological conditions, including fibrotic and neoplastic processes
physiological function
-
transglutaminase is a transferase that catalyzes the acyl transfer reaction between the gamma-carboxamide group in glutamine residues and various primary amines in polyamine
physiological function
-
transglutaminases (TGase) catalyze the acyl transfer reaction between a free amine group (e.g. in a protein or peptide-bound lysine or an amine) and the gamma-carboxy amide group of proteins or peptide bound glutamine thus leading to the modification of proteins. When an epsilon-amino group of a peptide bound lysine acts as a acyl acceptor, isopeptide bond is formed between the glutamine and lysine residues in them, introducing both inter- and intramolecular covalent cross-links, resulting in the polymerization of the proteins
physiological function
transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl) lysine bonds between appropriate substrates. This reaction is essential for physiological cell functions, such as in blood coagulation, during cell differentiation and survival, skin formation, and signal transduction
physiological function
transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl) lysine bonds between appropriate substrates. This reaction is essential for physiological cell functions, such as in blood coagulation, during cell differentiation and survival, skin formation, and signal transduction
physiological function
transglutaminases form extensively crosslinked, generally insoluble protein polymers. These structures are important for organisms in the formation of skin barrier, hair growth, wound healing and blood clotting. Transglutaminases are a family of enzymes that catalyse the cross-linking of proteins by forming covalent bonds between glutamine (Q) and lysine (K) residues in different polypeptides. Such isopeptide bonds created by TG are highly resistant to proteolysis and increase the mechanical stability of the modified proteins
physiological function
type 2 transglutaminase, tTG, is an important player in numerous diseases, including celiac disease, neuronal degenerative diseases, and cancer, and its roles in these diseases often depend as much upon its conformation as its catalytic activity. Several roles of tTG in diseases, detailed overview. ApoE is able to protect against Abeta plaque formation by transporting Abeta out of the brain. Crosslinking by tTG inactivates the protein, rendering it unable to clear Abeta. Parkinson's disease is a related disorder, and tTG plays similar, but unique, roles in this disease as well. Where Alzheimer's disease is driven in part by a buildup of Abeta aggregates, Parkinson's disease is caused by the aggregation of alpha-synuclein. In Parkinson's disease, alpha-synuclein is incorrectly processed into beta-pleated fibrils, which in turn aggregate to form cytoplasmic inclusions called Lewy Bodies. tTG catalyzes the crosslinking of alpha-synuclein, both in vitro and in cell models, tTG and alpha-synuclein both localize to the endoplasmic reticulum in disease brain samples. tTG is the major autoantigen in celiac disease. Celiac disease is an auto-immune disorder in which T-cells attack and damage the small intestine. This process is driven by gliadin, a protein in most grains, which precipitates an immune response. Crosslinking of gliadin formed antigenic complexes. And thioredoxin-1 is released by macrophages exposed to inflammatory stimuli in sufficient quantity to reduce the tTG C370-C371 disulfide bond, activating the enzyme. Since inflammatory conditions are present in celiac disease gut, this effect essentially creates a self-stimulating loop in which activated tTG leads to inflammation, which then activates more tTG. tTG has been shown to play roles in cancer cell adhesion, migration, and invasion via its interactions with fibronectin. tTG binds to fibronectin, and crosslinks it to various surfaces, allowing cells to adhere. Matrix metalloproteinase can then break these crosslinks, and in combination with tTG crosslinking this allows for cell motility. Similarly, tTG is thought to play a role in vesicle trafficking by helping to dock extracellular vesicles (microvesicles) generated by aggressive cancer cells to fibroblasts, through its ability to bind and crosslink fibronectin on the vesicle surface. This docking event can then be blocked by inhibiting its crosslinking activity. tTG can promote either cell survival or apoptosis, depending upon the physiological context. As a pro-survival protein, the crosslinking-competent, open-state form of tTG has been shown to crosslink pRB (a pro-apoptotic protein), causing it to oligomerize and thus lose its activity. This is analogous to its role in Alzheimer's disease, crosslinking ApoE. Closed-state tTG is able to sequester c-Cbl, and block ubiquitinylation and subsequent degradation of the EGF receptor, thereby also promoting cell growth and survival. Thus, both open- and closed-state can tTG promote survival depending upon the specific conditions. The same is true of its pro-apoptotic functions. In pancreatic cancer cells treated with the calcium ionophore A23187, tTG adopts the crosslinking-active open-state to facilitate release of the apoptosis-inducing factor from mitochondria, promoting cell death. In contrast, ectopically expressed tTG in SH-SY5Y cells, which presumably exists in the closed-state, is found to promote apoptosis following osmotic shock or staurosporine treatment. Cytotoxicity of the open-state of tTG
physiological function
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mammalian transglutaminases (TGs) catalyze irreversible posttranslational modifications of proteins, the most prominent of which is the calcium-dependent formation of covalent acyl transfers between the gamma-carboxamide group of glutamine and the epsilon-amino-group of lysine (GGEL-linkage)
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physiological function
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mammalian transglutaminases (TGs) catalyze irreversible posttranslational modifications of proteins, the most prominent of which is the calcium-dependent formation of covalent acyl transfers between the gamma-carboxamide group of glutamine and the epsilon-amino-group of lysine (GGEL-linkage)
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additional information
active-site titration using N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide and Z-Glu(HMC)-Gly-OH
additional information
active-site titration using N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide and Z-Glu(HMC)-Gly-OH
additional information
active-site titration using N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide and Z-Glu(HMC)-Gly-OH
additional information
active-site titration using N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide and Z-Glu(HMC)-Gly-OH
additional information
active-site titration using N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide and Z-Glu(HMC)-Gly-OH
additional information
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addition of TGase at 0.1 U/mg increases the gel strength, setting temperature, setting time, and melting temperature of cold-set gelatin gel
additional information
comparison of the crayfish enzyme to the commercial enzyme from guinea pig liver, which is highly active at 37°C
additional information
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comparison of the crayfish enzyme to the commercial enzyme from guinea pig liver, which is highly active at 37°C
additional information
comparison of the crayfish enzyme, which is highly active at 4°C, to the commercial enzyme from guinea pig liver
additional information
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comparison of the crayfish enzyme, which is highly active at 4°C, to the commercial enzyme from guinea pig liver
additional information
comparison of the different TGases from Streptomyces mobaranensis and Streptomyces cinnamoneus, and of a chimeric mutant constructed from both, overview
additional information
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comparison of the different TGases from Streptomyces mobaranensis and Streptomyces cinnamoneus, and of a chimeric mutant constructed from both, overview
additional information
comparison of the different TGases from Streptomyces mobaranensis and Streptomyces cinnamoneus, and of a chimeric mutant constructed from both, overview
additional information
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comparison of the different TGases from Streptomyces mobaranensis and Streptomyces cinnamoneus, and of a chimeric mutant constructed from both, overview
additional information
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comparison of the recombinantly expressed enzyme TGZo from Zea mays with the microbial transglutaminase(MTG) enzymes from Streptomyces mobaraensis and Streptomyces hygroscopicus. TGZo has higher thermostability and wider range of pH than the MTGs from the Streptomyces strains. Texture analysis of cow milk yogurts cross-linked by different concentrations of TGZo and MTG
additional information
docking study and homology structure molecular modeling using the crystal structure of homologous hTGase 2 (PDB ID 2Q3Z) as template
additional information
effect of microbial transglutaminase on the mechanical properties and microstructure of acid-induced gels and emulsion gels produced from thermal denatured egg white proteins (TD-EWPs), overview. Impact of TGase on mechanical, rheological, and microstructural properties of cold-set EWP gels and emulsion gels produced from the TD-EWP. EWP is sufficiently cross-linked by MTGase
additional information
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in the open active conformation, the catalytic core, which contains the catalytic triad Cys277, His335, and Asp358, is accessible and capable of catalyzing the formation of isopeptide bonds (cross-links) between peptide bound Gln and Lys residues. The cross-linking activity is also referred to as transamidation and occurs via a ping-pong mechanism. First, the nucleophilic active site thiolate (Cys277) attacks an acyl donor substrate (i.e. a peptide-bound Gln residue) resulting in the release of one equivalent of ammonia and the formation of the intermediate thioester. Subsequently, the thiolate is regenerated by nucleophilic attack of an acyl acceptor substrate (i.e. a peptide-bound Lys residue) to afford the isopeptide product, or the thioester is cleaved by water to afford the deamidated (or hydrolysis) product. Upon GTP binding, hTG2 primarily adopts a closed or compact conformation where the catalytic Cys277 becomes inaccessible
additional information
intracellular tTG is predominantly in the closed-state, with a small portion being in the crosslinking-competent open-state, while extracellular tTG would adopt the open-state, and be crosslinking-competent. This view is somewhat complicated by the mildly oxidative conditions in the extracellular space. A triad of cysteine residues (Cys 230, Cys 370, and Cys 371) are able to make one of two disulfide bonds (C370-C230, or C370-C371) in oxidative conditions. Either disulfide bond reduces crosslinking catalytic activity, but oxidized tTG maintains a conformation similar to the open-state. Cp4d is a reversible small molecule which has little effect on tTG conformation, while NC9 is a bulkier, irreversible peptidomimetic compound presumed to stabilize tTG in the open-state. Cp4d treatment has little effect on the sensitivity of the assorted cells to glucose-oxygen deprivation-induced cell death. NC9 causes the tTG wild-type and tTG C277S mutant expressing cells to undergo a greater degree of cell death under the same conditions. The conformation of tTG is responsible for the cell death enhancement. Binding partners of tTG depend upon its conformation, confromation-independent binding modes of tTG, structure-function analysis, detailed overview
additional information
mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview
additional information
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mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview
additional information
mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview
additional information
mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview
additional information
molecular dynamics simulations
additional information
molecular dynamics simulations are developed to model the binding modes of donor substrates in the gTG2 active site. The inability of gTG2 to efficiently catalyze peptide synthesis from donors containing alanine results from the narrow substrate binding tunnel, which prevents bulkier donors from adopting a catalytically productive binding mode. Molecular homology modeling of TG2 using the structure of inhibitor-complexed human enzyme as template (PDB ID: 2Q3Z). Donor substrate specificity of gTG2-catalyzed peptide synthesis, overview
additional information
mTGase structure-function relationship, overview. The active site is a single cysteine (C64) residing at the bottom cleft of the crystal structure (PDB ID 3IU0) where it forms a catalytic triad with the aspartic acid (D255) and histidine (H274) residues. The pro-sequence region is vital for enzyme folding and inhibition of enzyme activation within the cells to avoid detrimental cross-linking of cytosolic proteins. The enzyme structure has a wide active site cleft position that accommodates the alpha-helix pro-sequence. This unique attribute explains the broad substrate specificity for acyl donors which allows for additional flexibility in the active site to accommodate a less specific substrate, overview
additional information
the catalytic core domain of TG2 is essential for the TG2-DNAJA1 interaction, mass spectrometry analysis. In contrast, the cross-linking activity of TG2 is not essential for the interaction since DNAJA1 also interacts with the catalytically inactive form of TG2. DNAJA1 interacts with the open form of TG2 and regulates its transamidation activity under both in vitro and in situ conditions
additional information
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the catalytic core domain of TG2 is essential for the TG2-DNAJA1 interaction, mass spectrometry analysis. In contrast, the cross-linking activity of TG2 is not essential for the interaction since DNAJA1 also interacts with the catalytically inactive form of TG2. DNAJA1 interacts with the open form of TG2 and regulates its transamidation activity under both in vitro and in situ conditions
additional information
the enzyme shows a ping-pong mechanism
additional information
the MTG has a triplet active center Cys151-Asp342-His361
additional information
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the N-terminal amino acid sequence of MsTGase is GKIEEG-LVI
additional information
transglutaminase 2 (TG2) is the only mammalian transglutaminase to harbor the conserved Cys-triad
additional information
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transglutaminase 2 (TG2) is the only mammalian transglutaminase to harbor the conserved Cys-triad
additional information
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comparison of the different TGases from Streptomyces mobaranensis and Streptomyces cinnamoneus, and of a chimeric mutant constructed from both, overview
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additional information
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mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview
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additional information
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the MTG has a triplet active center Cys151-Asp342-His361
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additional information
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comparison of the different TGases from Streptomyces mobaranensis and Streptomyces cinnamoneus, and of a chimeric mutant constructed from both, overview
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additional information
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the enzyme shows a ping-pong mechanism
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additional information
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mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview
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C277S
the mutant binds to heparin with about wild type affinity
D94A/D97A
the mutant is found at comparable levels on the cell surface with that shown for the wild type enzyme
K205A/R209A
the mutant shows increased activity in NIH 3T3 and HEK-293/T17 cell lysates compared to the wild type enzyme
K60A/R601A/K602A
the mutant shows reduced activity in NIH 3T3 cell lysates and increased activity in HEK-293/T17 cell lysates compared to the wild type enzyme
C230A
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the mutant shows about wild type activity but is less susceptible to oxidation than the wild type enzyme
C277A
the mutant is unable to bind guanine nucleotides
C277V
the mutant is susceptible to digestion by trypsin, and significantly impaired in nucleotide binding
C370A
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the kcat/Km is 33% of the wild type enzyme
C371A
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the kcat/Km is 5% of the wild type enzyme
D151N/E153Q/E154Q/E155Q/E158Q
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mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity. GTPase activity is activated by presence of Ca2+
D306N/N308S/N310S
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mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
D306N/N310A
the purified tTG mutant adopts a conformation similar to that of wild-type tTG, based on their mutual ability to bind bodipy-GTP-gammaS and to resist proteolysis by trypsin
D434A
the mutant can be transiently expressed in NIH 3T3 cells but not be generated as recombinant protein. The mutant is cytotoxic when expressed in NIH 3T3 cells
D434N/E435Q/E437N
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mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity. GTPase activity is activated by presence of Ca2+
E396Q/N398S/D400N
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mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
E447Q/E451Q/E452Q/E454Q
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mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
F174A
the F174A mutant is deficient in nucleotide binding, and is digested by trypsin in the presence of GTP-gammaS, Phe174 appears to be involved in a pi-stacking interaction
F174W
mutant resists proteolysis and is able to bind nucleotide
K677A
the mutant can be transiently expressed in NIH 3T3 cells but not be generated as recombinant protein, the mutant is unable to bind bodipy-GTP-gammaS, and shows high sensitivity to degradation by trypsin. The mutant is cytotoxic when expressed in NIH 3T3 cells
N229S/N231S/D232N/D233N
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mutation of calcium binding site, does not cause major structural alterations. Mutant binds less than 6 Ca2+ and is deficient in transglutaminase activity
N681A
the mutant can be transiently expressed in NIH 3T3 cells and generated as recombinant protein. The mutant is cytotoxic when expressed in NIH 3T3 cells
Q163D
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
Q163L
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
Q164L
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
Q169L
the mutant shows no loss of nucleotide binding ability when assayed with [alpha-32P] GTP, and exhibits only a moderate loss of binding ability when assayed with [35S]GTP-gammaS
R476A
the mutant binds nucleotide as well as the wild-type enzyme
R478A
the mutant has partially reduced nucleotide binding
R579A
the R579A mutant of tTG is far more susceptible to proteolysis by trypsin or by calpain than the wild-type
R580A
the mutant is GTP-binding deficient
R580K
decreases in nucleotide binding are observed for the R580L and R580K mutants
R580L
decreases in nucleotide binding are observed for the R580L and R580K mutants
R580L/C277A
the tTG mutant is deficient in GTP-binding and protein crosslinking activity, but still induces cell death
S171A
the mutant binds nucleotide as well as the wild-type enzyme
S216A
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the mutant lacks the S216 phosphorylation site
T360A
mutants show an increase in preference for deamidation with respect to transamidation compared to the wild-type enzyme
T360W
mutants show an increase in preference for deamidation with respect to transamidation compared to the wild-type enzyme
W241A
no detectable activity
W254A
the mutant can be transiently expressed in NIH 3T3 cells and generated as recombinant protein, the mutant is unable to bind bodipy-GTP-gammaS, and shows high sensitivity to degradation by trypsin. W254A forms a dimer of tTG molecules in the open-state conformation. The mutant is cytotoxic when expressed in NIH 3T3 cells
W332A
no detectable activity
Y516C
the mutant is less capable of binding guanine nucleotide compared to wild-type
Y516F
the mutant is less capable of binding guanine nucleotide compared to wild-type
C277A
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the mutant lacks transamidation function
I331N
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the mutant is associated with early-onset type 2 diabetes, has no GTP-binding ability and shows 32% of wild type activity
M330R
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the mutant is associated with early-onset type 2 diabetes, has very weak GTP-binding ability and shows 20% of wild type activity
N333S
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the mutant is associated with early-onset type 2 diabetes, has elevated GTP-binding ability and shows 7% of wild type activity
S216A
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the mutant lacks the S216 phosphorylation site
C324A
no enzymic activity
C302A
the mutant shows dramatically decreasing activity compared to the wild type enzyme
D348A
the mutant shows dramatically decreasing activity compared to the wild type enzyme
H333A
the mutant shows dramatically decreasing activity compared to the wild type enzyme
prosuction
expression of enzyme as inclusion bodies in Escherichia coli, and purification using an on-column refolding procedure based on cation SP fast flow chromatography. Protein yield is 53%, and 105 mg from 3.2 g wet weight cells, specific activity is 21 U/mg. Refolded protein demonstrates nearly identical abilities compared with native enzyme
N160Q
the mutant shows wild type activity
N160Q/N355Q
the mutant shows 57% activity compared to the wild type enzyme
N355Q
the mutant shows 147% activity compared to the wild type enzyme
N160Q
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the mutant shows wild type activity
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N160Q/N355Q
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the mutant shows 57% activity compared to the wild type enzyme
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N355Q
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the mutant shows 147% activity compared to the wild type enzyme
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A10S
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the mutant shows higher specific activity compared to the wild type enzyme
D14N
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the mutant shows higher specific activity compared to the wild type enzyme
D20A
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the mutant shows reduced activity compared to the wild type enzyme
D301A
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the mutation drastically reduces the catalytic activity of the enzyme
D304A
41.1% residual activity
D3F
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the mutant shows higher specific activity compared to the wild type enzyme
D3L
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the mutant shows higher specific activity compared to the wild type enzyme
D3N
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the mutant shows higher specific activity compared to the wild type enzyme
E164L
site-directed mutagenesis, the E164L mutant exhibits a 1.95fold increased specific activity and 1.66fold increased half-life at 50°C compared to wild-type. The molecular dynamics (MD) simulation results indicate that the mutation Glu164Leu results in weaker interactions of Asp159-Glu164 and Gly228-Leu231, leading to the enhanced instability of Ile240-Asn253 linked to Gly228-Leu231 by eight residues. It further causes reduced interactions between loop region 1 (Ile240-Asn253) and loop region 2 (His277-Met288), facilitating the access of substrate molecule to the active site. Structure-activity relationship for MTG adapted to high temperature conditions. Enhancing activity and thermostability of Streptomyces mobaraensis transglutaminase by directed evolution, Molecular mechanism of improved activity of E164L analyzed by molecular dynamics simulations
E28D
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the mutant shows higher specific activity compared to the wild type enzyme
E29A
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the mutant shows about 60% reduced activity compared to the wild type enzyme
E300A
54.7% residual activity
E58D
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the mutant shows higher specific activity compared to the wild type enzyme
F254A
complete loss of activity
F305A
18.6% residual activity
G63A
complete loss of activity
H274A
9.3% residual activity
H277A
complete loss of activity
H289F
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the mutant shows higher specific activity compared to the wild type enzyme
I240A
68.3% residual activity
I24A
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the mutant shows reduced activity compared to the wild type enzyme
K269S
site-directed mutagenesis
K294L
site-directed mutagenesis
L16A
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the mutant shows wild type activity
L27A
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the mutant shows about 40% reduced activity compared to the wild type enzyme
L285A
36.8% residual activity
M16T
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the mutant shows higher specific activity compared to the wild type enzyme
M16T/G283S
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the mutant shows higher specific activity compared to the wild type enzyme
N23A
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the mutant shows about 50% reduced activity compared to the wild type enzyme
N25A
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the mutant shows reduced activity compared to the wild type enzyme
N276A
1.7% residual activity
N28A
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the mutant shows about 45% reduced activity compared to the wild type enzyme
N320D
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the mutant shows higher specific activity compared to the wild type enzyme
N32D
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the mutant shows higher specific activity compared to the wild type enzyme
N32D/E264D/N320T
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the mutant shows higher specific activity compared to the wild type enzyme
NG257S
site-directed mutagenesis
P12S
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the mutant shows higher specific activity compared to the wild type enzyme
Q74A
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the mutant shows higher specific activity compared to the wild type enzyme
Q74L
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the mutant shows higher specific activity compared to the wild type enzyme
Q74N
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the mutant shows higher specific activity compared to the wild type enzyme
R238F
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the mutant shows higher specific activity compared to the wild type enzyme
R238L
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the mutant shows higher specific activity compared to the wild type enzyme
R26A
18% residual activity
R26F
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the mutant shows higher specific activity compared to the wild type enzyme
R26L
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the mutant shows higher specific activity compared to the wild type enzyme
R5K
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the mutant shows higher specific activity compared to the wild type enzyme
S199A
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the mutant shows higher specific activity compared to the wild type enzyme
S23Y/S24N
site-directed mutagenesis
S284T
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the mutant shows higher specific activity compared to the wild type enzyme
S299L
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the mutant shows higher specific activity compared to the wild type enzyme
S2P
site-directed mutagenesis, the mutant shows increased activity compared to wild-type
S2P/S23Y/S24N/H289Y/K294L
site-directed mutagenesis, the mutant TG16 shows 19fold reduced thermal stability/half-life at 60°C compared to wild-type enzyme, differential scanning fluorimetry, the transition point of thermal unfolding is increased by 7.9°C compared to wild-type. The inactivation process follows a pseudo-first-order reaction which is accompanied by irreversible aggregation and intramolecular self-crosslinking of the enzyme. The increased thermoresistance is caused by a higher backbone rigidity as well as increased hydrophobic interactions and newly formed hydrogen bridges, molecular dynamics simulations, overview. The mutant shows increased activity compared to wild-type
S303A
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the mutant shows higher specific activity compared to the wild type enzyme
S303F
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the mutant shows higher specific activity compared to the wild type enzyme
S303T
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the mutant shows higher specific activity compared to the wild type enzyme
T77A
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the mutant shows higher specific activity compared to the wild type enzyme
T77F
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the mutant shows higher specific activity compared to the wild type enzyme
T77L
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the mutant shows higher specific activity compared to the wild type enzyme
T77S
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the mutant shows higher specific activity compared to the wild type enzyme
V21A
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the mutant shows about wild type activity
V252A
6.0% residual activity
V30D
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the mutant shows higher specific activity compared to the wild type enzyme
V30I
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the mutant shows higher specific activity compared to the wild type enzyme
V30T
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the mutant shows higher specific activity compared to the wild type enzyme
V65A
10.2% residual activity
V65I
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the mutant shows higher specific activity compared to the wild type enzyme
V6T
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the mutant shows higher specific activity compared to the wild type enzyme
W59F
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the mutant shows higher specific activity compared to the wild type enzyme
Y10A
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the mutant shows reduced activity compared to the wild type enzyme
Y14A
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the mutant shows wild type activity
Y278A
3.9% residual activity
Y34F
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the mutant shows higher specific activity compared to the wild type enzyme
Y34F/D268N
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the mutant shows higher specific activity compared to the wild type enzyme
Y42H
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the mutant shows higher specific activity compared to the wild type enzyme
Y62A
complete loss of activity
Y75F
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the mutant shows higher specific activity compared to the wild type enzyme
Y75H
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the mutant shows higher specific activity compared to the wild type enzyme
E28D
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the mutant shows higher specific activity compared to the wild type enzyme
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E58D
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the mutant shows higher specific activity compared to the wild type enzyme
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R26L
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the mutant shows higher specific activity compared to the wild type enzyme
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S303A
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the mutant shows higher specific activity compared to the wild type enzyme
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Y42H
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the mutant shows higher specific activity compared to the wild type enzyme
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production
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overexpression of enzyme in Escherichia coli and purification from inclusion bodies, refolding by rapid dilution in a Ca2+- and guanidine-containing buffer. Purified enzyme has similar characteristics as native protein
C277S
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active-site mutant
C277S
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mutation in active site
C277S
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mutation of active site. Mutant still binds 6 Ca2+
C277S
the mutation has no effect on cell death
G224V
the mutation increases the enzyme's calcium-binding affinity and transamidation activity 10fold and isopeptidase activity severalfold
G224V
a putative natural mutant variant of isozyme TG2, mutant TG2 G224V gains higher stability and Ca2+-dependent activity compared to the G224 form. Possibly the G224V form, rather than the G224 form, is the natural TG2 variant
C64A
complete loss of activity
C64A
0.4% residual activity
D255A
complete loss of activity
D255A
0.2% residual activity
H289Y
site-directed mutagenesis
H289Y
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the mutant shows higher specific activity compared to the wild type enzyme
N253A
complete loss of activity
N253A
1.1% residual activity
Y256A
complete loss of activity
Y256A
1.9% residual activity
Y75A
5.3% residual activity
Y75A
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the mutant shows higher specific activity compared to the wild type enzyme
additional information
the TG2DELTA1-15 mutant is not detectable within the extracellular matrix
additional information
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mutants in BH3 peptide of enzyme fail to sensitize cells toward apoptosis
additional information
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downregulation of enzyme by RNAi in U87MG glioblastoma cells demonstrates decreases assembly of fibronectin in the extracellular matrix
additional information
comparison of wild-type with G224V mutant enzyme structure and actives sites, overview
additional information
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comparison of wild-type with G224V mutant enzyme structure and actives sites, overview
additional information
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efficient site-specific antibody-drug conjugation by engineering a nature-derived recognition tag for microbial transglutaminase, overview
additional information
generation of stable cell lines of HEK-293T AD cells overexpressing human TG2. Generation of domain variants of TG2, i.e. GST-TG2DELTAbeta-barrel2, full-length TG2, GST-CAT, GST-TG2DELTAbeta-sandwich, GST-TG2DELTAbeta-barrel1, GST-TG2DELTACAT
additional information
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generation of stable cell lines of HEK-293T AD cells overexpressing human TG2. Generation of domain variants of TG2, i.e. GST-TG2DELTAbeta-barrel2, full-length TG2, GST-CAT, GST-TG2DELTAbeta-sandwich, GST-TG2DELTAbeta-barrel1, GST-TG2DELTACAT
additional information
identification of tTG mutants which adopt either the open or the closed state, overview
additional information
by first reacting a bifunctionalized peptide with the more specific KalbTG and in a second step with the less specific MTG from Streptomyces mobaraensis (UniProt ID P81453), a successful bio-orthogonal labeling system is demonstrated. Fusing the KalbTG recognition motif to an antibody allows for site-specific and ratio-controlled labeling using low label excess
additional information
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by first reacting a bifunctionalized peptide with the more specific KalbTG and in a second step with the less specific MTG from Streptomyces mobaraensis (UniProt ID P81453), a successful bio-orthogonal labeling system is demonstrated. Fusing the KalbTG recognition motif to an antibody allows for site-specific and ratio-controlled labeling using low label excess
additional information
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by first reacting a bifunctionalized peptide with the more specific KalbTG and in a second step with the less specific MTG from Streptomyces mobaraensis (UniProt ID P81453), a successful bio-orthogonal labeling system is demonstrated. Fusing the KalbTG recognition motif to an antibody allows for site-specific and ratio-controlled labeling using low label excess
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additional information
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downregulation of enzyme by RNAi in U87MG glioblastoma cells demonstrates decreased assembly of fibronectin in the extracellular matrix
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for analysis of the effect of TG2 deficiency, two independent groups of TG2 knockout mouse models are generated, one a global TG2 knockout fromconception and the other offering the versatility of the Cre/loxP site-specific recombination system to generate, in a temporally specific manner, global knockouts or tissue-specific knockouts
additional information
for analysis of the effect of TG2 deficiency, two independent groups of TG2 knockout mouse models are generated, one a global TG2 knockout fromconception and the other offering the versatility of the Cre/loxP site-specific recombination system to generate, in a temporally specific manner, global knockouts or tissue-specific knockouts
additional information
construction of a chimeric mutant constructed from the TGases of Streptomyces mobaranensis (SMTG) and Streptomyces cinnamoneus (SCTG), the mutant enzyme consists of the N-terminal half of SCTG and the C-terminal half of SMTG
additional information
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construction of a chimeric mutant constructed from the TGases of Streptomyces mobaranensis (SMTG) and Streptomyces cinnamoneus (SCTG), the mutant enzyme consists of the N-terminal half of SCTG and the C-terminal half of SMTG
additional information
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construction of a chimeric mutant constructed from the TGases of Streptomyces mobaranensis (SMTG) and Streptomyces cinnamoneus (SCTG), the mutant enzyme consists of the N-terminal half of SCTG and the C-terminal half of SMTG
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additional information
deletion analysis of the TGase promoter, the pro-peptide is essential for the correct folding of Streptomyces TGase, TGase is usually expressed in an inactive pro-TGase form, which is then converted to active TGase by the addition of activating proteases in vitro
additional information
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deletion analysis of the TGase promoter, the pro-peptide is essential for the correct folding of Streptomyces TGase, TGase is usually expressed in an inactive pro-TGase form, which is then converted to active TGase by the addition of activating proteases in vitro
additional information
the enzyme is mutated by deleting a specific 84 bp fragment using overlapping extension PCR. The deletion of 28 amino acid residues fragment presents an external free state that results in the mutant MTG spatial configuration to be compressed and thus can enhance the stability or solubility of mutant MTG. The mutant MTG is more stable than the wild-type MTG at 50-60°C, at pH 4.0-9.0, at 7-9% salinity, 30-35% ethanol concentration, and in the presence of Li(I) and Ag(I). The mutant MTG is an intracellular expression protein and mainly expresses in soluble form
additional information
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the enzyme is mutated by deleting a specific 84 bp fragment using overlapping extension PCR. The deletion of 28 amino acid residues fragment presents an external free state that results in the mutant MTG spatial configuration to be compressed and thus can enhance the stability or solubility of mutant MTG. The mutant MTG is more stable than the wild-type MTG at 50-60°C, at pH 4.0-9.0, at 7-9% salinity, 30-35% ethanol concentration, and in the presence of Li(I) and Ag(I). The mutant MTG is an intracellular expression protein and mainly expresses in soluble form
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additional information
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deletion analysis of the TGase promoter, the pro-peptide is essential for the correct folding of Streptomyces TGase, TGase is usually expressed in an inactive pro-TGase form, which is then converted to active TGase by the addition of activating proteases in vitro
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additional information
construction of a chimeric mutant constructed from the TGases of Streptomyces mobaranensis (SMTG) and Streptomyces cinnamoneus (SCTG), the mutant enzyme consists of the N-terminal half of SCTG and the C-terminal half of SMTG
additional information
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construction of a chimeric mutant constructed from the TGases of Streptomyces mobaranensis (SMTG) and Streptomyces cinnamoneus (SCTG), the mutant enzyme consists of the N-terminal half of SCTG and the C-terminal half of SMTG
additional information
development and evaluation of a method for production of a reusable immobilized recombinant His-tagged Escherichia coli biotin ligase (BirA) onto amine-modified magnetic microspheres (MMS) via covalent cross-linking catalyzed using microbial transglutaminase (MTG). The site-specifically immobilized BirA exhibited approximately 95% of enzymatic activity of the free BirA, and without a significant loss in intrinsic activity after 10 rounds of recycling. Method, overview
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development of enzyme engineering to improve, alter, or customise the functional properties of mTGase, e.g. thermoengineering for better heat stability and heat sensitivity, overview. The N-termius of mTGase is an important region that influences the thermal properties of the enzyme due to the fact that all single-point mutations related to the altered thermal properties are located in this area, random mutagenesis. Semirational mutagenesis is also successful to isolate mTGase variants with increased thermostabilities. Seven hot spot residues, which are reported to be the thermostabilizing sites, are mutated for the generation of mutant libraries to screen for thermostable variants. Later, variants with single amino acid substitution comprising of the highest thermostabilities are mixed by DNA shuffling to generate a secondary library for screening. Finally, the variants with improved thermostabilities are isolated via standard assay. For production of soluble enzyme, introduction of a fusion partner with the extension of the N-terminal region to contain few LacZ residues followed by the first 20 residues of enzyme purine nucleoside phosphorylase is done. This strategy results in the accumulation of high levels of mTGase in the cytoplasm. The thermoinducible expression system yields a lower protein yield but produces the enzyme with a higher specificity as no major modification is done to the enzyme making it preferable compared to constitutive expression system
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effect of microbial transglutaminase on the mechanical properties and microstructure of acid-induced gels and emulsion gels produced from thermal denatured egg white proteins. Impact of TGase on mechanical, rheological, and microstructural properties of cold-set EWP gels and emulsion gels produced from the TD-EWP, preparation of cold-set TD-EWP emulsion gels reinforced with MTGase, size determination of emulsion droplets and evaluation of MTGase mediated-covalent cross-linking in gels and emulsion gels by SDS-PAGE, method, overview
additional information
engineering an automaturing transglutaminase with enhanced thermostability by genetic code expansion with two codon reassignments. The first amino acid, 3-chloro-L-tyrosine, is incorporated into microbial transglutaminase (MTG) in response to in-frame UAG codons to substitute for the 15 tyrosine residues separately. The two substitutions at positions 20 and 62 are found to each increase thermostability of the enzyme, while the seven substitutions at positions 24, 34, 75, 146, 171, 217, and 310 exhibit neutral effects. Then, these two stabilizing chlorinations are combined with one of the neutral ones, and the most stabilized variant is found to contain 3-chlorotyrosines at positions 20, 62, and 171, exhibiting a half-life 5.1fold longer than that of the wild-type enzyme at 60°C. Next, this MTG variant is further modified by incorporating the alpha-hydroxy acid analogue of Nepsilon-allyloxycarbonyl-L-lysine (AlocKOH), specified by the AGG codon, at the end of the N-terminal inhibitory peptide. The ester bond, thus incorporated into the main chain, efficiently self-cleaves under alkaline conditions (pH 11.0), achieving the autonomous maturation of the thermostabilized MTG in transformed Escherichia coli. Method, overview
additional information
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engineering an automaturing transglutaminase with enhanced thermostability by genetic code expansion with two codon reassignments. The first amino acid, 3-chloro-L-tyrosine, is incorporated into microbial transglutaminase (MTG) in response to in-frame UAG codons to substitute for the 15 tyrosine residues separately. The two substitutions at positions 20 and 62 are found to each increase thermostability of the enzyme, while the seven substitutions at positions 24, 34, 75, 146, 171, 217, and 310 exhibit neutral effects. Then, these two stabilizing chlorinations are combined with one of the neutral ones, and the most stabilized variant is found to contain 3-chlorotyrosines at positions 20, 62, and 171, exhibiting a half-life 5.1fold longer than that of the wild-type enzyme at 60°C. Next, this MTG variant is further modified by incorporating the alpha-hydroxy acid analogue of Nepsilon-allyloxycarbonyl-L-lysine (AlocKOH), specified by the AGG codon, at the end of the N-terminal inhibitory peptide. The ester bond, thus incorporated into the main chain, efficiently self-cleaves under alkaline conditions (pH 11.0), achieving the autonomous maturation of the thermostabilized MTG in transformed Escherichia coli. Method, overview
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introducing point mutations within MTG's active site increases reactivity toward the most reactive substrate variant, I6Q-GB1, enhancing MTG's capacity to fluorescently label an engineered, highly reactive glutamine substrate
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mTG crosslinked gelatin hydrogel preparation
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mutiple-site mutagenesis of Streptomyces mobaraensis transglutaminase is performed in Escherichia coli. According to enzymatic assay and thermostability study, among three penta-site MTG mutants (DM01-03), DM01 exhibits the highest enzymatic activity of 55.7 U/mg and longest half-life at 50°C (418.2 min) and 60°C (24.8 min)
additional information
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mutiple-site mutagenesis of Streptomyces mobaraensis transglutaminase is performed in Escherichia coli. According to enzymatic assay and thermostability study, among three penta-site MTG mutants (DM01-03), DM01 exhibits the highest enzymatic activity of 55.7 U/mg and longest half-life at 50°C (418.2 min) and 60°C (24.8 min)
additional information
peptidyl-linker sequences used that facilitate modification by microbial transglutaminase, overview
additional information
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peptidyl-linker sequences used that facilitate modification by microbial transglutaminase, overview
additional information
site-specific transglutaminase-mediated conjugation of interferon alpha-2b at glutamine or lysine residues
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the S2P variant is generated by random mutagenesis of the wild-type enzyme, and found to be more thermostable, able to withstand incubation at 60°C, and more active than the wild-type enzyme. The synthetic operon construct (based on GenBank ID KX775947) consists of two parts: first a gene encoding the pro-domain crucial for proper folding of the enzyme and second the gene encoding the mTG thermostable variant S2P, with a C-terminal His-tag. Each part is paired with a preceding PelB secretory sequence. The Km value is 3fold lower for the mutant S2P as compared to the wild-type. Conversely, the turnover number is higher for the wild-type enzyme, although the enzymatic efficiency is 2fold higher for the mutant. The mutant unfolds at a slightly higher temperature (56.3°C vs. 55.8°C) indicating improved thermostability although not statistically significant
additional information
utility of single lysine substitutions and the C-terminal Lys447 for engineering efficient acyl acceptor sites suitable for site-specific conjugation to a range of glutamine-based acyl donor substrates. Because recombinant mAbs lack the C-terminal Lys447 due to cleavage by carboxypeptidase B in the production cell host, it is analyzed if blocking the cleavage of Lys447 by the addition of a C-terminal amino acid can result in transamidation of Lys447 by a variety of acyl donor substrates. MTG efficiently transamidates Lys447 in the presence of any nonacidic, nonproline amino acid residue at position 448. Scanning mutagenesis of the hinge region in a Fab' fragment reveals sites of transamidation that are not reactive in the context of the full-length mAb. A positive-control peptide with two known lysine acyl acceptor sites (GGSTKHKIPGGS) is genetically fused to the C-terminus of mAb1 HC or LC (HC-KTag or LC-KTag, respectively) and analyzed for transamidation. The addition of the KTag to the HC C-terminus blocks removal of Lys447, thereby allowing MTG to utilize Lys447 as an acyl acceptor site. Mutational analysis of binding sites
additional information
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construction of a chimeric mutant constructed from the TGases of Streptomyces mobaranensis (SMTG) and Streptomyces cinnamoneus (SCTG), the mutant enzyme consists of the N-terminal half of SCTG and the C-terminal half of SMTG
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additional information
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production of optimized Zea mays transglutaminase (TGZo) using Pichia pastoris strain GS115 (pPIC9K-tgzo), method optimization, overview
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