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(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala + H2O
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg + Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
-
-
?
2-amino benzoyl-AEQDRNTREVFAQ-T(3-nitro-tyrosine)-A + H2O
2-amino benzoyl-AEQDRNTR + EVFAQ-T(3-nitro-tyrosine)-A
-
furin-mediated cleavage of a fluorogenic peptide derived from hSARS-CoV spike protein
-
-
?
2-aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp + H2O
?
-
-
-
-
?
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
?
-
-
-
-
?
5-carboxyfluorescein-Gln-Arg-Val-Arg-Arg-Ala-Val-Gly-Ile-Asp-Lys(5-carboxytetramethylrhodamine)-OH + H2O
?
-
-
-
?
Abz-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
?
-
-
-
-
?
Abz-GIRRKRSVSHQ-EDDnp + H2O
Abz-GIRRKR + SVSHQ-EDDnp
-
-
-
-
?
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GIRRKR + SVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Rous sarcoma viral envelope glycoprotein
-
-
?
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GRRTRR + EAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Ebola Zaire viral envelope glycoprotein
-
-
?
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HHRQRR + SVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human A disintegrin and metalloproteinase with thrombospondin ADAM-TS 6
-
-
?
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HKREKR + QAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human bone morphogenetic protein hBMP-2
-
-
?
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRREKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Dengue 2 viral envelope glycoprotein
-
-
?
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRRQKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Dengue 3 viral envelope glycoprotein
-
-
?
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-KIRRRR + DVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Herpes HHV-6A viral envelope glycoprotein
-
-
?
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-LKRRRR + DTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Borna disease viral envelope glycoprotein
-
-
?
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-NLRRRR + DLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Herpes HHV-6B viral envelope glycoprotein
-
-
?
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RERRRKKR + GLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RKRSRR + QVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Ebola Sudan viral envelope glycoprotein
-
-
?
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRAKR + SPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human bone morphogenetic protein hBMP-4
-
-
?
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRDKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Dengue 4 viral envelope glycoprotein
-
-
?
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLfGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + SLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RVKRGLAY(NO2)D-OH + H2O
?
-
-
-
-
?
Abz-SGRSRRAIDLQEDDnp + H2O
Abz-SGRSRR + AIDLQEDDnp
-
-
-
-
?
Abz-SKRSRRSVSVQ-EDDnp + H2O
Abz-SKRSRR + SVSVQ-EDDnp
-
-
-
-
?
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SKRSRR + SVSVQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Japan beta-encephalitis viral envelope glycoprotein
-
-
?
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRHKR + FAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from measle virus Fo viral envelope glycoprotein
-
-
?
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + DVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Ebola Ivory Coast viral envelope glycoprotein
-
-
?
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + SASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Herpes HHV-8 viral envelope glycoprotein
-
-
?
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SSRHRR + ALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human transforming growth factor TGF-beta3
-
-
?
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-TRRFRR + SITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from infectious bronchitis viral envelope glycoprotein
-
-
?
Ac-AAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AAKYKR
-
-
-
?
Ac-AARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AARYKR
-
-
-
?
Ac-Arg-Val-Arg-Arg-4-nitroanilide + H2O
Ac-Arg-Val-Arg-Arg + 4-nitroaniline
-
-
-
-
?
Ac-KARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-KARYKR
-
-
-
?
Ac-norleucine-YKR-4-methylcoumarin-7-amide
acetyl-norleucine-YKR + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-RA-norvaline-YKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RA-norvaline-YKR
-
-
-
?
Ac-RAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RAKYKR
-
-
-
?
Ac-RARYAR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYAR
-
-
-
?
Ac-RARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYKR
-
-
-
?
Ac-RARYRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYRR
-
-
-
?
Ac-RYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRR
-
-
-
?
Ac-RYRFKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRFKR
-
-
-
?
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
acetyl-norleucine-YKR-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-YKR + 7-amino-4-methylcoumarin
-
-
-
-
?
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Acetyl-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-7-amido-4-methylcoumarin + H2O
acetyl-Tyr-Glu-Lys-Glu-Arg + Ser-Lys-7-amido-4-methylcoumarin
-
-
-
-
?
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
AcRARYKK-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + AcRARYKK
-
-
-
?
ADAMTS9 propeptide + H2O
?
alpha-Subunit of the rat endopeptidase-24.18 + H2O
?
-
-
-
-
?
anthrax protective antigen + H2O
?
-
-
-
-
?
anthrax protective antigen precursor + H2O
?
-
-
-
-
?
anthrax protective antigen-83 + H2O
?
-
-
-
-
?
anthrax protective antigen-83 + H2O
anthrax protective antigen-63 + ?
-
-
-
-
?
avian influenza virus A hemagglutinin + H2O
?
Boc-RVRR-4-methylcoumarin 7-amide + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-RVRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Boc-RVRR
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
Carboxybenzyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
chimeric transforming growth factor-beta1/beta2 + H2O
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
duck carboxypeptidase D + H2O
?
-
i.e. DCPD, duck carboxypeptidase D acts as species-specific docking receptor for the duck hepatitis B virus. No cleavage of recombinant DCPD expressed in LMH cells
-
-
?
duck hepatitis B virus large envelope pre-S protein + H2O
?
-
the protein needs to be cleaved by duck endosomal furin or furin-like proprotein convertase for duck hepatocyte infection by duck hepatitis B virus
-
-
?
epithelial Na+ channel + H2O
?
extracellular superoxide dismutase + H2O
?
-
-
-
?
factor IX + H2O
?
-
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
FPV precursor molecule HA0 + H2O
subunit HA1 + subunit HA2
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
G-protein-coupled receptor GPR107 + H2O
?
Glu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate + H2O
Glu-Arg-Thr-Lys-Arg + (7-methylcoumarin-4-yl)acetate
-
-
-
-
?
glycoprotein 160 + H2O
?
-
from HIV-1, low activity
-
-
?
gp40/15 + H2O
gp40 + gp15
gp40/15 subtype 1e + H2O
gp40 + gp15
hBMP-2 precursor protein + H2O
?
-
cleavage sites are HKREKR-/-QAKH and HVRISR-/-SLHQ
-
-
?
hBMP-4 precursor protein + H2O
?
-
cleavage sites are RRRAKR-/-SPKH and HVRISR-/-SLPQ
-
-
?
hemagglutinin high pathogenic avian influenza virus subtype H5 + H2O
?
-
hemagglutinin loop of high pathogenic avian influenza virus subtype H5 binds much more tightly into the catalytic site of furin than the hemagglutinin low pathogenic avian influenza virus subtype H3 and hemagglutinin low pathogenic avian influenza virus subtype H5 systems. The -RRRKK- insertion in the hemagglutinin high pathogenic avian influenza virus subtype H5 in particular two arginines at S4 and S6 positions helps directly to hold the hemagglutinins cleavage loop in place by forming many strong hydrogen bonds between residues of hemagglutinin and furin
-
-
?
hemagglutinin low pathogenic avian influenza virus subtype H3 + H2O
?
-
-
-
-
?
hemagglutinin low pathogenic avian influenza virus subtype H5 + H2O
?
-
-
-
-
?
heparan sulfate 6-O-endosufatase Sulf2 + H2O
?
-
cleavage at arginine 570, located in the consensus sequence for the cleavage by furin-type proprotein convertases. The consensus sequence of the cleavage by furin and PCs is R/K-X-R/K-X-R/K-R-/-X. R, K, X, and denote arginine, lysine, any amino acid. Proteolytic processing of SulfFP2 protein by furin and furin-like proprotein convertases, and activity with Sulf2 truncation and exchange mutants, overview
-
-
?
hepatitis B e antigen precursor + H2O
?
high pathogenic H5N1 hemagglutinin + H2O
?
-
furin can only cleave the high pathogenic hemagglutinin. It generates most of its selectivity through interactions with subsites P1, P4, and P6, with interactions at P2 being less important and little preference at P3, P5, P7, and P8. The S1, S4, and S6 pockets are specifically designed to accommodate arginine, with lysine substitution fitting less well in different degrees
-
-
?
highly pathogenic Queretaro H5N2 hemagglutinin + H2O
?
-
only processed in the presence of heparin
-
-
?
histonin + H2O
?
-
furin releases intact histonin monomers from F4-multimeric histonin (12-mer). Histonin has an RLKR motif at the C-terminus after which furin cleaves specifically
-
-
?
HIV-1 gp160 + H2O
?
-
13mer and 19mer peptides digested equally well by furin at site1, showing complete processing at 5 h. 41mer and 51mer peptides are either barely or unprocessed, respectively. Product inhibition does not explain inability of furin to process the 41mer and 51mer peptides. Extended sequences require heparin for optimal processing
-
-
?
HIV-1 Tat protein + H2O
?
human semaphorin 3F + H2O
?
IBV spike protein + H2O
?
-
-
-
?
inactive pro-MT1-MMP + H2O
active MT1-MMP + ?
-
-
-
-
?
influenza deltaK-Fujian-like H5N1 hemagglutinin + H2O
?
-
76% processed
-
-
?
influenza Fujian-like H5N1 hemagglutinin + H2O
?
-
70% processed
-
-
?
influenza variant Fujian-like H5N1 hemagglutinin + H2O
?
-
mutations at the furin-processing site of the hemagglutinin, is less cleaved (38%) by furin as compared to the parent Fujian-like strain derived peptides
-
-
?
insulin-like growth factor-1 receptor + H2O
?
-
furin-like proprotein convertase activates insulin-like growth factor-1 receptor in vascular smooth muscle cell
-
-
?
lethal factor inhibitor 2 + H2O
?
-
-
-
-
?
membrane type-1 matrix metalloproteinase + H2O
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
membrane-bound collagen XXIII + H2O
shed collagen XXIII
-
furin is the major protease to process collagen XXIII. Processing occurs after the downstream recognition motif 94KIRTVR99, releasing the ectodomain
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
membrane-type 1-matrix metalloproteinase + H2O
?
-
-
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
mouse pro-growth hormone-releasing hormone + H2O
?
N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
nodal + H2O
?
-
cripto interacts with the nodal pro segment and mature domain and presents uncleaved precursor to extracellular furin that is recruited through its P-domain
-
-
?
p-Glu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
PA83 + H2O
?
a protective antigen
-
-
?
parathyroid hormone-related peptide + H2O
?
-
-
-
-
?
PC1/3 C-terminal peptide + H2O
?
-
cleavage by furin into a peptide with an apparent molecular mass of 12.5 kDa. Cleavage of the C-terminal to the pair of Args occupying positions 627 and 628
-
-
?
PC2-S383A
?
-
furin fully processes the PC2 mutant at the secondary site in AtT-20 cells, site is accessible to in trans cleavage
-
-
?
PCSK9 + H2O
?
-
cleavage by furin at Arg218. Mutations R218S, F216L, and D374Y of PCSK9 associated with hypercholesterolemia result in total or partial loss of furin/PC5/6A processing at the motif RFHR21, mutant A443T shows enhanced susceptibility to furin cleavage
-
-
?
PE2 glycoprotein precursor + H2O
?
enzyme is involved in maturation of PE2 glycoprotein of alphaviruses. Enzyme cleaves efficiently PE2 glycoprotein mutants with residues arginine, serine, phenylalanine, histidine, asparagine, or aspartic acid at the +1 position
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
pERKTR-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
pGlu-Arg-Thr-Lys-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate + H2O
?
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methyl-coumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
phenylacetyl-Arg-Val-Arg-7-amido-4-methylcoumarin + H2O
phenylacetyl-Arg-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
POMC prohormone precursor + H2O
ACTH + alpha-MSH + beta-endorphin
-
human pituitary may utilize the cathepsin L and prohormone convertase pathways for producing POMC-derived peptide hormones
-
-
?
precursor of transforming growth factor beta + H2O
?
pro-ADAMTS4 + H2O
?
-
furin plays an important role in the intracellular removal of ADAMTS4 prodomain. Multiple furin recognition sites: 206RPRR209, 209RAKR212, or 211KR212
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
pro-CD109 + H2O
CD109 + CD109 propeptide
pro-hADAM-15 protein + H2O
?
-
cleavage site is HIRRRR-/-DVVT
-
-
?
pro-hADAM-TS 4 protein + H2O
?
-
cleavage site is RPRRAKR-/-FASL
-
-
?
pro-hADAM-TS 6 protein + H2O
?
-
cleavage site is HHRQRR-/-SVSI
-
-
?
pro-hADAMTS-17 protein + H2O
?
-
cleavage site is HVRKRR-/-ADPD
-
-
?
pro-hADAMTS-23 protein + H2O
?
-
cleavage site is LKRRKR-/-AVNP
-
-
?
pro-hepcidin + H2O
active mature hepcidin
pro-hTGF-best1 protein + H2O
?
-
-
-
-
?
pro-hTGF-beta1 protein + H2O
?
-
cleavage site is NRRKKR-/-ALDA
-
-
?
pro-hTGF-beta2 protein + H2O
?
-
cleavage site is GQRKKR-/-ALDT
-
-
?
pro-hTGF-beta3 protein + H2O
?
-
cleavage site is SSRHRR-/-ALDT
-
-
?
pro-hTGF-beta4 protein + H2O
?
-
cleavage site is RSRGRR-/-FSQS
-
-
?
pro-MT-MMP 1 protein + H2O
?
-
cleavage site is NVRRKR-/-YALT
-
-
?
pro-MT-MMP 11 protein + H2O
?
-
cleavage site is RHRQKR-/-FVLS
-
-
?
pro-MT-MMP 3 protein + H2O
?
-
cleavage site is RNRQKR-/-FVLS
-
-
?
pro-MT-MMP 4 protein + H2O
?
-
cleavage site is QSRRRR-/-QTPP
-
-
?
pro-MT-MMP 6 protein + H2O
?
-
cleavage site is VRRRRR-/-YALS
-
-
?
pro-Notch1 + H2O
Notch1 + propeptide
pro-transforming growth factor-beta1 + H2O
transforming growth factor-beta1 + propeptide
-
-
-
?
pro-von Willebrand factor + H2O
?
-
-
-
-
?
proactivin A + H2O
activin A + ?
-
-
-
?
proaerolysin + H2O
?
-
cleavage site is KVRRAR-/-SVDG
-
-
?
procollagen V + H2O
?
-
proteolytic processing of the proalpha1(V) C-propeptide chain. Proteolytic C-propeptide removal by furin occurs between Arg1585 and Asn1586. Processing of the C-propeptide by furin is more efficient than processing by bone morphogenetic protein-1
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
proPDGF-A + H2O
PDGF-A + PGDF-A propeptide
-
a growth factor proform
-
-
?
proPDGF-B + H2O
PDGF-B + PGDF-B propeptide
-
a growth factor proform of 31 kDa
mature form of 17 kDa
-
?
proprotein convertase PCSK9 + H2O
?
-
-
PCSK9 is inactivated by furin by cleavage at residue R218. PCSK9 mutants R218S and F216L show a 50% reduction in the levels of the inactivated form, PCSK9 is inactivated by furin by cleavage at residue R218
-
?
Prorenin + H2O
?
-
-
-
-
?
protective antigen + H2O
?
-
-
-
-
?
Protective antigen component of anthrax toxin + H2O
?
-
cleavage at the sequence Arg-Lys-Lys-Arg
-
-
?
protein APRIL + H2O
?
commercial substrate preparation
-
-
?
Protein precursor + H2O
?
proVEGF-C + H2O
VEGF-C + VEGF-C propeptide
-
a growth factor proform
-
-
?
Pseudomonas aeruginosa exotoxin A + H2O
?
-
-
-
?
Pseudomonas exotoxin A + H2O
?
Pseudomonas toxin + H2O
?
-
cleavage site is RHRQPR-/-GWEQ
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin + Pyr-Arg-Thr-Lys-Arg
-
pERTKR-MCA
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
pyroglutamic acid-RTKR-4-methylcoumarin 7-amide + H2O
pyroglutamic acid-RTKR + 7-amino-4-methylcoumarin
-
-
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
SARS coronavirus spike glycoprotein + H2O
?
-
introduction of a prototypic furin recognition motif at R667 allows for efficient cleavage of the mutant glycoprotein
-
-
?
Sema3B + H2O
?
cleavage at the furin recognition site is critical for the function of this tumor suppressor
-
-
?
Sema3C + H2O
?
cleavage at the furin recognition site 742RNRR745. The point mutation R745A at the basic domain at the hypothetical furin recognition site 742RNRR745 disables the processing of Sema3C at this specific location. The C-terminal arginine of the putative furin cleavage site at the basic domain of Sema3C protein is critical for its functions in angiogenesis process
-
-
?
Synthetic peptides + H2O
?
-
based on the N-terminal sequence of human proalbumin
-
-
?
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
TACE/ADAM17 + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-RVRR-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
TGFbeta1 + H2O
?
-
-
-
-
?
type 1 IGF receptor + H2O
mature type I IDF receptor + ?
-
-
-
?
type 1 IGF receptor pro-form + H2O
mature type I IDF receptor + ?
-
-
-
-
?
viral precursor protein E3E2
?
-
processes E3E2 from African Chikungunya virus strain at the HRQRR642ST site, whereas a Chikungunya virus strain of Asian origin is cleaved at site RRQRR642SI
-
-
?
Viral spike glycoproteins + H2O
?
additional information
?
-
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
ADAMTS9 propeptide + H2O
?
-
the intact zymogen is secreted to the cell surface and is subsequently processed by furin before release into thge medium. ADAMTS9 processing is exclusively extracellular and occurs at the cell surface in cells that express high levels of furin
-
-
?
ADAMTS9 propeptide + H2O
?
-
ADAMTS is a disintegrin and metalloprotease domain with thrombospondin type 1 repeats
-
-
?
avian influenza virus A hemagglutinin + H2O
?
-
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
avian influenza virus A hemagglutinin + H2O
?
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
chimeric transforming growth factor-beta1/beta2 + H2O
?
-
consists of the transforming growth factor-beta1 LAP region, the transforming growth factor-beta2 cleavage site and the transforming growth factor-beta2 mature peptide
-
-
?
chimeric transforming growth factor-beta1/beta2 + H2O
?
-
efficiently cleaved
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
-
peptide derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
-
peptide-derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
-
?
epithelial Na+ channel + H2O
?
-
furin-dependent cleavage of the ectodomain at two sites in the alpha subunit and at a single site within the gamma subunit. Cleavage of the gamma subunit by furin and prostasin is required to release an inhibitory domain
-
-
?
epithelial Na+ channel + H2O
?
-
furin-dependent cleavage of the ectodomain at two sites in the alpha subunit and at a single site within the gamma subunit. Cleavage of the gamma subunit by furin and prostasin is required to release an inhibitory domain
-
-
?
epithelial Na+ channel + H2O
?
-
furin cleavage of epithelial Na+ channel subunits activates the channels by relieving Na+ self-inhibition. Activation requires that the alpha-subunit is cleaved twice
-
-
?
epithelial Na+ channel + H2O
?
-
epithelial Na+ channel activation during preferential assembly requires furin-dependent and furin-independent processing. Furin consensus site on the alpha subunit is required for epithelial Na+ channel activation upon assembly into alphabetagamma complexes, beta subunit may play a distinct furin-independent role in activation. No causal relationship between gamma cleavage and epithelial Na+ channel activation upon preferential assembly
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
-
-
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
-
the furin consensus site RRRR-/-D is located between the feline foamy virus Env residues 127 and 128
-
-
?
FPV precursor molecule HA0 + H2O
subunit HA1 + subunit HA2
-
-
-
?
FPV precursor molecule HA0 + H2O
subunit HA1 + subunit HA2
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
G-protein-coupled receptor GPR107 + H2O
?
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
-
-
?
G-protein-coupled receptor GPR107 + H2O
?
recombinant HA-tagged substrate expressed in HeLa cells. GPR107 contains an extended furin recognition site that includes KSKR, a variant of the classical furin cleavage motif (Arg-Xaa-(Lys/Arg)-Arg), although not common among furin substrates, in GPR107 the Lys residue replaces the first conserved Arg
-
-
?
gp40/15 + H2O
gp40 + gp15
-
putative furin cleavage site RSRR
-
-
?
gp40/15 + H2O
gp40 + gp15
-
cleaves recombinant Cryptosporidium parvum and Cryptosporidium hominis gp40/15. Putative furin cleavage site RSRR
-
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
-
?
hemagglutinin + H2O
?
-
-
-
-
?
hemagglutinin + H2O
?
-
from avian influenza H5N1 virus, high activity
-
-
?
hepatitis B e antigen precursor + H2O
?
-
furin can cleave the RRDR, RRGR, and RSPR motifs
-
-
?
hepatitis B e antigen precursor + H2O
?
-
-
-
-
?
HIV-1 Tat protein + H2O
?
-
furin processing is a likely mechanism for inactivating extracellular HIV-1 Tat protein. Furin cleavage reduces the transactivation activity of tat without preventing Tat uptake and entry into the nucleus
-
-
?
HIV-1 Tat protein + H2O
?
-
furin cleaves full-length Tat protein between amino acid 56 and 57, irrespective of seuence differences at amino acid 57
-
-
?
human semaphorin 3F + H2O
?
-
furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview
-
-
?
human semaphorin 3F + H2O
?
-
the substrate is produced as a C-terminal or an N-terminal human growth hormone fusion from the pLexM vector. Cleavage at the RXRR furin recognition site in the C-terminus, which is essential for the interaction of the C-terminus of Sema3F with the b1 domain of neuropilin
-
-
?
membrane type-1 matrix metalloproteinase + H2O
?
-
-
-
-
?
membrane type-1 matrix metalloproteinase + H2O
?
-
-
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
-
-
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
-
intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
-
furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP at the surface of cancer cells. Furin and related PCs are the essential components of the specialized cellular machinery that controls the levels of the functionally active, mature, MT1-MMP enzyme on the cell surface to continually support the potency of pericellular proteolysis
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
-
there are two furin cleavage motifs, R89-R-P-R-C93 and R108-R-K-R-Y112
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
-
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
furin cleaves the Env precursor into the surface and transmembrane subunits in the cell and then the viral protease cleaves the R-peptide from TM in newvirus. Structure analysis of the open cage-like structure like that of the R-peptide precursor and of the mature protein, overview. Furin cleavage not only separates the subunits and liberates the fusion peptide at the end of TM but also allows the C-terminal domain to relocate into a peripheral position. This conformational change might explain how the C-terminal domain of surface subunit gains the potential to undergo disulfide isomerization, an event that facilitates membrane fusion
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
-
production of mature growth hormone-releasing hormone from pro-growth hormone-releasing hormone is a stepwise process mediated predomionantly by furin at the N-terminal cleavage site followed by PC1/3 at the C terminus
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
-
furin is the most efficient convertase in cleaving the N-terminal RXXR/RXRR site
-
-
?
PA83 + H2O
PA63 + PA20
-
-
-
-
?
PA83 + H2O
PA63 + PA20
the protective antigen substrate is from Bacillus anthracis, commercial plant-produced deglycosylated PA83 (dPA83). Cleavage of the substrate generates two protein fragments with distinctly different molecular masses of 63 kDa (PA63) and 20 kDa (PA20). Plant-produced PA83 protein is almost fully cleaved by commercial furin, while plant-produced truncated enzymatically active furin displays about 75% relative activity compared to commercial human furin in vitro
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
-
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
-
activation by N-terminal fragment cleavage of proBNP in human plasma through furin
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
-
cleavage sequence is Arg73-Ala-Pro-Arg76-/-Ser77
-
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
-
pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4
-
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
-
i.e. pro-bone morphogenetic protein 4, site-specific cleavage by furin
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
-
CD109 is produced as a 205 kDa glycoprotein, which is then processed in the Golgi apparatus into 180 kDa and 25 kDa proteins by furin
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
-
CD109 is a glycosylphosphatidylinositol-anchored glycoprotein, cleavage motif comprises amino acids 1270-RRRR-1273
-
-
?
pro-hepcidin + H2O
active mature hepcidin
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
-
?
pro-hepcidin + H2O
active mature hepcidin
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
-
?
pro-Notch1 + H2O
Notch1 + propeptide
-
-
-
?
pro-Notch1 + H2O
Notch1 + propeptide
-
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
Protein precursor + H2O
?
-
Sindbis virus gpE2
-
-
?
Protein precursor + H2O
?
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
?
Protein precursor + H2O
?
-
human complement pro-C3
-
-
?
Protein precursor + H2O
?
-
fowl plague virus hemagglutinin
-
-
?
Protein precursor + H2O
?
-
Newcastle disease virus glycoprotein F0
-
-
?
Protein precursor + H2O
?
-
human insulin pro-receptor
-
-
?
Protein precursor + H2O
?
-
human immunodeficiency virus glycoprotein 160
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
measles glycoprotein F0
-
-
?
Protein precursor + H2O
?
-
human cytomegalovirus glycoprotein B
-
-
?
Protein precursor + H2O
?
-
the term -+- depicts the point of cleavage, e.g. stromelysin 3
-
-
?
Protein precursor + H2O
?
-
proalbumin (human)
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
-
-
-
?
Protein precursor + H2O
?
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
?
Protein precursor + H2O
?
-
human complement pro-C3
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
rapid cleavage of the-Arg-Arg-Asp-site, no significant cleavage of natural unprocessed variants with cleavage site sequences of-Arg-Arg-Val-, His-Arg-Asp- or Cys-Arg-Asp
-
-
?
Protein precursor + H2O
?
-
proalbumin (human)
-
-
?
Protein precursor + H2O
?
-
circulating human proalbumin variants with a mutation at either of the basic amino acids adjacent to the cleavage site are not cleaved
-
-
?
Protein precursor + H2O
?
-
cleavage following the prosequence Arg-Gly-Val-Phe-Arg-Arg
-
-
?
Protein precursor + H2O
?
-
also cleaves chicken proalbumin after a single arginine residue following the Arg-Asn-Leu-Gln-Arg-Phe-Ala-Arg prosequence
-
-
?
Protein precursor + H2O
?
-
proalbumin (human)
-
-
?
Pseudomonas exotoxin A + H2O
?
-
-
-
-
?
Pseudomonas exotoxin A + H2O
?
-
-
-
-
?
Pseudomonas exotoxin A + H2O
?
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
RPTPkappa + H2O
?
-
furin is required for S1 processing of RPTPkappa in the secretory pathway. Purified furin cleaves RPTPkappa within the membrane-proximal fibronectin type III domain at the sequence RTKR
-
-
?
RPTPkappa + H2O
?
-
-
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
-
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
-
-
?
Shiga toxin + H2O
?
-
not only the sequence known to be a minimal furin-recognition site, but also the structure around this site are important for furin processing of Shiga toxin and for rapid intoxication
-
-
?
Shiga toxin + H2O
?
-
cleavage site is ASRVAR-/-MASD
-
-
?
Shiga toxin + H2O
?
-
not only the sequence known to be a minimal furin-recognition site, but also the structure around this site are important for furin processing of Shiga toxin and for rapid intoxication
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Viral spike glycoproteins + H2O
?
-
-
-
-
?
Viral spike glycoproteins + H2O
?
-
-
-
-
?
additional information
?
-
-
viruses can be activated by furin
-
-
?
additional information
?
-
-
processing of viral glycoproteins
-
-
?
additional information
?
-
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
?
additional information
?
-
-
Borna disease virus glycoprotein is synthesized as a precursor that is cleaved by cellular furin to produce the mature glycoproteins GP1 and GP2
-
-
?
additional information
?
-
-
mutation in the RSRR cleavage site prevents processing of gp40/15
-
-
?
additional information
?
-
alternative PE2 cleavage phenotypes observed in vertebrate and arthropod cells are due to differences in substrate specificity between the arthropod and vertebrate furin enzymes and not to differences in host cell glycoprotein processing pathways
-
-
?
additional information
?
-
-
alternative PE2 cleavage phenotypes observed in vertebrate and arthropod cells are due to differences in substrate specificity between the arthropod and vertebrate furin enzymes and not to differences in host cell glycoprotein processing pathways
-
-
?
additional information
?
-
-
intracellular processing by furin-like prohormone convertases is required for secretion of cysteine-rich FGF receptor
-
-
?
additional information
?
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
-
-
?
additional information
?
-
-
no processing of: human lactase-phlorizin hydrolase
-
-
?
additional information
?
-
-
Preference for Arg-Glu-Lys-Arg-+-Ala vs. Lys-Ala-Lys-Arg-+-Arg
-
-
?
additional information
?
-
-
peptides patterned on the sequence 307-330 of the specific viral strains of the gp120 V3 loop
-
-
?
additional information
?
-
-
study of the specificity of human prohormone convertase PC1 and human furin
-
-
?
additional information
?
-
-
viruses can be activated by furin
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
probably involved in the proteolysis resulting in secretion of rat endopeptidase 24.18 alpha-subunit
-
-
?
additional information
?
-
-
possible role in processing essential cellular factors
-
-
?
additional information
?
-
-
processing of viral glycoproteins
-
-
?
additional information
?
-
-
implicated in maturation of substrates involved in development, signaling, coagulation, and pathogenesis, constitutive secretory pathway
-
?
additional information
?
-
-
proteolytic processing of a variety of proteins in the exocytic and endocytic pathways
-
?
additional information
?
-
-
is not able to cleave mutant Shiga-2D toxin
-
-
?
additional information
?
-
-
low pathogenic Mexico H5N2 hemagglutinin is not processed by furin
-
-
?
additional information
?
-
-
mutation in the RSRR cleavage site prevents processing of gp40/15
-
-
?
additional information
?
-
-
a three-step autocatalytic processing including the cleavage of the prodomain at the Arg-Leu-Gln-Arg89Q-Glu90 site, is required for the efficient activation of furin
-
-
?
additional information
?
-
-
furin possesses a strong preference for substrates containing the multibasic cleavage motif Arg-X-Arg/Lys-ArgV-X
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase, recombinantly expressed as GFP-tagged enzyme in human MDA-MB-468 cells, breast adenocarcinoma cells, is furin-dependent and specific
-
-
?
additional information
?
-
-
furin cleavage sequence is RXXR-/-X, X is not Cys
-
-
?
additional information
?
-
-
furin is a proprotein convertase that requires the cleavage sequence R-X-K/R-R, clear interdependence of furin subsites, substrate specificity with synthetic peptide substrates, overview
-
-
?
additional information
?
-
-
furin performs a calcium-dependent proteolytic cleavage at the C-terminus of a consensus amino acid motif R-X-K/R-R, with X being any amino acid. This tetrapeptide motif provides sufficient specificity to bind the active furin
-
-
?
additional information
?
-
-
furin performs autocleaqvage to its soluble form
-
-
?
additional information
?
-
activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
-
-
?
additional information
?
-
-
activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
-
-
?
additional information
?
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
high substrate selectivity and enzymatic activity of furin
-
-
?
additional information
?
-
recombinant expression of Sema3 wild-type substrates and of mutant Sema3C (R745A, 85.2 kDa) in HEK-293FT cells
-
-
?
additional information
?
-
-
recombinant expression of Sema3 wild-type substrates and of mutant Sema3C (R745A, 85.2 kDa) in HEK-293FT cells
-
-
?
additional information
?
-
to transiently express the substrate factor IX (FIX, amino acids 29-461) in Nicotiana benthamiana plants, the signal peptide (amino acids 1-28) is removed from the FIX sequence (UniProt ID P00740) and replaced with a Nicotiana tabacum PR-1a signal peptide. a KDEL sequence and the His6 tag are added to the C-terminus. Enzyme substrate precursor polypeptide of factor IX (FIX) undergoes several post translational modifications (PTMs), including the removal of the signal peptide (aa 1-28), carboxylation of the first 12 glutamic acid residues downstream from the 18-amino acid propeptide sequence (aa 29-46) in the region rich in glutamic acid (aa 47-92, called the gamma-carboxyglutamic acid or Gla domain) at the N-terminus. Proper gamma-carboxylation of the Gla domain is required for binding to calcium and phospholipids that is critical for proper protease activity during coagulation. In vivo, vitamin K-dependent gamma-carboxylase binds to the 18-amino acid propeptide of FIX, which is then cleaved and is required for optimal binding of the Gla domain to Ca2+ and phospholipids
-
-
?
additional information
?
-
-
to transiently express the substrate factor IX (FIX, amino acids 29-461) in Nicotiana benthamiana plants, the signal peptide (amino acids 1-28) is removed from the FIX sequence (UniProt ID P00740) and replaced with a Nicotiana tabacum PR-1a signal peptide. a KDEL sequence and the His6 tag are added to the C-terminus. Enzyme substrate precursor polypeptide of factor IX (FIX) undergoes several post translational modifications (PTMs), including the removal of the signal peptide (aa 1-28), carboxylation of the first 12 glutamic acid residues downstream from the 18-amino acid propeptide sequence (aa 29-46) in the region rich in glutamic acid (aa 47-92, called the gamma-carboxyglutamic acid or Gla domain) at the N-terminus. Proper gamma-carboxylation of the Gla domain is required for binding to calcium and phospholipids that is critical for proper protease activity during coagulation. In vivo, vitamin K-dependent gamma-carboxylase binds to the 18-amino acid propeptide of FIX, which is then cleaved and is required for optimal binding of the Gla domain to Ca2+ and phospholipids
-
-
?
additional information
?
-
-
survey of furin substrate specificity using substrate phage display
-
-
?
additional information
?
-
-
synthetic tripeptide substrates containing only pairs of basic amino acids are not well cleaved
-
-
?
additional information
?
-
-
the term -+- depicts the point of cleavage, the enzyme prefers substrates with an arginine 4-amino acid amino-terminal to the cleavage site
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
role in processing of proenkephalin
-
-
?
additional information
?
-
-
proprotein processing activity
-
-
?
additional information
?
-
-
is not able to cleave mutant Shiga-2D toxin
-
-
?
additional information
?
-
-
no cleavage of the low pathogenic H1N1 H1 hemagglutinin
-
-
?
additional information
?
-
-
soluble hemojuvelin originates from a furin cleavage at position 332-335. Soluble hemojuvelin is increased in cells overexpressing exogenous furin
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
-
-
?
additional information
?
-
-
3D structural environment of the furin binding pocket surrounding the core region P6-P2' of furin substrates, comparison to other protein convertases, to allow the rational design of novel specific molecular inhibitors targeting specific members of the mammalian proprotein convertase family, overview. The furin autocleavage site is RGVTKR75 -/-
-
-
?
additional information
?
-
-
furin performs a calcium-dependent proteolytic cleavage at the C-terminus of a consensus amino acid motif R-X-K/R-R, with X being any amino acid. This tetrapeptide motif provides sufficient specificity to bind the active furin
-
-
?
additional information
?
-
-
probably plays a role in proprotein maturation
-
-
?
additional information
?
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
?
additional information
?
-
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
?
additional information
?
-
plays an important role in posttranslatioal protein processing
-
?
additional information
?
-
-
plays an important role in posttranslatioal protein processing
-
?
additional information
?
-
-
regular (short) form of transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin
-
-
?
additional information
?
-
-
transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin. Transforming growth factor-beta2 is only inefficiently cleaved as a consequence of the isoform specific characteristics of its latency-associated peptide region structures
-
-
?
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(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(3-guanidinophenylcarbamate)
-
-
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
-
-
(1S,14S,17S,20S,23S,26S,33r)-26-amino-N-(4-carbamimidoylbenzyl)-20,23-bis(3-guanidinopropyl)-17-neopentyl-4,8,16,19,22,25,32-heptaoxo-3,9,15,18,21,24,31-heptaazabicyclo[31.2.2]heptatriacontane-14-carboxamide
-
(D-Arg)6 amide
-
IC50: 0.3 mM
(D-Arg)9 amide
-
IC50: 0.01 mM
(D-Arg)9-amide
-
protects RAW264.7 cells against anthrax toxemia with an IC50 of 0.0037 mM
(E)-N-((E)-5-(2-chloro-5-nitrobenzylidene)-4-oxothiazolidin-2-ylidene)-4-methylbenzenesulfonamide
-
competitive inhibitor
(N'Z,N''Z)-4,4'-oxybis(N'-(2-hydroxybenzylidene)benzenesulfonohydrazide)
-
competitive inhibitor
1,1'-((1R,3S,4S,6R)-4,6-bis(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
meso compound
1,1'-((1R,3S,4S,6R)-4-((4-guanidinonaphthalen-1-yl)oxy)-6-(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
racemate, blocks the S2 pocket
1,1'-((1S,3R,4R,6S)-4-((4-guanidinonaphthalen-1-yl)oxy)-6-(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
blocks the S2 pocket
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(azeno)-4,10-benzodiazacyclopentadecine
-
12% inhibition at 0.1 mM
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
10% inhibition at 0.1 mM
1-[(1R,2R,4S,5S)-2,4-bis(4-carbamimidamidophenoxy)-5-[(4-carbamimidamidophenyl)amino]cyclohexyl]guanidine
-
-
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
-
-
11-amino-undecanoyl-RARRRKKRT
-
-
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
noncompetitive inhibitor
2-Bromopalmitate
-
inhibits nodal processing by Flag-tagged furin
3'-oxo-6a,14a-dihydro-3'H-spiro[dibenzo[c,h]xanthene-7,1'-isobenzofuran]-3,11-diyl diacetate
-
-
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-bromophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-chlorophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((3,4,5-trimethoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((4-isopropoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-(benzo[d][1,3]dioxol-5-ylmethylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
-
3-allyl-1-methyl-1,2,3,4-tetrahydroisoquinoline
-
competitive inhibitor
3-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(4-amidomethyl)-benzamidine
MI-52, a substrate-analogous, noncovalent inhibitor. The furin-MI-52 complex is highly stable
3-guanidinomethylphenylacetyl-Val-Arg 4-amidinobenzylamide
-
3-hydroxy-5-(4-methoxyphenyl)-2-(4-phenoxy-3-sulfophenyl)-3H-pyrazol-2-ium
-
competitive inhibitor
4,10-bis[(4-methylphenyl)sulfonyl]-1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
-
4,6-bis(4-guanidinylphenoxy)-1-guanidinyl-3-(4-guanidinylphenylamino)cyclohexane
-
-
4,7-dibenzyl-1,2,9,10-tetradehydro-3,4,5,6,7,8-hexahydro-4,7-benzodiazacyclododecine
-
-
4-(2-aminoethyl)benzenesulphonyl fluoride
-
-
4-aminomethyl-phenylacetyl-Arg-Tle-Arg-4-aminomethyl-benzamidine
-
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
-
6-oxo-6H-benzo[c]chromen-3-yl 2-chlorobenzoate
-
-
8,11,22,25-tetrabenzyl-5,6,13,14,19,20,27,28-octadehydro-7,8,9,10,11,12,21,22,23,24,25,26-dodecahydrodibenzo[h,t][1,4,13,16]tetraazacyclotetracosine
-
-
8-amino-octanoyl-RARRRKKRT
-
-
Ac-Ac-RQIKIWFQNRRMKWKKRVR 4-amidinobenzylamide
-
Ac-AGYLLGKINLKALAALAKKILRVR 4-amidinobenzylamide
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Leu-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Leu-NH2
-
-
Ac-RRRRRRRVR 4-amidinobenzylamide
-
Ac-YGRKKRRQRRRVR 4-amidinobenzylamide
-
acetyl-Val-Arg-4-amidinobenzylamide
-
-
acetyl-Val-Arg-4-aminomethyl-benzamidine
-
AEBSF
-
partially inhibits ectodomain shedding by 45%
alpha1-Aantichymotrypsin
-
incorporation of furin recognition sequences within the reactive site loop of alpha1-antiprypsin leads to the production of furin inhibitors, construction of a series of alpha1-antichymotrypsin mutants by modifying the P7-P1 region of the reactive site loop
-
alpha1-antitrypsin M352R
i.e. alpha1-PDX. Engineering of alpha1-antitrypsin variants, containing Arg at the P1 site within the reactive site loop, with improved specificity for the proprotein convertase furin using site-directed random mutagenesis, screening, overview. The engineered a1-antitrypsin variant carrying the RXXR consensus motif for furin within its reactive site loop. Furin-mediated maturation of bone morphogenetic protein-4 is completely inhibited by ectopic expression of the AVNR variant
-
alpha1-antitrypsin Portland variant
-
alpha1-AT
-
a naturally occurring serpin and a potent inhibitor of furin
-
alpha1-PDX inhibitor
-
-
-
antithrombin/heparin
-
not: antithrombin alone
-
Arg-Arg-Arg-Arg-Arg-Arg
-
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
-
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
-
Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
Arg-Arg-Arg-Val-Arg-4-amidinobenzylamide
-
Arg-Arg-Arg-Val-Arg-4-aminomethyl-benzamidine
-
Arg-Arg-Val-Arg 4-amidinobenzylamide
-
beta-Ala-TPRARRRKKRT-amide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
-
Chloroquine
-
weakly affects proprotein convertase activity and E3E2 processing. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
Cu(2,2':6,2''-terpyridine)Cl2
-
IC50: 0.0077 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-hydroxo-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0072 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0051 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.005 mM
Cu(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(di-[2-picolyl]amine)Cl2
-
IC50: 0.038 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
cyclo[glutaryl-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[glutaryl-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[glutaryl-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
D-Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-Arg-Tle-Arg 4-amidinobenzylamide
-
D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Arg-D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
D-Tyr-Ala-Lys-Arg-CH2Cl
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
decanoyl-RVKR-chloromethyl ketone
decanoyl-RVKR-chloromethylketone
decanoyl-RVRR-chloromethyl ketone
-
-
diisopropyl fluorophosphate
DYYHFWHRGVKRSLSPHRPRHSR
-
i.e. profurin 39-62
E-64
-
minimal inhibition of ectodomain shedding
eglin c Arg replaced with Asp at P3
-
-
-
eglin c mutant D42R
-
-
-
eglin c mutant L45R
-
-
-
eglin variant M1 RVTR
-
-
-
eglin variant M2 RVKR
-
-
-
eglin variant M3 RVTRDERY
-
-
-
eglin variant M4 RVTRDRRY
-
-
-
eglin variant M5 RVTRDLDY
-
-
-
eglin variant M6 RVTRDLRR
-
-
-
eglin variant M7 RVTRDLRE
-
-
-
eglin variant M8 RVTRDARY
-
-
-
furin-Eda peptide acyclic
-
synthesis, overview. Designed a potent furin inhibitor that contains a highly reactive beta-turn inducing and radical generating enediynyl amino acid moiety, which is inserted between P1 and P19 residues of hfurin98-112 peptide, derived from the primary cleavage site of furin's own prodomain. The inhibitor displays a predominantly beta-turn structure. The inhibitor protects furin protein from self degradation
furin-Eda peptide cyclic
-
synthesis, overview
Glu-Gly-Arg-chloromethylketone
-
poor inhibitor
hfurin25-107
-
i.e. furin prodomain protein, competitive inhibitor, blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain, overview. Secondary structure of furin prodomain protein, overview
-
histone H1
-
efficiently blocks furin-dependent pro-von Willebrand factor processing in a dose-dependent manner, interaction between histone H1 and furin mainly takes place on the cell surface. H1 may be involved in extracellular and/or intracellular furin regulation
-
human proteinase inhibitor 8
-
-
-
inter-alpha-inhibitor protein IalphaIp
-
blocks furin activity in vitro and provides significant protection against cytotoxocity for murine peritoneal macrophages exposed to up to 500 ng/ml anthrax lethal toxin
-
L-1-chloro-3-(4-tosylamido)-7-amino-2-heptanone
-
-
lethal factor inhibitor 2
-
IC50: 0.002 mM
-
Lys-Arg chloromethyl ketone
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 4-[4-(2-amino-2-oxoethyl)piperazin-1-yl]butanamide bridged)
-
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]butanediamide bridged)
-
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]pentanediamide bridged)
-
m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
a competitive, noncovalent inhibitor, binding structure, overview
methyl 4-(bis(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl)benzoate
-
noncompetitive inhibitor
monensin
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
N''-[(1E)-[2-[(4-chlorobenzyl)oxy]phenyl]methylidene]carbonohydrazonic diamide
-
competitive inhibitor
N,N'-[[(1R,3S,4S,6R)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine
racemate, interferes directly with the catalytic competent conformation of the catalytic triad. Inhibition mechanism, overview
N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine
interferes directly with the catalytic competent conformation of the catalytic triad. Inhibition mechanism, overview
N-(benzo[d][1,3]dioxol-5-yl)-1,2,3,4-tetrahydroacridin-9-amine
-
competitive inhibitor
N-(thiazol-2-yl)-4-(5-((2,4,6-trioxotetrahydropyrimidin-5(6H)-ylidene)methyl)furan-2-yl)benzenesulfonamide
-
competitive inhibitor
N-tosyl-L-lysine chloromethyl ketone
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-2-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenoxy]acetamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-N'-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]propanediamide
-
-
N-[5-guanidino-2,4-bis-(4-guanidino-phenoxy)-cyclohexyl]-guanidine
-
-
N-[5-guanidino-2,4-bis-(5-guanidino-pyridin-2-yloxy)-cyclohexyl]-guanidine
-
-
N2(carbamidoyl)Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
-
N2(carbamidoyl)Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-(3-aminomethyl-phenylacetyl)-Val-Arg 4-amidinobenzylamide
-
N2-(5-(guanidino)valeroyl)-Val-Arg 4-amidinobenzylamide
-
N2-(5-aminopentanoyl)-Val-Arg 4-amidinobenzylamide
-
N2-(5-guanidinopentanoly)-Val-Arg 4-amidinobenzylamide
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-aminopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-aminobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidamidobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-aminopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-carbamimidamidopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(piperidin-4-ylmethyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-acetyl-D-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
-
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Arg 4-amidinobenzylamide
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Lys 4-amidinobenzylamide
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Arg 4-amidinobenzylamide
-
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-lysinamide
-
-
N2-phenylacetyl-Ala-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Arg-Val-Arg 4-amidinobenzylamide
-
N2-phenylacetyl-Arg-Val-Arg 4-amidinobenzylamide
-
Nalpha(carbamidoyl)Arg-Arg-Val-Arg 4-amidinobenzylamide
-
nona-L-arginine
-
most potent inhibitor
Octapeptidyl chloromethane inhibitor
-
potent irreversible inhibitor
-
p-chloromercuribenzenesulfonic acid
-
-
PenLen (rSAAS-(221-2546))
-
neuroendocrine protein proSAAS-derived peptide
Peptidyl chloroalkyl ketones
Phe-Pro-Arg-chloromethylketone
-
poor inhibitor
phenylacetyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Thr-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
a competitive, noncovalent inhibitor, binding structure, overview
phenylacetyl-Arg-Val-Arg-4-aminomethyl-benzamidine
-
phenylacetyl-Cit-Arg-Val-Arg-4-aminomethyl-benzamidine
-
phenylmethanesulfonyl fluoride
phenylmethylsulfonyl fluoride
-
-
Pro-Gly-Lys-Arg-CH2Cl
-
-
pro-hepcidin
-
hydrolytic activity of membrane furin against the fluorescent substrate Boc-RVRR-7-amino-4-methyl-coumarin is reduced by approximately 50% in presence of 2 micromol pro-hepcidin and completely abolished in presence of 5 micromol pro-hepcidin
-
profurin 39-62 DYYHFWHRGVKRSLSPHRPRHSR
-
-
profurin 48-62 VTKRSLSPHRPRHSR
-
peptide derived from proprotein convertase 1/3
profurin 54-62 SPHRPRHSR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62 NHYLFKHKSHPRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62/A NAYLF KAKSAPRRSRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-62 RRSRR SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 55-62 SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 55-62/A SALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 74-83 QQYEKERSKR
-
peptide derived from proprotein convertase 1/3
SAAS-(235-244)
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P1'A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P2'A
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P3A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P3AP5A
-
neuroendocrine protein proSAAS-derived peptide
tosyl-Lys chloromethyl ketone
Zn(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
[Cu(2,2':6,2''-terpyridine)Cl2] (OCl4)
-
IC50: 0.0069 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
alpha1-antitrypsin
-
incorporation of furin recognition sequences within the reactive site loop of alpha1-antiprypsin leads to the production of furin inhibitors, construction of a series of alpha1-antitrypsin mutants by modifying the P7-P1 region of the reactive site loop
-
alpha1-antitrypsin
-
in cells overexpressing alpha1-antitrypsin, mRNA level of furin is reduced
-
alpha1-antitrypsin
-
not inhibited by normal antitrypsin M
-
alpha1-antitrypsin
-
type Pittsburgh as well as wild type
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-PDX
-
-
-
alpha1-PDX
-
a furin- and PC6-selective inhibitor, blocks cleavage of furin minimal consensus motifs, and of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase
-
antipain
-
-
antipain
-
minimal inhibition of ectodomain shedding
antithrombin
-
not
-
Arg-oxime
-
-
brefeldin A
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
brefeldin A
-
inhibits the secretion of furin
Ca2+
-
5-10 mM inhibit; activation below
Ca2+
-
100 mM; activation below
Ca2+
-
100 mM; activation below
CDTA
-
-
chymostatin
-
-
chymostatin
-
minimal inhibition of ectodomain shedding
Cu2+
-
IC50: 0.014 mM
CuSO4
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
efficiently inhibits ectodomain shedding by 95%
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
20 micromol results in a decrease in processed sol-membrane type-1 matrix metalloproteinase, significant decrease in motility compared to control cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
most inhibitory, inhibits Cryptosporidium parvum infection of HCT-8 cells in a dose-dependent manner, with ca. 50% inhibition occurring at a concentration of 0.01 mM
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin protease inhibitor, significantly diminishes secretion of S-tag-containing cysteine-rich FGF receptor products
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
significantly blocks the processing of ADAMTS4 in HEK-293 cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks cleavage of the first and second motifs in human hepatoma cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
fully blocks the substrate cleavage by the wild-type enzyme
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks furin activity, 99% inhibition of parathyroid hormone-related peptide maturation
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin inhibitor, pro-hepcidin activity is abolished
decanoyl-RVKR-chloromethyl ketone
-
-
decanoyl-RVKR-chloromethyl ketone
-
inhibition of furin inhibits processing of pro-B-type natriuretic peptide
decanoyl-RVKR-chloromethyl ketone
-
-
decanoyl-RVKR-chloromethyl ketone
-
furin inhibitor, inhibits E3E2 cleavage. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
decanoyl-RVKR-chloromethylketone
-
the furin inhibitor reduces DHBV infection of primary duck hepatocytes
decanoyl-RVKR-chloromethylketone
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
moderately
EDTA
-
-
EDTA
-
97% inhibition, Ca2+ can reverse the inhibitory effect
EDTA
-
completely inhibits
Eglin c
-
engineered variants
Eglin c
-
engineered variants
EGTA
-
-
hexa-D-arginine
-
-
hexa-D-arginine
-
blocks furin activity, 85% inhibition of parathyroid hormone-related peptide maturation
Hg2+
-
-
HgCl2
-
-
iodoacetamide
-
about 50% inhibition
iodoacetamide
about 50% inhibition
leupeptin
-
-
leupeptin
-
minimal inhibition of ectodomain shedding
Lys-Arg chloromethyl ketone
-
-
Lys-Arg chloromethyl ketone
-
-
NaCl
-
600 mM
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Peptidyl chloroalkyl ketones
-
-
Peptidyl chloroalkyl ketones
-
-
phenylmethanesulfonyl fluoride
-
-
phenylmethanesulfonyl fluoride
-
not
phenylmethanesulfonyl fluoride
-
moderately
phenylmethanesulfonyl fluoride
-
not
siRNA
-
-
-
siRNA
-
furin mRNA knockdown, pro-hepcidin activity is diminished
-
tosyl-Lys chloromethyl ketone
-
-
tosyl-Lys chloromethyl ketone
-
-
TPRARRRKKRT
-
-
Zn2+
-
-
Zn2+
-
IC50: 0.021 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
ZnCl2
-
-
additional information
-
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
cell-permeable, small-molecule compound, which inhibits at 15 micromol furin-mediated cleavage of pro-membrane type-1 matrix metalloproteinase, resulting in an almost complete inhibition of matrix metalloprotease-2-related cell motility in CHO cells
-
additional information
-
aprotinin has no effect on furin-like protease activity
-
additional information
-
a potent inhibitor containing a ketomethylene arginyl pseudopeptide bond; contains Cys near the active site His
-
additional information
-
not: pepstatin
-
additional information
-
Boc-RVRR-4-methylcoumarin-7-amide does not show any signs of substrate inhibition
-
additional information
-
the prodomain exhibits inhibitory action toward furin
-
additional information
-
siRNA-mediated depletion of endogenous c-Jun NH2-terminal kinase-interacting leucine zipper protein (JLP) or phosphoinositide kinase for position 5 containing a five finger domain (PIKfyve), profoundly delays microtubule-based transport of chimeric furin (Tac-furin) from endosomes to the trans-Golgi network in a CHO cell line, which is rescued upon ectopic expression of siRNA-resistant JLP or PIKfyve constructs
-
additional information
-
cell-permeable, small-molecule compound, which inhibits furin-mediated cleavage of pro-membrane type-1 matrix metalloproteinase, resulting in a 50% decrease in the invasiveness of the HT1080 cell
-
additional information
-
expression of furin in HaCaT cells declines with respect to time in response to UV radiation irrespective of the type or the dose used
-
additional information
-
O-glycosylation of substrate proBNP in the cleavage site region at Thr71 reduces furin cleaving activity, overview
-
additional information
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
-
EC values of furin inhibitors, overview. Inhibition of cell-surface PA83 processing in cell-based assays, overview
-
additional information
-
synthetic aromatic enediyne derivatives and their effects on protease activity of proprotein convertases furin, overview
-
additional information
peptidomimetic compounds based on a phenylacetyl-Arg-Val-Arg-4-(amidomethyl)benzamidine core structure belong to the strongest noncovalent enzyme inhibitors. Upon variation of the P5 position, dramatic changes of the Ki values are observed that cannot be explained by the known recognition motive. The Ki improves by approximately 2 orders of magnitude after addition of basic substituents, e.g., by modification of the Phac-moiety at P5 by a m- or p-guanidinomethyl group. Structure-guided drug design, overview
-
additional information
-
peptidomimetic compounds based on a phenylacetyl-Arg-Val-Arg-4-(amidomethyl)benzamidine core structure belong to the strongest noncovalent enzyme inhibitors. Upon variation of the P5 position, dramatic changes of the Ki values are observed that cannot be explained by the known recognition motive. The Ki improves by approximately 2 orders of magnitude after addition of basic substituents, e.g., by modification of the Phac-moiety at P5 by a m- or p-guanidinomethyl group. Structure-guided drug design, overview
-
additional information
active site distortions of human furin by a small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, analysis of binding structures of noncovalent 2,5-dideoxystreptamine-derived furin inhibitors, overview
-
additional information
-
active site distortions of human furin by a small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, analysis of binding structures of noncovalent 2,5-dideoxystreptamine-derived furin inhibitors, overview
-
additional information
analysis of the interactions of P4-P6 of furin with substrate-like peptide inhibitors using X-ray crystallography, substrate specificity is mediated at these binding sites, docking study, detailed overview
-
additional information
inhibitor constructuion, synthesis, and structure-function analysis, overview. Evaluation of inhibition of alphavirus propagation and inhibition of diphtheria toxin action
-
additional information
development of specific inhibitors of furin, synthesis of several truncated analogues of the bicyclic sunflower trypsin inhibitor (SFTI-1), or of compounds by various head-to-tail, head-to-side chain, and side-chain-to-tail cyclizations within multibasic octapeptides, or of several cationic cyclized peptides with cell-penetrating properties, overview. Inhibitory potency of these compounds is determined in enzyme kinetic assays with furin. Inhibitor docking study, crystal structure determination, and structure-function analysis. Modeling of furin in complex with inhibitors N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide, diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate, diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate, and diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate. Inhibition of respiratory syncytial virus propagation in A549 cells
-
additional information
no inhibition of human furin by DFP, 4-(2-aminoethyl)benzensulfonylfluorid (AEBSF), and PMSF
-
additional information
-
not: pepstatin
-
additional information
-
soluble hemojuvelin is reduced in cells treated with a furin inhibitor
-
additional information
-
pepstatin A, 1,10-ortho-phenanthroline, EDTA, or TAPI-0 do not inhibit ectodomain shedding
-
additional information
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
-
design of specific small molecule inhibitors targeting furi, overview
-
additional information
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
compounds 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(2-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(3-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(3-guanidinopyridin-4-yloxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-2,4-bis(2-amino-1H-benzo[d]imidazol-6-yloxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(pyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide and (1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(2-guanidinophenylcarbamate) do not inhibit
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.03
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
-
0.0038
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH
-
-
0.00039 - 0.00042
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00021 - 0.0012
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0003 - 0.0032
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00038 - 0.0027
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0002 - 0.00022
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00028 - 0.00037
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00005 - 0.0001
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00028 - 0.0052
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00033 - 0.0014
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0001
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0002 - 0.0065
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0012 - 0.0122
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00039 - 0.00041
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0155
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00022
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00023
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00041 - 0.00049
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00007
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00015 - 0.00045
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00014 - 0.005
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00086 - 0.00416
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00053
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0123
Ac-Arg-Val-Arg-Arg-4-nitroanilide
-
-
0.016
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.008
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.345
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide
-
-
0.0015
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.005
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.106
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.001
acetyl-norleucineYKR-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
-
0.028
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.00194
acetyl-RVRR-4-methylcoumarin 7-amide
-
pH 7.0, 37°C
0.0071
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.0009
AcRARYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
0.0008
AcRYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
0.0006
AcRYRFKR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
0.019
Boc-RVRR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
0.01
Boc-RVRR-7-amido-4-methyl-coumarin
-
-
0.029
Boc-RVRR-7-amido-4-methylcoumarin
-
0.035
DSSARIRRNAKG
-
pH 7.0, 37°C
0.0059
Glu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate
-
-
0.00007 - 0.0013
hBMP-2 precursor protein
-
0.0014 - 0.0015
hBMP-4 precursor protein
-
0.00124
pERKTR-7-amido-4-methylcoumarin
-
0.005
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide
-
-
0.0002
pro-hADAM-15 protein
-
pH 7.0, 37°C
-
0.00055
pro-hADAM-TS 4 protein
-
pH 7.0, 37°C
-
0.0004
pro-hADAM-TS 6 protein
-
pH 7.0, 37°C
-
0.0091
pro-hADAMTS-17 protein
-
pH 7.0, 37°C
-
0.0067
pro-hADAMTS-23 protein
-
pH 7.0, 37°C
-
0.0001
pro-hTGF-best1 protein, pro-hTGF-beta2 protein
-
pH 7.0, 37°C
-
0.00014
pro-hTGF-beta3 protein
-
pH 7.0, 37°C
-
0.0022
pro-hTGF-beta4 protein
-
pH 7.0, 37°C
-
0.00015
pro-MT-MMP 1 protein
-
pH 7.0, 37°C
-
0.00011
pro-MT-MMP 11 protein, pro-MT-MMP 3 protein
-
pH 7.0, 37°C
-
0.00045
pro-MT-MMP 4 protein
-
pH 7.0, 37°C
-
0.00037
pro-MT-MMP 6 protein
-
pH 7.0, 37°C
-
0.00064
proaerolysin
-
pH 7.0, 37°C
-
0.002
protective antigen
-
(-Arg-Lys-Lys-Arg-Ser-Thr-Ser-Ala-Gly-)
-
0.0118
Pseudomonas toxin
-
pH 7.0, 37°C
-
0.0032
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide
-
pH 7.5, 37°C
0.0026
Shiga toxin
-
pH 7.0, 37°C
-
0.01517
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.0156
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
-
-
0.000036 - 0.000122
viral precursor protein E3E2
-
additional information
additional information
-
0.00039
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00042
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00021
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0012
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0003
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0032
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00038
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0027
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0002
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00022
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00028
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00037
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00005
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0001
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00028
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0052
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00033
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0014
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0001
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0001
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0002
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0065
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0012
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0122
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00039
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00041
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0155
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0155
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00022
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00022
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00023
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00023
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00041
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00049
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00007
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00007
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00015
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00045
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00014
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.005
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00086
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00416
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00053
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00053
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00007
hBMP-2 precursor protein
-
first cleavage site, pH 7.0, 37°C
-
0.0013
hBMP-2 precursor protein
-
second cleavage site, pH 7.0, 37°C
-
0.0014
hBMP-4 precursor protein
-
second cleavage site, pH 7.0, 37°C
-
0.0015
hBMP-4 precursor protein
-
first cleavage site, pH 7.0, 37°C
-
0.000036
viral precursor protein E3E2
-
R64A mutant peptide of E3E2 from Asian Chikungunya virus strain
-
0.000122
viral precursor protein E3E2
-
wild-type E3E2 from Asian Chikungunya virus strain
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
upon increase of the pH from 6.0 to 9.0, KM-decreases linearly up to pH 7.5 and then remains constant
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
29.3
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH
-
-
29.6 - 30.3
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
3.6 - 4.2
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
28.9 - 39.5
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
6.3 - 6.9
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
7.6 - 12.2
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
9.2 - 14.9
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.6 - 3.1
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
0.61 - 6.7
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
2 - 3.5
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
2.6 - 12.3
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
8.4 - 11.3
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
5.3 - 8.7
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
12.2 - 14.6
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
5
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2.4 - 6.7
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
1 - 7.6
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
10.5 - 18.3
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
0.21 - 2.4
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
9.2 - 9.9
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
10 - 11.1
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
5.6 - 7.1
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
16.4 - 19.8
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
0.000934
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.02
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.0507
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide
-
-
0.00111
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.0403
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.00159
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
50
acetyl-norleucine-YKR-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.00088
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.7
acetyl-RVRR-4-methylcoumarin 7-amide
-
pH 7.0, 37°C
0.00135
acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-7-amido-4-methylcoumarin
-
-
-
250
AcRARYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
193
AcRYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
200
AcRYRFKR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
21
Boc-RVRR-4-methylcoumarin-7-amide
-
pH 7.0, 37°C
0.003
Boc-RVRR-7-amido-4-methylcoumarin
-
3 - 3.6
hBMP-2 precursor protein
-
3.6 - 5.6
hBMP-4 precursor protein
-
0.008
pERKTR-7-amido-4-methylcoumarin
-
5.5
pro-hADAM-15 protein
-
pH 7.0, 37°C
-
4.5
pro-hADAM-TS 4 protein
-
pH 7.0, 37°C
-
40
pro-hADAM-TS 6 protein
-
pH 7.0, 37°C
-
1
pro-hADAMTS-17 protein, pro-hADAMTS-23 protein
-
pH 7.0, 37°C
-
1.5
pro-hTGF-beta1 protein
-
pH 7.0, 37°C
-
3.4
pro-hTGF-beta2 protein
-
pH 7.0, 37°C
-
8.4
pro-hTGF-beta3 protein
-
pH 7.0, 37°C
-
1.2
pro-hTGF-beta4 protein
-
pH 7.0, 37°C
-
2.4
pro-MT-MMP 1 protein
-
pH 7.0, 37°C
-
1.3
pro-MT-MMP 11 protein
-
pH 7.0, 37°C
-
0.5
pro-MT-MMP 3 protein
-
pH 7.0, 37°C
-
5.5
pro-MT-MMP 4 protein
-
pH 7.0, 37°C
-
0.84
pro-MT-MMP 6 protein
-
pH 7.0, 37°C
-
12.2
proaerolysin
-
pH 7.0, 37°C
-
11
protective antigen
-
(-Arg-Lys-Lys-Arg-Ser-Thr-Ser-Ala-Gly-)
-
0.54
Pseudomonas toxin
-
pH 7.0, 37°C
-
16
Shiga toxin
-
pH 7.0, 37°C
-
0.192
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
-
-
additional information
additional information
-
29.6
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
30.3
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3.6
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
4.2
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
28.9
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
39.5
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
6.3
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
6.9
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
7.6
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
12.2
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
9.2
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
14.9
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.6
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3.1
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.61
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
6.7
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3.5
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2.6
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
12.3
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
8.4
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
11.3
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
5.3
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
8.7
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
12.2
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
14.6
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
2.4
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
6.7
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
7.6
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
10.5
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
18.3
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.21
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
2.4
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
9.2
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
9.9
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
10
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
11.1
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
5.6
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
7.1
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
16.4
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
19.8
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
3
hBMP-2 precursor protein
-
second cleavage site, pH 7.0, 37°C
-
3.6
hBMP-2 precursor protein
-
first cleavage site, pH 7.0, 37°C
-
3.6
hBMP-4 precursor protein
-
second cleavage site, pH 7.0, 37°C
-
5.6
hBMP-4 precursor protein
-
first cleavage site, pH 7.0, 37°C
-
additional information
additional information
-
-
-
additional information
additional information
-
over the pH intercal 6.0 to 9.0 kcat occurs as a bell-shaped form with a maximum at pH 7.0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70550 - 77100
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
3085 - 20190
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
9031 - 116100
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
2354 - 17730
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
38300 - 55640
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
32430 - 40270
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
6000 - 53450
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
1303 - 2184
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
1470 - 10610
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
1555 - 123000
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
1291 - 56300
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
710 - 4383
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
29660 - 37510
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
322
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
797 - 30500
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
606 - 33040
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
25360 - 37350
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
559 - 33860
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
20470 - 66000
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
1992 - 76230
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
1707 - 6488
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
28360 - 37360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
361
acetyl-RVRR-4-methylcoumarin 7-amide
-
pH 7.0, 37°C
2331 - 50710
hBMP-2 precursor protein
-
2649 - 3700
hBMP-4 precursor protein
-
27600
pro-hADAM-15 protein
-
pH 7.0, 37°C
-
8127
pro-hADAM-TS 4 protein
-
pH 7.0, 37°C
-
100000
pro-hADAM-TS 6 protein
-
pH 7.0, 37°C
-
109
pro-hADAMTS-17 protein
-
pH 7.0, 37°C
-
143
pro-hADAMTS-23 protein
-
pH 7.0, 37°C
-
14700
pro-hTGF-beta1 protein
-
pH 7.0, 37°C
-
34200
pro-hTGF-beta2 protein
-
pH 7.0, 37°C
-
60140
pro-hTGF-beta3 protein
-
pH 7.0, 37°C
-
534
pro-hTGF-beta4 protein
-
pH 7.0, 37°C
-
15800
pro-MT-MMP 1 protein
-
pH 7.0, 37°C
-
11450
pro-MT-MMP 11 protein
-
pH 7.0, 37°C
-
4545
pro-MT-MMP 3 protein
-
pH 7.0, 37°C
-
12670
pro-MT-MMP 4 protein
-
pH 7.0, 37°C
-
2240
pro-MT-MMP 6 protein
-
pH 7.0, 37°C
-
20670
proaerolysin
-
pH 7.0, 37°C
-
45
Pseudomonas toxin
-
pH 7.0, 37°C
-
6134
Shiga toxin
-
pH 7.0, 37°C
-
70550
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
77100
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3085
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
20190
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
9031
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
116100
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
2354
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
17730
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
38300
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
55640
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
32430
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
40270
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
6000
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
53450
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1303
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2184
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
1470
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
10610
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1555
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
123000
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1291
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
56300
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
710
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
4383
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
29660
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
37510
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
797
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
30500
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
606
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
33040
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
25360
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
37350
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
559
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
33860
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
20470
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
66000
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1992
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
76230
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1707
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
6488
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
28360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
37360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2331
hBMP-2 precursor protein
-
second cleavage site, pH 7.0, 37°C
-
50710
hBMP-2 precursor protein
-
first cleavage site, pH 7.0, 37°C
-
2649
hBMP-4 precursor protein
-
second cleavage site, pH 7.0, 37°C
-
3700
hBMP-4 precursor protein
-
first cleavage site, pH 7.0, 37°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.001768
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(3-guanidinophenylcarbamate)
-
-
0.000812
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
-
-
0.00000099
(1S,14S,17S,20S,23S,26S,33r)-26-amino-N-(4-carbamimidoylbenzyl)-20,23-bis(3-guanidinopropyl)-17-neopentyl-4,8,16,19,22,25,32-heptaoxo-3,9,15,18,21,24,31-heptaazabicyclo[31.2.2]heptatriacontane-14-carboxamide
pH and temperature not specified in the publication
0.0000013
(D-Arg)9-amide
-
-
0.000046
1-[(1R,2R,4S,5S)-2,4-bis(4-carbamimidamidophenoxy)-5-[(4-carbamimidamidophenyl)amino]cyclohexyl]guanidine
-
-
0.000423
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
-
-
0.0000089
11-amino-undecanoyl-RARRRKKRT
-
pH 7.5, 37°C
0.000169
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
-
-
0.000404
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000089
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000022
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000069
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000012
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000042
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000006
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.012
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
with CPA95 as substrate/with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.0033
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
0.00104
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
0.1851
3,3'-((2-bromophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0783
3,3'-((2-chlorophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.022
3,3'-((3,4,5-trimethoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0208
3,3'-((4-isopropoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.00605
3,3'-(benzo[d][1,3]dioxol-5-ylmethylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0188
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
2
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0000025
3-guanidinomethylphenylacetyl-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000000224
4-aminomethyl-phenylacetyl-Arg-Tle-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
1.3
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
7.3
4-Hydroxycoumarin
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0000083
8-amino-octanoyl-RARRRKKRT
-
pH 7.5, 37°C
0.000019
Ac-Ac-RQIKIWFQNRRMKWKKRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000228
Ac-AGYLLGKINLKALAALAKKILRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0024
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH2
-
pH 7.0, 37°C
0.0053
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Leu-NH2
-
pH 7.0, 37°C
0.007
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Arg-NH2
-
pH 7.0, 37°C
0.0227
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Leu-NH2
-
pH 7.0, 37°C
0.0103
Ac-HHKRRR-NH2
-
pH 7.0, 37°C
0.0021
Ac-HRKRRR-NH2
-
pH 7.0, 37°C
0.0052
Ac-KHKRRR-NH2
-
pH 7.0, 37°C
0.0016
Ac-KRKRRR-NH2
-
pH 7.0, 37°C
0.0132
Ac-MHKRRR-NH2
-
pH 7.0, 37°C
0.0023
Ac-MRKRRR-NH2
-
pH 7.0, 37°C
0.0034
Ac-RHKRRR-NH2
-
pH 7.0, 37°C
0.0013
Ac-RRKRRR-NH2
-
pH 7.0, 37°C
0.0000107
Ac-RRRRRRRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000011
Ac-YGRKKRRQRRRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000065
acetyl-RARRRKKRT
-
pH 7.5, 37°C
0.00239
acetyl-Val-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0024
acetyl-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.0035
AcLLRVKR
-
pH 7.0, 37°C
0.0000094
Arg-Arg-Arg-Arg-Arg-Arg
pH and temperature not specified in the publication
0.000006
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
pH and temperature not specified in the publication
0.0000093
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
pH and temperature not specified in the publication
0.0000000754
Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000337
Arg-Arg-Arg-Val-Arg-4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000000000337
Arg-Arg-Arg-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.0000000119
Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000574
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.000009
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000151
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000383
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0042
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000152
cholyl-RARRRKKRT
-
pH 7.5, 37°C
0.0000278
cyclo[(Arg)10]
pH and temperature not specified in the publication
0.0001104
cyclo[(Arg)6]
pH and temperature not specified in the publication
0.0000227
cyclo[(Arg)8]
pH and temperature not specified in the publication
0.00000068
cyclo[glutaryl-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000504
cyclo[glutaryl-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.00000105
cyclo[glutaryl-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000146
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000154
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000000538
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000136
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000378
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000618
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000000943
D-Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.000000491
D-Arg-Arg-Tle-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000062
D-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.000000108
D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.00000011
D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000378
D-Arg-D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000078
eglin c mutant Arg replaced with Asp at P3
-
pH 7.5, 37°C
-
0.000023
eglin c mutant D42R, eglin c mutant L45R, eglin variant M1 RVTR
-
pH 7.5, 37°C
-
0.0000016
eglin variant M2 RVKR
-
pH 7.5, 37°C
-
0.00092
eglin variant M3 RVTRDERY
-
pH 7.5, 37°C
-
0.0003
eglin variant M4 RVTRDRRY
-
pH 7.5, 37°C
-
0.0000078
eglin variant M5 RVTRDLDY
-
pH 7.5, 37°C
-
0.000047
eglin variant M6 RVTRDLRR
-
pH 7.5, 37°C
-
0.000039
eglin variant M7 RVTRDLRE
-
pH 7.5, 37°C
-
0.00002
eglin variant M8 RVTRDARY
-
pH 7.5, 37°C
-
0.000068
hepta-L-arginine
-
pH 7.0, 37°C
0.000106
hexa-D-arginine
-
pH 7.0, 37°C
0.000156
hfurin25-107
-
pH 7.4, 37°C, versus N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide
-
0.0000000538
human proteinase inhibitor 8
-
pH 7.5, 37°C
-
0.00042
LLRVKR
-
pH 7.0, 37°C
0.0008 - 0.0034
LLRVKR-NH2
0.000000491
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 4-[4-(2-amino-2-oxoethyl)piperazin-1-yl]butanamide bridged)
pH and temperature not specified in the publication
0.00000504
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]butanediamide bridged)
pH and temperature not specified in the publication
0.00000117
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]pentanediamide bridged)
pH and temperature not specified in the publication
0.1452
methyl 4-(bis(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl)benzoate
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0118
N''-[(1E)-[2-[(4-chlorobenzyl)oxy]phenyl]methylidene]carbonohydrazonic diamide
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.00058
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-2-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenoxy]acetamide
-
pH 7.0,22°C
0.00046
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
pH 7.0,22°C
0.00104
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
pH 7.0,22°C
0.00113
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-N'-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]propanediamide
-
pH 7.0,22°C
0.000000193
N2(carbamidoyl)Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.000000449
N2(carbamidoyl)Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0002693
N2-(3-aminomethyl-phenylacetyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000459
N2-(5-(guanidino)valeroyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.00000126 - 0.0000385
N2-(5-aminopentanoyl)-Val-Arg 4-amidinobenzylamide
0.0000267
N2-(5-guanidinopentanoly)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.00302
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-aminopropyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000063
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00749
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-aminobutyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000078
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidamidobutyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00000081
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000553
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-aminopentyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00107
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-carbamimidamidopentyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00971
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(piperidin-4-ylmethyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000053
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00132
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(aminomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00273
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(carbamimidamidomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000627
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(aminomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00143
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(carbamimidamidomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.0000000786
N2-acetyl-D-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
pH 7.0, 22°C
0.000001
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000164
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000482
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Lys 4-amidinobenzylamide
pH 7.0, 22°C
0.0000378
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.000000164
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
pH 7.0, 22°C
0.0000016
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.0000033
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-lysinamide
-
pH 7.0, temperature not specified in the publication
0.000000051
N2-phenylacetyl-Ala-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000283
N2-phenylacetyl-Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000337
N2-phenylacetyl-Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000491
N2-phenylacetyl-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000563
N2-phenylacetyl-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000138
Nalpha(carbamidoyl)Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.00004 - 0.000042
nona-L-arginine
0.000061
octa-L-arginine
-
pH 7.0, 37°C
0.0193
PenLen (rSAAS-(221-246))
-
pH 7.4, 37°C
-
0.00099
penta-L-arginine
-
pH 7.0, 37°C
0.0000367
phenylacetyl-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.000006
phenylacetyl-Arg-Thr-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.00000081
phenylacetyl-Arg-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.000238
phenylacetyl-Cit-Arg-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.0009
profurin 39-62 DYYHFWHRGVKRSLSPHRPRHSR
-
pH 7.0, 25°C
0.0028
profurin 48-62 VTKRSLSPHRPRHSR
-
pH 7.0, 25°C
0.023
profurin 54-62 SPHRPRHSR
-
pH 7.0, 25°C
0.0007 - 0.0154
proPC1/3 39-62 NHYLF KHKSHPRRSALAITKR
0.0012
proPC1/3 39-62/A NAYLF KAKSAPRRSRRSALAITKR
-
pH 7.0, 25°C
0.0023
proPC1/3 50-62 RRSRR SALHITKR
-
pH 7.0, 25°C
0.0048
proPC1/3 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
pH 7.0, 25°C
0.0316
proPC1/3 55-62 SALHITKR
-
pH 7.0, 25°C
0.013
proPC1/3 55-62/A SALAITKR
-
pH 7.0, 25°C
0.0475
proPC1/3 74-83 QQYEKERSKR
-
pH 7.0, 25°C, competitive inhibition
0.000008
RARRRKKRT
-
pH 7.5, 37°C
0.000261
SAAS-(235-244)
-
pH 7.4, 37°C
0.0394
SAAS-(235-246)
-
pH 7.4, 37°C
-
0.00128
SAAS-(235-246)P1'A
-
pH 7.4, 37°
0.0044
SAAS-(235-246)P2'A
-
pH 7.4, 37°C
-
0.092
SAAS-(235-246)P3A
-
pH 7.4, 37°C
0.000114 - 0.0064
tetra-L-arginine
0.000038
TPQRARRRKKRF
-
-
0.000033
TPQRARRRKKRT
-
-
0.000034
TPQRARRRKKRW
-
-
0.000047
TPQRARRRKKRY
-
-
additional information
additional information
-
0.0008
LLRVKR-NH2
-
pH 7.0, 37°C
0.0034
LLRVKR-NH2
-
pH 7.0, 37°C
0.00000126
N2-(5-aminopentanoyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000385
N2-(5-aminopentanoyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.00004
nona-L-arginine
-
pH 7.0, 37°C
0.000042
nona-L-arginine
-
pH 7.0, 37°C
0.0007
proPC1/3 39-62 NHYLF KHKSHPRRSALAITKR
-
pH7.0, 25°C
0.0154
proPC1/3 39-62 NHYLF KHKSHPRRSALAITKR
-
pH 7.0, 25°C
0.000114
tetra-L-arginine
-
pH 7.0, 37°C
0.0064
tetra-L-arginine
-
pH 7.0, 37°C
0.000023
TPRARRRKKRT
-
-
0.000023
TPRARRRKKRT
-
pH 7.5, 37°C
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
Ki-values of alpha1-antitrypsin and alpha1-antichymotrypsin mutants obtained by incorporation of furin recognition sequences within the reactive site loop of the molecule and modifying the P7-P1 region of the reactive site loop
-
additional information
additional information
Ki values of the inhibitors with inhibition constants above 0.1 nM are determined by fitting of the data to the equation for classical reversible competitive inhibition
-
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evolution
-
molecular evolution of enzyme function in the proprotein convertase family, overview
evolution
-
PC members are paralogous genes derived from a common ancestor, which represents independent lineages by gene replication in evolution. Abalone PC1 is located in PC1 clade which is orthologous genes in different species. The potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
evolution
furin is a member of the pro-hormone/pro-protein convertase family of subtilisin-like endoproteinases
evolution
-
furin is a member of the proprotein convertase family
evolution
furin is a member of the proprotein convertase family
evolution
-
furin is a member of the subtilisin-like proteases and belongs to the proprotein convertase subtilisin/kexin-like proteases, subgroup PCSK3
evolution
-
phylogenetic analysis and sequence comparisons. Differences may exist between furin proteases present in fruit bats compared to furins in other mammalian species, and these differences may impact protease usage for viral glycoprotein processing. Subtle differences in cellular distribution and localization of furin or trafficking through trans-Golgi network may exist between different mammalian species
evolution
the enzyme belongs to the family of serine proteases
evolution
the enzyme belongs to the proprotein convertase family of proteases
evolution
the enzyme is a member of the subtilisin-like proprotein convertase family
evolution
four of nine conserved proprotein convertases (PCs), including furin, Pace4, PC5A/B, and PC7, cleave substrates after the minimal dibasic recognition motif (K/R)-(X)n-(K/R)Y, where n is 0, 2, 4, or 6 and X can be any amino acid. In 152 PC sequences examined across species, the catalytic sites are 95% identical
evolution
furin belongs to the family of Ca2+-dependent proprotein convertases (PCs), all of which contain a subtilisin-like serine protease domain. Furin and the other six basic PCs, i.e. PC1, PC2, PC4, PACE4, PC5, and PC7, cleave their substrates at multibasic sequences mainly after arginine, whereas the nonbasic PC site-1 protease (S1P) cleaves preferentially after leucine, valine, or isoleucine
evolution
furin belongs to the proprotein convertase subtilisin/kexin (PCSK) family of enzymes play a crucial role in processing and trafficking of a wide variety of precursor proteins such as hormones, receptors, and enzymes
evolution
furin is a member of the prototypical PC family
malfunction
-
blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain, overview
malfunction
-
furin inhibition leads to a 38% reduction of oocyte release from ovaries, overview
malfunction
-
furin is involved in many physiological and pathological processes
malfunction
-
furin is linked to cancer, tumorgenesis, and viral and bacterial pathogenesis
malfunction
-
furin or a furin-like proprotein convertase facilitates duck hepatitis B virus, DHBV, infection by cleaving both the docking receptor and the viral large envelope protein
malfunction
-
inhibition of furin inhibits processing of pro-B-type natriuretic peptide
malfunction
ablation of productive infectious bronchitis virus, IBV, infection by knockdown of furin expression in H1299 cells
malfunction
-
furin inhibition reduces brain-derived neurotrophic factor maturation and secretion
malfunction
-
furin siRNA significantly increases apoptosis of the granulosa cells from large antral/preovulatory follicles, in part via downregulation of the anti-apoptotic proteins, XIAP and p-AKT. On the contrary, furin siRNA markedly decreases proliferation of granulosa cells based on the downregulation of proliferation cell nuclear antigen
malfunction
furin siRNAs upregulate HIF-1alpha protein under normoxic condition to a level similar to that obtained by cobalt chloride treatment, eventually leading to activation of VEGF-A synthesis in two human head and neck squamous cell carcinoma cell lines. HIF-1alpha induction of the enzyme siRNAs and either cobalt chloride or the 26S ribosome inhibitor, MG-132, suggesting a post-transcriptional enzyme-mediated regulation, the induction by siRNAs is inhibited by a specific IGF-1R signaling inhibitor
malfunction
furin-specific siRNAs or inhibitors inhibit cell fusion in choriocarcinoma BeWo cells, as well as trophoblast syncytialization in human placental explants
malfunction
knockdown of the enzyme expression in C8161.9, MelJuSo, and HeLa cells by shRNA leads to reduced or complete loss of KISS1 processing
malfunction
-
placenta-specific knockdown of furin in the mouse leads to severe defects in syncytialization and embryonic lethality, phenotype, overview
malfunction
an unbalanced activity of proprotein convertases is connected to pathologies like cancer, atherosclerosis, hypercholesterolaemia, and infectious diseases
malfunction
dysregulation of furin is implicated in numerous disease states, including cancer and fibrosis
malfunction
interleukin-2 is increased initially in furin-deficient mouse CD4+ T cells, but the T-cell receptor-induced interleukin-2 mRNA expression is not sustained in the absence of furin. Conditional deletion of FURIN in CD4+ T-cells leads to hyperactive T-cells and the overproduction of Th1 and Th2 cytokines and systemic autoimmunity as a result of the loss of Treg-mediated immunologic tolerance
malfunction
plant-produced human furin treated with PNGase F and Endo H does not exhibit cleavage activity. Similarly, when commercial human furin (NEB) is treated with commercial Endo H or PNGase F, no cleavage is observed for the substrate PA83
malfunction
Sema3B acts as a tumor suppressor in lung cancer and inhibits the formation of endothelial cells tubes in an in vitro angiogenesis. This function is abrogated upon mutation at the furin cleavage site. The C-terminal arginine of the putative furin cleavage site at the basic domain of Sema3C protein is critical for its functions in angiogenesis process
malfunction
the inhibition of furin in human Jurkat T cell lines also results in a decrease in interleukin-2 production, whereas the overexpression of wild-type furin is associated with elevated interleukin-2 levels
malfunction
the PLC motif in the cytosolic tail of proprotein convertase 7 (PC7) is dispensable for endosomal activity, but it is specifically required for trans-Golgi network (TGN) recycling and to rescue proactivin-A cleavage in furin-depleted B16-F1 melanoma cells. PC7 complements furin in cleaving Notch1 independently of PLC-mediated TGN access
malfunction
-
furin inhibition reduces brain-derived neurotrophic factor maturation and secretion
-
metabolism
cellular furin content might be a potential factor determining the susceptibility of cultured human and animal cells to coronavirus infectious bronchitis virus infection
metabolism
-
the enzyme activates large numbers of proprotein substrates and is ubiquitously expressed and implicated in many physiological and pathological processes
metabolism
all proprotein convertase (PC) activity detected in the trans-Golgi network/endosomal system of B16-F1 cells is mediated by furin, but not by endogenous PC7
metabolism
furin promotes the activation of T cell receptor-induced transcription factors
metabolism
furin-dependent transactivators in different mouse CD4+ T-cell subsets, overview
physiological function
-
bone morphogenetic proteins, BMPs, require proteolytic activation by members of the proprotein convertase family
physiological function
-
furin activation of the C-terminus of Sema3F produces a species that potently inhibits the binding of VEGF to neuropilin, the C-terminal neuropilin binding region of human Sema3F comprises residues 605-785. Furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, mechanism, overview
physiological function
-
furin and related proprotein convertases cleave the multibasic motifs R-X-R/K/X-R in the precursor proteins and, as a result, transform the latent proproteins into biologically active proteins and peptides
physiological function
-
furin cleavage of CD109 is necessary for its biological activity, CD109 negatively regulates transforming growth factor-beta signaling in keratinocytes by directly modulating receptor activity. Processing of CD109 into 180 kDa and 25kDa proteins by furin, followed by complex formation with the type I TGF-beta receptor is required for the regulation of TGF-beta signaling in cancer cells and keratinocytes
physiological function
-
furin is involved in many physiological and pathological processes, it plays a role in human trophoblast invasion and migration
physiological function
-
furin is responsible for the shedding of the endogenous (pro)renin receptor, (P)RR, it generates the soluble form of (P)RR, in cultured cells
physiological function
-
furin is responsible for the shedding of the endogenous (pro)renin receptor, (P)RR, it generates the soluble form of (P)RR, in cultured cells
physiological function
-
furin is responsible for the shedding of the endogenous (pro)renin receptor, (P)RR, it generates the soluble form of (P)RR, in cultured cells
physiological function
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proprotein convertase FurinA plays a role in zebrafish fin development and cell surface shedding of Fras1 and Frem2, large basement membrane proteins, thereby allowing proper localization of the proteins within the basement membrane of forming fins, mechanisms of basement membrane anchorage, overview
physiological function
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the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific, furin activates the luciferase activity 30fold
physiological function
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the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific, furin activates the luciferase activity 7fold
physiological function
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the enzyme plays a key role in the posttranslational processing of precursors for bioactive peptides
physiological function
expression of Dfurin1 enhances Sindbis virus titers in RPE.40 cells by a factor of 100-1000, and this increase correlates with efficient cleavage of PE2 glycoprotein
physiological function
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furin is involved in processing of bone morphogenetic protein BMP10. Processing occurs mostly intracellularly, but also at the cell surface
physiological function
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furin serves as an intermolecular chaperone for matrix metalloprotease MMP-28 secretion by interacting with the propeptide domain of MMP-28. cleavage of MMP-28 at the furin consensus sequence does not occur and proteolytic inactive furin is equally effective in enhancing MMP-28 secretion
physiological function
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hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells. Exposing these cells back to normoxic conditions reverses furin redistribution, suggesting that the tumor microenvironment modulates furin trafficking in a highly regulated manner. Both Rab4GTPase-dependent recycling and interaction of furin with the cytoskeletal anchoring protein, filami A, are essential for the cell surface relocalization of furin. Interference with the association of furin with filamin A, prevents cell surface relocalization of furin and abolishes the ability of cancer cells to migrate in response to hypoxia
physiological function
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in mice lacking furin in hepatocytes, the PCSK9-inactivated form is strongly reduced. Full-length, membrane-bound, but not soluble, furin is the cognate convertase which inactivates PCSK9 by cleavage at R218
physiological function
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fruit bat cells have homologues of cathepsin and furin proteases capable of cleaving and activating both the cathepsin-dependent Hendra virus F and the furin-dependent parainfluenza virus 5 F proteins, involvement of a furin protease in the cleavage of the PIV5 fusion protein, overview
physiological function
furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure, overview
physiological function
furin is involved in the secretory pathway. It is the major proprotein convertase required for KISS1-to-kisspeptin processing. KISS1 is a broadly functional secreted proprotein that is then processed into small peptides, termed kisspeptins
physiological function
furin is the major processing protease of the secretory pathway. GPR107 localizes to the trans-Golgi network and is essential for retrograde transport. It is cleaved by the endoprotease furin
physiological function
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furin is upregulated and cleaves certain substrates during hypoxia in cancer cells, the enzyme mediates brain-derived neurotrophic factor upregulation in cultured rat astrocytes exposed to oxygen-glucose deprivation. Maturation of brain-derived neurotrophic factor in astrocytes requires furin-mediated endoproteolytic processing of the precursor protein pro-brain-derived neurotrophic factor to brain-derived neurotrophic factor
physiological function
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furin may play an important role in regulating apoptosis and proliferation of granulosa cells, role of furin in the development of granulosa cells during folliculogenesis, overview
physiological function
furin mediates maturation of bone morphogenetic protein-4
physiological function
regulation of HIF-1 alpha, a major transcription factor involved in tumorigenesis by sensing intratumoral hypoxia, by the proprotein convertases furin and PC7 in human squamous carcinoma cells, overview. Furin is one of the numerous target genes regulated by HIF-1alpha transactivation and its distribution into endosomal compartments and onto the cell surface can be triggered by hypoxia via HIF-1alpha, overview
physiological function
the enzyme is necessary to promote the formation of higher order dendritic branches in PVD mechanosensory neurons and to ensure self-avoidance of sister branches, but is likely not required during maintenance of dendritic arbors. The enzyme also regulates the development of other neurons in all major neuronal classes in Caenorhabditis elegans, including aspects of branching and extension of neurites as well as cell positioning. The enzyme functions in a pathway with MNR-1/menorin, SAX-7/L1CAM and DMA-1 to control dendritic branch formation and extension of PVD neurons. The enzyme acts in concert with the menorin pathway to control branching and growth of somatosensory dendrites in PVD
physiological function
the furin expression level is directly proportional to the efficiency of hemagglutinin cleavage, with implications for viral spread in the host, activation mechanism of avian influenza virus H9N2 by furin, overview
physiological function
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the multinucleated syncytial trophoblast, which forms the outermost layer of the placenta and serves multiple functions, is differentiated from and maintained by cytotrophoblast cell fusion. Cytotrophoblast cell fusion and syncytialization are accompanied by furin expression. Processing of type 1 IGF receptor by furin is an essential mechanism for syncytialization. Furin function is required for the development of syncytiotrophoblast structure in the labyrinth layer, as well as for normal embryonic development
physiological function
the multinucleated syncytial trophoblast, which forms the outermost layer of the placenta and serves multiple functions, is differentiated from and maintained by cytotrophoblast cell fusion. Cytotrophoblast cell fusion and syncytialization are accompanied by furin expression. Processing of type 1 IGF receptor by furin is an essential mechanism for syncytialization. Furin function is required for the development of syncytiotrophoblast structure in the labyrinth layer, as well as for normal embryonic development
physiological function
activation of viral glycoproteins or bacterial toxins, furin and other PCs contribute to the propagation of certain pathogenic viruses and to the toxicity of some bacteria
physiological function
CRISPR editing reveals that both furin and PC7 are functional in B16-F1 cells and able to substitute for each other during Notch1 and ADAM10 precursor processing
physiological function
furin is a calcium-dependent serine endoprotease that processes a wide variety of proproteins involved in cell function and homeostasis
physiological function
furin is a ubiquitous proprotein convertase that is involved in the processing (activation) of a wide variety of precursor proteins, including blood coagulation factors, cell surface receptors, hormones and growth factors, viral envelope glycoproteins, etc. and plays a critical regulatory role in a wide variety of cellular events
physiological function
morula compaction and inner cell mass formation depend on PC7 and the related proteases Furin and Pace4. These proteases jointly regulate cell-cell adhesion mediated by E-cadherin processing during blastocyst formation
physiological function
proprotein convertase furin is a highly specific serine protease modifying and thereby activating proteins in the secretory pathway by proteolytic cleavage. Its substrates are involved in many diseases, including cancer and infections caused by bacteria and viruses
physiological function
proprotein convertase substilisin/kexin-type (PCSK) enzymes regulate proprotein maturation by catalyzing the proteolytic cleavage of their substrates. The prototype PCSK furin is induced upon T cell receptor (TCR) activation, and its expression in T cells is critical for the maintenance of peripheral immune tolerance. Proprotein convertase furin regulates T cell receptor-induced transactivation. TGF-beta1 and NOTCH1 are synthesized initially as inactive precursors and are proteolytically activated during T cell activation. In Jurkat cells, furin is dispensable for immediate T cell receptor (TCR) signaling steps, such as ERK, ZAP70, or LAT phosphorylation. Furin regulates the expression of interleukin-2 in human Jurkat T cell lines, specific TGF-beta1-independent role for furin in interleukin-2 regulation. Furin activates specifically and nonredundantly the anti-inflammatory cytokine pro-TGF-beta1 and thus, directly modulates the activity of CD4+ and CD8+ T cells. Importantly, Furin regulates its own activity by autocleavage, and its mRNA and protein levels are modulated dynamically during alterations in T cell physiology. Furin does not affect TCR-induced immediate phosphorylation events in Jurkat T cells
physiological function
proprotein convertase substilisin/kexin-type (PCSK) enzymes regulate proprotein maturation by catalyzing the proteolytic cleavage of their substrates. The prototype PCSK furin is induced upon T-cell receptor (TCR) activation, and its expression in T cells is critical for the maintenance of peripheral immune tolerance. Proprotein convertase furin regulates T cell receptor-induced transactivation. TGF-beta1 and NOTCH1 are synthesized initially as inactive precursors and are proteolytically activated during T-cell activation. In Jurkat cells, furin is dispensable for immediate T-cell receptor (TCR) signaling steps, such as ERK, ZAP70, or LAT phosphorylation. Furin regulates the expression of interleukin-2 in human Jurkat T-cell lines, specific TGF-beta1-independent role for furin in interleukin-2 regulation. Furin activates specifically and nonredundantly the anti-inflammatory cytokine pro-TGF-beta1 and thus, directly modulates the activity of CD4+ and CD8+ T-cells. Importantly, Furin regulates its own activity by autocleavage, and its mRNA and protein levels are modulated dynamically during alterations in T-cell physiology
physiological function
proprotein convertases (PCs) are highly specific proteases required for the proteolytic modification of many secreted proteins. Calcium-dependent activity regulation of furin
physiological function
transforming growth factor beta (TGF-beta) is a signalling molecule that plays a key role in developmental and immunological processes in mammals. Pro-TGF-beta forms homodimers and is further processed in the trans-Golgi by a furin protease. Proteolytic cleavage by furin separates mature TGF-beta from latency-associated peptide (LAP). This dimeric complex is called the small latency complex (SLC) and keeps mature TGF-beta in an inactive form. Furin requires multiple processing steps and correct localization within the secretory pathway to become active
physiological function
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furin is upregulated and cleaves certain substrates during hypoxia in cancer cells, the enzyme mediates brain-derived neurotrophic factor upregulation in cultured rat astrocytes exposed to oxygen-glucose deprivation. Maturation of brain-derived neurotrophic factor in astrocytes requires furin-mediated endoproteolytic processing of the precursor protein pro-brain-derived neurotrophic factor to brain-derived neurotrophic factor
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additional information
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alpha1-PDX blocks cleavage of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase, probably PC7, overview
additional information
enzyme modeling by molecular dynamics calculations. Furin shows a complex activation mechanism and exists in at least four defined states: (i) the off state, incompatible with substrate binding as seen in the unliganded enzyme; (ii) the active on state seen in inhibitor-bound furin; and the respective (iii) calcium-free and (iv) calcium-bound forms. The transition from the off to the on state is triggered by ligand binding at subsites S1 to S4 and appears to underlie the preferential recognition of the four-residue sequence motif of furin. Ligation by calcium at the PC-specific binding site II influences the active-site geometry and determines the rotamer state of the oxyanion hole-forming Asn295, and adds a second level of the activity modulation of furin. Analysis of substrate induced structural rearrangements of furin, the spatial restrictions at and around the catalytic serine residue 368 of furin are structurally reminiscent of typical trypsin-like proteases, overview. Hotspots of conformational changes include the catalytic residues His194, Ser368, Asn295 of the oxyanion hole, the sodium binding site (Thr309 and Ser316), and residues in direct contact with the inhibitor peptide (e.g. the region Ser253-Pro256, the alignment template). Mapping of the Calpha displacement to the surface of the structure induced by inhibitor binding reveals a concerted local rearrangement at the substrate-binding cleft
additional information
X-ray structures of the proprotein convertase furin bound with substrate analogue inhibitors reveal substrate specificity determinants beyond the S4 pocket, overview. Substrate specificity is mediated at the P4-P6 binding sites of furin
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