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Information on EC 2.4.2.36 - NAD+-diphthamide ADP-ribosyltransferase
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2.4.2.36 NAD+-diphthamide ADP-ribosyltransferaseIUBMB Comments
Diphtheria toxin and some other bacterial toxins catalyse this reaction, which inactivates translation elongation factor 2 (EF2). The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. cf. EC 2.4.2.31 NAD(P)+---protein-arginine ADP-ribosyltransferase. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii.
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Word Map
- 2.4.2.36
- camp
- cyclase
- vibrio
- mucosal
- pertussis
-
adp-ribosylation
- adenylate
- forskolin
-
retrograde
- gm1
- ganglioside
- aeruginosa
- enterotoxin
- iga
- agonist
-
tracer
-
dorsal
- prostaglandin
-
heat-labile
-
intranasal
-
dibutyryl
-
afferent
- isoproterenol
-
adenylyl
- g-proteins
-
innervation
-
gtp-binding
- diphtheria
- immunotoxins
-
anterograde
-
b-subunits
-
rostrally
-
toxigenic
-
ribosylation
- pilus
-
toxin-induced
-
toxin-sensitive
-
pyrogenic
- toxoid
- 8-bromo-camp
-
diarrheal
- antitoxin
-
ventrolateral
-
peyer
-
exoenzyme
-
enterotoxigenic
-
gppnhp
-
preganglionic
- drug development
-
wga-hrp
-
parabrachial
- medicine
- diagnostics
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
+
=
+
N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
Synonyms
cholera toxin, exotoxin a, adp-ribosyltransferase, mono-adp-ribosyltransferase, cholix toxin, cholix, ehtoxin-like, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-elongation factor 2
-
-
-
-
ADP-ribosyltransferase
-
-
-
-
cholera toxin
diphthamide-specific ADPRT
ExoA
exotoxin A
mono(ADPribosyl)transferase
-
-
-
-
NAD(+)-diphthamide ADP-ribosyltransferase
-
-
-
-
NAD-diphthamide ADP-ribosyltransferase
-
-
-
-
NAD-diphthamide ADP-ribosyltransferase NAD-elongation factor 2 ADP-ribosyltransferase
-
-
-
-
NAD:elongation factor 2-adenosine diphosphate ribose-transferase
-
-
-
-
cholera toxin
Vibrio cholerae serotype O1 569B
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD+ + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
pentosyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NAD+:diphthamide-[translation elongation factor 2] N-(ADP-D-ribosyl)transferase
Diphtheria toxin and some other bacterial toxins catalyse this reaction, which inactivates translation elongation factor 2 (EF2). The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. cf. EC 2.4.2.31 NAD(P)+---protein-arginine ADP-ribosyltransferase. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii.
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CAS REGISTRY NUMBER
COMMENTARY
52933-21-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + diphthamide-[Escherichia coli elongation factor Tu]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[Escherichia coli elongation factor Tu]
-
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
NAD+ + essential ribosomal elongation factor 2
nicotinamide + H+ + ADP-ribosylated essential ribosomal elongation factor 2
NAD+ + G-protein
?
-
NAD-dependent ADP-ribosylation of Arg201 of G-protein alpha-subunit, this locks the G-protein in its active state producing cAMP
-
-
?
NAD+ + peptide diphthamide
nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide
-
-
-
-
?
eEF2 + NAD+
eEF2 N-(ADP-D-ribosyl)diphthamide + NADH + H+
-
i.e. eukaryotic elongation factor 2, contains a post-translationally modified histidine residue, known as diphthamide, which is the specific ADP-ribosylation target of Pseudomonas aeruginosa exotoxin A
-
-
?
eEF2 + NAD+
eEF2 N-(ADP-D-ribosyl)diphthamide + NADH + H+
-
i.e. eukaryotic elongation factor 2 with a diphthamide-containing loop comprising residues Leu693-Gly703, ADP-ribosylation at His699, site determination by mass spectrometry and mutational analysis, overview
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
-
-
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
-
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
-
-
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
liver enzyme
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
i.e. elongation factor 2 of baby hamster kidney cells, forward ADP-ribosylation reaction is reversed by fragment A from Pseudomonas aeruginosa
-
r
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
-
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
-
-
r
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
NAD-glycohydrolase activity without acceptor substrate
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
reaction involves a random-order ternary complex
-
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
-
-
-
?
NAD+ + essential ribosomal elongation factor 2
nicotinamide + H+ + ADP-ribosylated essential ribosomal elongation factor 2
transfer of ADP-ribose moiety (oxocarbenium ion) of NAD+ onto N3 of diphthamide imidazole of essential ribosomal elongation factor 2 (eEF2)
-
-
?
NAD+ + essential ribosomal elongation factor 2
nicotinamide + H+ + ADP-ribosylated essential ribosomal elongation factor 2
essential ribosomal elongation factor 2: eEF2, 2-step reaction by concerted GH and ADPRT activity, transition-state model
-
-
?
additional information
?
-
NAD+-dependent ADP-ribosyltransfer (ADPRT) including NAD+-glycohydrolysis (GH) activity, deadly virulent due to covalent modification and thus inactivation of proteins that are essential for the host
-
-
?
additional information
?
-
-
NAD+-dependent ADP-ribosyltransfer (ADPRT) including NAD+-glycohydrolysis (GH) activity, deadly virulent due to covalent modification and thus inactivation of proteins that are essential for the host
-
-
?
additional information
?
-
no ADP-ribosyl transfer by mutants R551H and R551C despite of occurring NAD+-binding and hydrolysis
-
-
?
additional information
?
-
-
no ADP-ribosyl transfer by mutants R551H and R551C despite of occurring NAD+-binding and hydrolysis
-
-
?
additional information
?
-
-
cholera toxin activates mouse bone marrow mast cells to release interleukin-4 via activation of nucleotide oligomerisation domain 1 and toll-like receptor-4, and initiation of antigen-specific T-helper 2 response
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
eEF2 + NAD+
eEF2 N-(ADP-D-ribosyl)diphthamide + NADH + H+
-
i.e. eukaryotic elongation factor 2, contains a post-translationally modified histidine residue, known as diphthamide, which is the specific ADP-ribosylation target of Pseudomonas aeruginosa exotoxin A
-
-
?
NAD+ + diphthamide-[Escherichia coli elongation factor Tu]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[Escherichia coli elongation factor Tu]
-
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
NAD+ + essential ribosomal elongation factor 2
nicotinamide + H+ + ADP-ribosylated essential ribosomal elongation factor 2
transfer of ADP-ribose moiety (oxocarbenium ion) of NAD+ onto N3 of diphthamide imidazole of essential ribosomal elongation factor 2 (eEF2)
-
-
?
NAD+ + G-protein
?
-
NAD-dependent ADP-ribosylation of Arg201 of G-protein alpha-subunit, this locks the G-protein in its active state producing cAMP
-
-
?
NAD+ + peptide diphthamide
nicotinamide + peptide N-(ADP-D-ribosyl)diphthamide
-
-
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
-
-
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
-
-
-
?
NAD+ + diphthamide-[translation elongation factor 2]
nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
-
-
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
liver enzyme
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
i.e. elongation factor 2 of baby hamster kidney cells, forward ADP-ribosylation reaction is reversed by fragment A from Pseudomonas aeruginosa
-
r
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
-
-
?
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
-
-
r
NAD+ + elongation factor 2
nicotinamide + ADPribose-elongation factor 2
-
NAD-glycohydrolase activity without acceptor substrate
-
?
additional information
?
-
NAD+-dependent ADP-ribosyltransfer (ADPRT) including NAD+-glycohydrolysis (GH) activity, deadly virulent due to covalent modification and thus inactivation of proteins that are essential for the host
-
-
?
additional information
?
-
-
NAD+-dependent ADP-ribosyltransfer (ADPRT) including NAD+-glycohydrolysis (GH) activity, deadly virulent due to covalent modification and thus inactivation of proteins that are essential for the host
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[(5,6-dimethyl-4-oxo-3,4,4a,7a-tetrahydrothieno[2,3-d]pyrimidin-2-yl)sulfanyl]-N-(2-hydroxyethyl)acetamide
-
3-((3,3-diethylguanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 24% inhibition
3-((3,3-diisopropylguanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 94% inhibition
3-((3-(1-benzylpiperidin-4-yl)guanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 96% inhibition
3-((3-(1-benzylpyrrolidin-3-yl)guanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 68% inhibition
3-((3-(2-(ethyl(m-tolyl)amino)ethyl)guanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 76% inhibition
3-((3-(2-morpholinoethyl)guanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 57% inhibition
3-((3-(4-bromobenzyl)guanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 98% inhibition
3-((3-(4-methoxybenzyl)guanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 97% inhibition, not sufficient material for IC50 and Ki estimation
3-((3-benzylguanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 93% inhibition
3-((3-phenethylguanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 93% inhibition
3-((3-phenylguanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 57% inhibition
3-((3-tert-butylguanidino)methyl)benzamide
-
1 mM, 37°C, pH 7, 39% inhibition
3-(3,3-diisopropylguanidino)benzamide
-
1 mM, 37°C, pH 7, 15% inhibition
3-(3-(1-benzylpiperidin-4-yl)guanidino)benzamide
-
1 mM, 37°C, pH 7, 58% inhibition
3-(3-(4-bromobenzyl)guanidino)benzamide
-
1 mM, 37°C, pH 7, 22% inhibition
3-(3-benzylguanidino)benzamide
-
1 mM, 37°C, pH 7, 10% inhibition
3-(3-phenylguanidino)benzamide
-
1 mM, 37°C, pH 7, 12% inhibition
3-(3-tert-butylguanidino)benzamide
-
1 mM, 37°C, pH 7, 77% inhibition
8-fluoro-2-[3-(piperidin-1-yl)propanoyl]-1,3,4,5-tetrahydrobenzo[c][1,6]naphthyridin-6(2H)-one
-
ethyl 4-(3-(3-carbamoylbenzyl)guanidino)piperidine-1-carboxylate
-
1 mM, 37°C, pH 7, 34% inhibition
additional information
-
cellular ADPribosyltransferase is not inhibited by anti-fragment A-antiserum
-
additional information
-
fragment A and toxin A are not inhibited by histamine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation, together with SDS or guanidine hydrochloride
guanidine hydrochloride
-
enhances activity together with dithiothreitol, cysteine, 2-mercaptoethanol or sulfite
SDS
-
enhances activity together with dithiothreitol, cysteine, 2-mercaptoethanol or sulfite
additional information
-
exotoxin is synthesized in a catalytically inactive, proenzyme form, unfolding of the toxin molecule may cause activation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NAD+
double mutant E546A/R551A, relative KD = 1.11 +/-0.03
additional information
NAD+
-
double mutant E546A/R551A, relative KD = 1.11 +/-0.03
additional information
NAD+
double mutant E546D/R551K, relative KD = 2.71 +/-0.74
additional information
NAD+
-
double mutant E546D/R551K, relative KD = 2.71 +/-0.74
additional information
NAD+
double mutant E546R/R551E, relative KD = 1.29 +/-0.49
additional information
NAD+
-
double mutant E546R/R551E, relative KD = 1.29 +/-0.49
additional information
NAD+
mutant D461A, KD = 1.03 +/-0.02 relative to wild-type (c)
additional information
NAD+
-
mutant D461A, KD = 1.03 +/-0.02 relative to wild-type (c)
additional information
NAD+
mutant D463A, KD = 1.18 +/-0.04 relative to wild-type (c)
additional information
NAD+
-
mutant D463A, KD = 1.18 +/-0.04 relative to wild-type (c)
additional information
NAD+
mutant E546A, relative KD = 1.77 +/-0.34
additional information
NAD+
-
mutant E546A, relative KD = 1.77 +/-0.34
additional information
NAD+
mutant E546D, relative KD = 3.83 +/-0.89
additional information
NAD+
-
mutant E546D, relative KD = 3.83 +/-0.89
additional information
NAD+
mutant E546F, relative KD = 1.97 +/-0.11
additional information
NAD+
-
mutant E546F, relative KD = 1.97 +/-0.11
additional information
NAD+
mutant E546H, relative KD = 1.03 +/-0.09
additional information
NAD+
-
mutant E546H, relative KD = 1.03 +/-0.09
additional information
NAD+
mutant E546N, relative KD = 2.14 +/-0.26
additional information
NAD+
-
mutant E546N, relative KD = 2.14 +/-0.26
additional information
NAD+
mutant E546Q, relative KD = 2.31 +/-0.71
additional information
NAD+
-
mutant E546Q, relative KD = 2.31 +/-0.71
additional information
NAD+
mutant E547A, relative KD = 1.97 +/-0.77
additional information
NAD+
-
mutant E547A, relative KD = 1.97 +/-0.77
additional information
NAD+
mutant E548A, relative KD = 2.69 +/-0.11
additional information
NAD+
-
mutant E548A, relative KD = 2.69 +/-0.11
additional information
NAD+
mutant E553A, relative KD = 2.57 +/-0.86
additional information
NAD+
-
mutant E553A, relative KD = 2.57 +/-0.86
additional information
NAD+
mutant G453A, KD = 4.85 +/-1.07 relative to wild-type (c)
additional information
NAD+
-
mutant G453A, KD = 4.85 +/-1.07 relative to wild-type (c)
additional information
NAD+
mutant G454A, KD = 6.25 +/-0.22 relative to wild-type (c)
additional information
NAD+
-
mutant G454A, KD = 6.25 +/-0.22 relative to wild-type (c)
additional information
NAD+
mutant G549A, relative KD = 8.00 +/-0.94
additional information
NAD+
-
mutant G549A, relative KD = 8.00 +/-0.94
additional information
NAD+
mutant G550A, relative KD = 6.60 +/-0.54
additional information
NAD+
-
mutant G550A, relative KD = 6.60 +/-0.54
additional information
NAD+
mutant L462A, KD = 1.86 +/-0.10 relative to wild-type (c)
additional information
NAD+
-
mutant L462A, KD = 1.86 +/-0.10 relative to wild-type (c)
additional information
NAD+
mutant L552A, relative KD = 4.43 +/-0.57
additional information
NAD+
-
mutant L552A, relative KD = 4.43 +/-0.57
additional information
NAD+
mutant Q460A, KD = 4.30 +/-0.43 relative to wild-type (c)
additional information
NAD+
-
mutant Q460A, KD = 4.30 +/-0.43 relative to wild-type (c)
additional information
NAD+
mutant R456A, KD = 3.56 +/-0.53 relative to wild-type (c)
additional information
NAD+
-
mutant R456A, KD = 3.56 +/-0.53 relative to wild-type (c)
additional information
NAD+
mutant R458A, KD = 5.78 +/-0.18 relative to wild-type (c)
additional information
NAD+
-
mutant R458A, KD = 5.78 +/-0.18 relative to wild-type (c)
additional information
NAD+
mutant R458H, KD = 31.02 +/-7.18 relative to wild-type (d)
additional information
NAD+
-
mutant R458H, KD = 31.02 +/-7.18 relative to wild-type (d)
additional information
NAD+
mutant R458K, KD = 3.18 +/-0.23 relative to wild-type (c)
additional information
NAD+
-
mutant R458K, KD = 3.18 +/-0.23 relative to wild-type (c)
additional information
NAD+
mutant R458Q, KD = 0.45 +/-0.06 relative to wild-type (e)
additional information
NAD+
-
mutant R458Q, KD = 0.45 +/-0.06 relative to wild-type (e)
additional information
NAD+
mutant R458W, KD = 11.26 +/-1.16 relative to wild-type (d)
additional information
NAD+
-
mutant R458W, KD = 11.26 +/-1.16 relative to wild-type (d)
additional information
NAD+
mutant R551A, relative KD = 2.69 +/-0.03
additional information
NAD+
-
mutant R551A, relative KD = 2.69 +/-0.03
additional information
NAD+
mutant R551C, relative KD = 5.57 +/-0.91
additional information
NAD+
-
mutant R551C, relative KD = 5.57 +/-0.91
additional information
NAD+
mutant R551E, relative KD = 5.03 +/-0.51
additional information
NAD+
-
mutant R551E, relative KD = 5.03 +/-0.51
additional information
NAD+
mutant R551H, relative KD = 2.29 +/-0.46
additional information
NAD+
-
mutant R551H, relative KD = 2.29 +/-0.46
additional information
NAD+
mutant R551K, relative KD = 1.29 +/-0.03
additional information
NAD+
-
mutant R551K, relative KD = 1.29 +/-0.03
additional information
NAD+
mutant R551Q, relative KD = 2.63 +/-0.39
additional information
NAD+
-
mutant R551Q, relative KD = 2.63 +/-0.39
additional information
NAD+
mutant S459A, KD = 1.59 +/-0.16 relative to wild-type (c)
additional information
NAD+
-
mutant S459A, KD = 1.59 +/-0.16 relative to wild-type (c)
additional information
NAD+
mutant V455A, KD = 3.31 +/-0.24 relative to wild-type (c)
additional information
NAD+
-
mutant V455A, KD = 3.31 +/-0.24 relative to wild-type (c)
additional information
NAD+
wild-type, KD = 35 +/-3 microM, relative KD = 1.00 +/-0.09, estimated according to quenched intrinsic tryptophan fluorescence upon NAD+ binding to the active site
additional information
NAD+
-
wild-type, KD = 35 +/-3 microM, relative KD = 1.00 +/-0.09, estimated according to quenched intrinsic tryptophan fluorescence upon NAD+ binding to the active site
additional information
NAD+
wild-type, KD = 36 +/-8 microM (c), KD = 62 +/-2 microM (d), KD = 74 +/-16 microM, relative KD = 1.00 +/-0.03
additional information
NAD+
-
wild-type, KD = 36 +/-8 microM (c), KD = 62 +/-2 microM (d), KD = 74 +/-16 microM, relative KD = 1.00 +/-0.03
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
NAD+
0.0062-0.13/min, wild-type GH activity, in the absence of eEF2, pH 7.9, 25°C, 60 min
additional information
NAD+
-
0.0062-0.13/min, wild-type GH activity, in the absence of eEF2, pH 7.9, 25°C, 60 min
additional information
NAD+
0.125 +/-0.007/min (a), wild-type GH activity, in the absence of eEF2, pH 7.9, 25°C, 60 min
additional information
NAD+
-
0.125 +/-0.007/min (a), wild-type GH activity, in the absence of eEF2, pH 7.9, 25°C, 60 min
additional information
NAD+
0.130 +/-0.012/min (b), wild-type GH activity, in the absence of eEF2, pH 7.9, 25°C, 60 min
additional information
NAD+
-
0.130 +/-0.012/min (b), wild-type GH activity, in the absence of eEF2, pH 7.9, 25°C, 60 min
additional information
NAD+
1306 +/-121/min (a), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
-
1306 +/-121/min (a), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
1495 +/-224/min (b), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
-
1495 +/-224/min (b), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
628 +/-8/min (B), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
-
628 +/-8/min (B), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
746 +/-18/min (A), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
-
746 +/-18/min (A), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
847 +/-21/min (C), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
-
847 +/-21/min (C), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
900 +/-20/min (D), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
-
900 +/-20/min (D), wild-type ADPRT activity, 12 microM eEF2, pH 7.9, 25°C, 300 sec
additional information
NAD+
double mutant E546A/R551A, kcat = 0.0001 +/-0.0001, relative to wild-type ADPRT activity (C)
additional information
NAD+
-
double mutant E546A/R551A, kcat = 0.0001 +/-0.0001, relative to wild-type ADPRT activity (C)
additional information
NAD+
double mutant E546A/R551A, kcat = 0.84 +/-0.04, relative to wild-type GH activity
additional information
NAD+
-
double mutant E546A/R551A, kcat = 0.84 +/-0.04, relative to wild-type GH activity
additional information
NAD+
double mutant E546D/R551K, kcat = 0.0009 +/-0.0013, relative to wild-type ADPRT activity (C)
additional information
NAD+
-
double mutant E546D/R551K, kcat = 0.0009 +/-0.0013, relative to wild-type ADPRT activity (C)
additional information
NAD+
double mutant E546D/R551K, kcat = 0.42 +/-0.0002, relative to wild-type GH activity
additional information
NAD+
-
double mutant E546D/R551K, kcat = 0.42 +/-0.0002, relative to wild-type GH activity
additional information
NAD+
double mutant E546R/R551E, kcat = 0.00001 +/-0.000002, relative to wild-type ADPRT activity (C)
additional information
NAD+
-
double mutant E546R/R551E, kcat = 0.00001 +/-0.000002, relative to wild-type ADPRT activity (C)
additional information
NAD+
double mutant E546R/R551E, kcat = 0.38 +/-0.01, relative to wild-type GH activity
additional information
NAD+
-
double mutant E546R/R551E, kcat = 0.38 +/-0.01, relative to wild-type GH activity
additional information
NAD+
mutant D461A, kcat = 1.001 +/-0.091, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant D461A, kcat = 1.001 +/-0.091, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant D461A, kcat = 1.076 +/-0.041, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant D461A, kcat = 1.076 +/-0.041, relative to wild-type GH activity (a)
additional information
NAD+
mutant D463A, kcat = 1.148 +/-0.038, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant D463A, kcat = 1.148 +/-0.038, relative to wild-type GH activity (a)
additional information
NAD+
mutant D463A, kcat = 1.270 +/-0.204, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant D463A, kcat = 1.270 +/-0.204, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant E546A, kcat = 0.0012 +/-0.00002, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant E546A, kcat = 0.0012 +/-0.00002, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant E546A, kcat = 0.24 +/-0.008, relative to wild-type GH activity
additional information
NAD+
-
mutant E546A, kcat = 0.24 +/-0.008, relative to wild-type GH activity
additional information
NAD+
mutant E546D, kcat = 0.00025 +/-0.00005, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant E546D, kcat = 0.00025 +/-0.00005, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant E546D, kcat = 0.45 +/-0.002, relative to wild-type GH activity
additional information
NAD+
-
mutant E546D, kcat = 0.45 +/-0.002, relative to wild-type GH activity
additional information
NAD+
mutant E546F, kcat = 0.007 +/-0.0002, relative to wild-type ADPRT activity (D)
additional information
NAD+
-
mutant E546F, kcat = 0.007 +/-0.0002, relative to wild-type ADPRT activity (D)
additional information
NAD+
mutant E546F, kcat = 0.69 +/-0.05, relative to wild-type GH activity
additional information
NAD+
-
mutant E546F, kcat = 0.69 +/-0.05, relative to wild-type GH activity
additional information
NAD+
mutant E546H, kcat = 0.0012 +/-0.0002, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant E546H, kcat = 0.0012 +/-0.0002, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant E546H, kcat = 0.59 +/-0.009, relative to wild-type GH activity
additional information
NAD+
-
mutant E546H, kcat = 0.59 +/-0.009, relative to wild-type GH activity
additional information
NAD+
mutant E546N, kcat = 0.0010 +/-0.00009, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant E546N, kcat = 0.0010 +/-0.00009, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant E546N, kcat = 0.67 +/-0.03, relative to wild-type GH activity
additional information
NAD+
-
mutant E546N, kcat = 0.67 +/-0.03, relative to wild-type GH activity
additional information
NAD+
mutant E546Q, kcat = 0.011 +/-0.002, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant E546Q, kcat = 0.011 +/-0.002, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant E546Q, kcat = 0.80 +/-0.04, relative to wild-type GH activity
additional information
NAD+
-
mutant E546Q, kcat = 0.80 +/-0.04, relative to wild-type GH activity
additional information
NAD+
mutant E547A, kcat = 0.795 +/-0.077, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant E547A, kcat = 0.795 +/-0.077, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant E547A, kcat = 0.83 +/-0.14, relative to wild-type GH activity
additional information
NAD+
-
mutant E547A, kcat = 0.83 +/-0.14, relative to wild-type GH activity
additional information
NAD+
mutant E548A, kcat = 0.76 +/-0.01, relative to wild-type GH activity
additional information
NAD+
-
mutant E548A, kcat = 0.76 +/-0.01, relative to wild-type GH activity
additional information
NAD+
mutant E548A, kcat = 1.669 +/-0.298, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant E548A, kcat = 1.669 +/-0.298, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant E553A, kcat = 0.0015 +/-0.00005, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant E553A, kcat = 0.0015 +/-0.00005, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant E553A, kcat = 0.07 +/-0.009, relative to wild-type GH activity
additional information
NAD+
-
mutant E553A, kcat = 0.07 +/-0.009, relative to wild-type GH activity
additional information
NAD+
mutant G453A, kcat = 0.290 +/-0.040, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant G453A, kcat = 0.290 +/-0.040, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant G453A, kcat = 0.331 +/-0.019, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant G453A, kcat = 0.331 +/-0.019, relative to wild-type GH activity (a)
additional information
NAD+
mutant G454A, kcat = 0.031 +/-0.003, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant G454A, kcat = 0.031 +/-0.003, relative to wild-type GH activity (a)
additional information
NAD+
mutant G454A, kcat = 0.046 +/-0.008, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant G454A, kcat = 0.046 +/-0.008, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant G549A, kcat = 0.30 +/-0.005, relative to wild-type GH activity
additional information
NAD+
-
mutant G549A, kcat = 0.30 +/-0.005, relative to wild-type GH activity
additional information
NAD+
mutant G549A, kcat = 0.770 +/-0.076, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant G549A, kcat = 0.770 +/-0.076, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant G550A, kcat = 0.41 +/-0.04, relative to wild-type GH activity
additional information
NAD+
-
mutant G550A, kcat = 0.41 +/-0.04, relative to wild-type GH activity
additional information
NAD+
mutant G550A, kcat = 0.562 +/-0.166, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant G550A, kcat = 0.562 +/-0.166, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant L462A, kcat = 0.268 +/-0.041, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant L462A, kcat = 0.268 +/-0.041, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant L462A, kcat = 0.955 +/-0.015, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant L462A, kcat = 0.955 +/-0.015, relative to wild-type GH activity (a)
additional information
NAD+
mutant L552A, kcat = 0.58 +/-0.002, relative to wild-type GH activity
additional information
NAD+
-
mutant L552A, kcat = 0.58 +/-0.002, relative to wild-type GH activity
additional information
NAD+
mutant L552A, kcat = 2.365 +/-0.527, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant L552A, kcat = 2.365 +/-0.527, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant Q460A, kcat = 0.115 +/-0.010, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant Q460A, kcat = 0.115 +/-0.010, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant Q460A, kcat = 0.622 +/-0.014, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant Q460A, kcat = 0.622 +/-0.014, relative to wild-type GH activity (a)
additional information
NAD+
mutant R456A, kcat = 0.230 +/-0.010, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant R456A, kcat = 0.230 +/-0.010, relative to wild-type GH activity (a)
additional information
NAD+
mutant R456A, kcat = 0.239 +/-0.034, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant R456A, kcat = 0.239 +/-0.034, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant R458A, kcat = 0.132 +/-0.031, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant R458A, kcat = 0.132 +/-0.031, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant R458A, kcat = 0.249 +/-0.021, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant R458A, kcat = 0.249 +/-0.021, relative to wild-type GH activity (a)
additional information
NAD+
mutant R458H, kcat = 0.018 +/-0.003, relative to wild-type GH activity (b)
additional information
NAD+
-
mutant R458H, kcat = 0.018 +/-0.003, relative to wild-type GH activity (b)
additional information
NAD+
mutant R458H, kcat = 0.019 +/-0.007, relative to wild-type ADPRT activity (b)
additional information
NAD+
-
mutant R458H, kcat = 0.019 +/-0.007, relative to wild-type ADPRT activity (b)
additional information
NAD+
mutant R458K, kcat = 0.428 +/-0.033, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant R458K, kcat = 0.428 +/-0.033, relative to wild-type GH activity (a)
additional information
NAD+
mutant R458K, kcat = 0.543 +/-0.155, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant R458K, kcat = 0.543 +/-0.155, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant R458Q, kcat = 0.650 +/-0.130, relative to wild-type ADPRT activity (b)
additional information
NAD+
-
mutant R458Q, kcat = 0.650 +/-0.130, relative to wild-type ADPRT activity (b)
additional information
NAD+
mutant R458Q, kcat = 0.991 +/-0.017, relative to wild-type GH activity (b)
additional information
NAD+
-
mutant R458Q, kcat = 0.991 +/-0.017, relative to wild-type GH activity (b)
additional information
NAD+
mutant R458W, kcat = 0.379 +/-0.043, relative to wild-type ADPRT activity (b)
additional information
NAD+
-
mutant R458W, kcat = 0.379 +/-0.043, relative to wild-type ADPRT activity (b)
additional information
NAD+
mutant R458W, kcat = 0.438 +/-0.040, relative to wild-type GH activity (b)
additional information
NAD+
-
mutant R458W, kcat = 0.438 +/-0.040, relative to wild-type GH activity (b)
additional information
NAD+
mutant R551A, kcat = 0.32 +/-0.005, relative to wild-type GH activity
additional information
NAD+
-
mutant R551A, kcat = 0.32 +/-0.005, relative to wild-type GH activity
additional information
NAD+
mutant R551A, kcat = 0.380 +/-0.024, relative to wild-type ADPRT activity (A)
additional information
NAD+
-
mutant R551A, kcat = 0.380 +/-0.024, relative to wild-type ADPRT activity (A)
additional information
NAD+
mutant R551C, kcat = ~0, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant R551C, kcat = ~0, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant R551C, kcat = 0.10 +/-0.006, relative to wild-type GH activity
additional information
NAD+
-
mutant R551C, kcat = 0.10 +/-0.006, relative to wild-type GH activity
additional information
NAD+
mutant R551E, kcat = 0.011 +/-0.005, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant R551E, kcat = 0.011 +/-0.005, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant R551E, kcat = 0.09 +/-0.001, relative to wild-type GH activity
additional information
NAD+
-
mutant R551E, kcat = 0.09 +/-0.001, relative to wild-type GH activity
additional information
NAD+
mutant R551H, kcat = ~0, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant R551H, kcat = ~0, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant R551H, kcat = 0.41 +/-0.002, relative to wild-type GH activity
additional information
NAD+
-
mutant R551H, kcat = 0.41 +/-0.002, relative to wild-type GH activity
additional information
NAD+
mutant R551K, kcat = 0.317 +/-0.024, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant R551K, kcat = 0.317 +/-0.024, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant R551K, kcat = 0.69 +/-0.03, relative to wild-type GH activity
additional information
NAD+
-
mutant R551K, kcat = 0.69 +/-0.03, relative to wild-type GH activity
additional information
NAD+
mutant R551Q, kcat = 0.185 +/-0.014, relative to wild-type ADPRT activity (B)
additional information
NAD+
-
mutant R551Q, kcat = 0.185 +/-0.014, relative to wild-type ADPRT activity (B)
additional information
NAD+
mutant R551Q, kcat = 0.38 +/-0.01, relative to wild-type GH activity
additional information
NAD+
-
mutant R551Q, kcat = 0.38 +/-0.01, relative to wild-type GH activity
additional information
NAD+
mutant S459A, kcat = 1.119 +/-0.054, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant S459A, kcat = 1.119 +/-0.054, relative to wild-type GH activity (a)
additional information
NAD+
mutant S459A, kcat = 1.256 +/-0.144, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant S459A, kcat = 1.256 +/-0.144, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant V455A, kcat = 0.241 +/-0.032, relative to wild-type ADPRT activity (a)
additional information
NAD+
-
mutant V455A, kcat = 0.241 +/-0.032, relative to wild-type ADPRT activity (a)
additional information
NAD+
mutant V455A, kcat = 0.254 +/-0.001, relative to wild-type GH activity (a)
additional information
NAD+
-
mutant V455A, kcat = 0.254 +/-0.001, relative to wild-type GH activity (a)
additional information
NAD+
relative kcat = 1.00 +/-0.02, wild-type GH activity
additional information
NAD+
-
relative kcat = 1.00 +/-0.02, wild-type GH activity
additional information
NAD+
relative kcat = 1.00 +/-0.05, wild-type GH activity (a) and (b)
additional information
NAD+
-
relative kcat = 1.00 +/-0.05, wild-type GH activity (a) and (b)
additional information
NAD+
relative kcat = 1.00 +/-0.09, wild-type ADPRT activity (A)-(D), and (a) and (b)
additional information
NAD+
-
relative kcat = 1.00 +/-0.09, wild-type ADPRT activity (A)-(D), and (a) and (b)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
3-((3-(1-benzylpiperidin-4-yl)guanidino)methyl)benzamide
-
37°C, pH 7
0.008
3-((3-(4-bromobenzyl)guanidino)methyl)benzamide
-
37°C, pH 7, 1400fold more potent than NAD+ and 400fold more potent than diethylamino(benzylidine-amino)guanidine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.049
3-((3-(1-benzylpiperidin-4-yl)guanidino)methyl)benzamide
Vibrio cholerae serotype O1
-
37°C, pH 7
0.031
3-((3-(4-bromobenzyl)guanidino)methyl)benzamide
Vibrio cholerae serotype O1
-
37°C, pH 7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
polyoma virus transformed baby hamster kidney cells, i.e. pyBHK-cells
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme is an important virulence factor from Aeromonas pathogenic species
physiological function
the enzyme is an important virulence factor from Aeromonas pathogenic species
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DTX_CORBE
567
1
61602
Swiss-Prot
Secretory Pathway (Reliability: 3)
DTX_COROM
560
0
60815
Swiss-Prot
Secretory Pathway (Reliability: 2)
TOXA_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
638
0
69284
Swiss-Prot
-
A0A0H3AF77_VIBC3
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
258
0
29336
TrEMBL
-
G2Z7B4_FLABF
Flavobacterium branchiophilum (strain FL-15)
226
1
25494
TrEMBL
-
A0A2A5T6P7_9GAMM
256
1
28908
TrEMBL
-
A0A806GMP9_CORD7
Corynebacterium diphtheriae (strain ATCC 27012 / C7 (beta))
560
0
60815
TrEMBL
-
Q6NK15_CORDI
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
560
0
60815
TrEMBL
-
CHTA_VIBCH
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
258
0
29336
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
-
SDS-PAGE of purified recombinant fusion enzyme cholera toxin B subunit with glutamic acid carboxylase 65 peptides 531-545 with histidine 6 tag
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
catalytically active A subunit and five identical B subunits for receptor binding
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 12% (w/v) polyethylene glycol 6000, 0.1 M MES pH 5.5, 0.1 M ammonium acetate
in complex with NAD+ and eEF2, PDB: 3B8H (mutant E546A), 3B82 (mutant E546H), 3B78 (mutant R551H), 2ZIT (wild-type), specific interactions of active-site loop1 with NAD+ and diphthamide results in solvent cover for dinucleotide-binding pocket and coordinates and stabilizes NAD+ in the active-site cleft during ADPRT reaction (transition-state model), crystals are of space group P(1)2(1), C2 symmetry, unit cell parameters: a: 326.9-329.4, b: 68.1-69.2, c: 190.0-191.6, beta: 102.9-103.3°, precipitant: PEG-8K or PEG-10K, 6-8%, 1.25 mM NAD+ (in cryo-protection buffer, pH 6.0) soaked into crystals
a 1.8 A crystal structure of cholix in complex with its natural substrate, nicotinamide adenine dinucleotide
-
hanging drop vapor diffusion method, using 12% (w/v) polyethylene glycol 6000, 0.1 M MES pH 5.5, 0.1 M ammonium acetate
-
hanging drop vapor diffusion method, using 12% (w/v) polyethylene glycol 6000, 0.1 M MES pH 5.5, 0.1 M ammonium acetate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E571A
E546A
reduced ADPRT activity compared to wild-type possibly due to leakage of aqueous solvent into binding pocket which prevents ADP-ribose transfer, no impaired NAD+ binding and glycohydrolase activity, Glu546 crucial for ADPRT activity of ExoA but not strictly conserved among toxin family members, part of active-site loop 3 (546-551), upon NAD+-binding Glu546 and Tyr481 (both connected by hydrogen bonds resulting in water molecule exclusion) in hydrogen bonding distance to nucleophilic N3 of diphthamide imidazole possibly increasing its nucleophilic character
E546A/R551A
double alanine mutant, almost complete loss of ADPRT activity not restored by mutations E546D/R551K or E546R/R551E
E553A
impaired NAD+ binding and glycohydrolase activity, Glu553 is a crucial catalytic residue and conserved among toxin family members
G454A
Q460A
reduced ADPRT activity compared to wild-type, Gln460 is part of active-site loop 1 (453-463), active-site loop1 flips towards diphthamide of eEF2 by a hinged action of Ala457 and Ala464 upon NAD+ binding which places Gln460 close to adenine phosphate of NAD+, interaction of Gln460 with A-phosphate of NAD+ possibly prevents hydrolysis of NAD+ to AMP or ADP
R458A
56-fold reduction in ADPRT activity, 53-fold reduction in GH activity, and 31-fold increased KD for NAD+ compared to wild-type, ADPRT activity sensitivity towards substitution in order Gln>Lys>Trp>Ala>His, Arg458 is part of active-site loop 1 (453-463) and implicated in NAD+ substrate docking and orientation, active-site loop1 flips towards diphthamide of eEF2 by a hinged action of Ala457 and Ala464 upon NAD+ binding which enables van der Waals interactions between Arg458 and the adenine base of NAD+
R551A
ADPRT activity sensitive to replacements in order Ala>Lys>Gln>Glu>His>Cys, Arg551 is part of active-site loop 3 (546-551)
DELTA424-634
-
catalytic domain of cholix has much greater affinity for NAD+ than the full-length enzyme. 15fold higher ADP-ribosyltransferase activity than full-length enzyme
E574A
-
mutation of catalytic fragment DELTA424-634: mutant does not have a large impact on NAD+-binding. Catalytic activity is 3fold reduced compared to catalytic fragment DELTA424-634
E574A/E581A
-
mutation of catalytic fragment DELTA424-634: mutant has low affinity for NAD+. Mutant shows no catalytic activity
E579R
-
mutation of catalytic fragment DELTA424-634: NAD+ binding not changed significantly. Catalytic activity is 1.6fold reduced compared to catalytic fragment DELTA424-634
E581A
-
mutation of catalytic fragment DELTA424-634: mutant has low affinity for NAD+. Mutant shows no catalytic activity
Y493A
-
mutation of catalytic fragment DELTA424-634: mutation of catalytic fragment DELTA424-634: mutant has little effect on NAD+-binding. Mutant shows a marked reduction in activity compared to catalytic fragment DELTA424-634
Y504A
-
mutation of catalytic fragment DELTA424-634: mutant has little effect on NAD+-binding. Mutant shows a marked reduction in activity compared to catalytic fragment DELTA424-634
Y504F
-
mutation of catalytic fragment DELTA424-634: mutant has little effect on NAD+-binding. Mutant has lower affinity for NAD+ than Y504A mutant. Mutant shows a mild reduction in activity compared to catalytic fragment DELTA424-634
additional information
-
recombinant gene of cholera toxin B subunit with triple glutamic acid decarboxylase 65 peptides 531-545 (3p531) with 6-bp oligonucleotide sequences as flexible hinges
G454A
reduced ADPRT activity compared to wild-type, Gly454 is part of active-site loop 1 (453-463)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
0.2 microm crossflow microfiltration, concentrated and diafiltered against 10 mM phosphate buffer, pH 7.6, with 30 kDa crossflow ultrafiltration, toxin bound on a S 5/50 GL cation exchange column and eluted with a salt gradient of 10 mM potassium phosphate buffer, pH 7.0 with 1 M NaCl
-
adsorption on Ni-NTA resin column, washing and elution with buffer containing 500 mM imidazole, dialyzing in 2 steps
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) with expression vector pET28a
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
drug development
more potent therapeutics for treatment of bacterial diseases and infections through understanding of ADPRT reaction meachanism
medicine
-
therapy for autoimmune diabetes with glutamic acid decarboxylase 65 as autoantigen combined with cholera toxin B subunit as adjuvans lowering the number of antigens needed for autoimmune suppression, oral application for 5 weeks reduces insulitis of pancreas in mouse model
diagnostics
-
toxin purification and recognition to enable cost effective toxin free cholera vaccine production, detection minimum 1 ng/ml
diagnostics
Vibrio cholerae serotype O1 569B
-
toxin purification and recognition to enable cost effective toxin free cholera vaccine production, detection minimum 1 ng/ml
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, H.; Iglewski, W.J.
Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A
Proc. Natl. Acad. Sci. USA
81
2703-2707
1984
Bos taurus, Mesocricetus auratus, Pseudomonas aeruginosa
brenda
Sanai, Y.; Morihara, K.; Tsuzuki, H.; Homma, J.Y.; Kato, I.
Proteolytic cleavage of exotoxin A from Pseudomonas aeruginosa: formation of an ADP-ribosyltransferase active fragment by the action of Pseudomonas elastase
FEBS Lett.
120
131-134
1980
Pseudomonas aeruginosa
brenda
Leppla, S.H.; Martin, O.C.; Muehl, L.A.
The exotoxin P. aeruginosa: a proenzyme having an unusual mode of activation
Biochem. Biophys. Res. Commun.
81
532-538
1978
Pseudomonas aeruginosa
brenda
Armstrong, S.; Merrill, A.R.
Toward the elucidation of the catalytic mechanism of the mono-ADP-ribosyltransferase activity of Pseudomonas aeruginosa exotoxin A
Biochemistry
43
183-194
2004
Pseudomonas aeruginosa
brenda
Zhang, Y.; Liu, S.; Lajoie, G.; Merrill, A.R.
The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A
Biochem. J.
413
163-174
2008
Pseudomonas aeruginosa
brenda
Jorgensen, R.; Wang, Y.; Visschedyk, D.; Merrill, A.R.
The nature and character of the transition state for the ADP-ribosyltransferase reaction
EMBO Rep.
9
802-809
2008
Pseudomonas aeruginosa (P11439), Pseudomonas aeruginosa
brenda
Zhang, G.
Design, synthesis, and evaluation of bisubstrate analog inhibitors of cholera toxin
Bioorg. Med. Chem. Lett.
18
3724-3727
2008
Vibrio cholerae serotype O1
brenda
Feng, B.S.; Zheng, P.Y.; Chen, X.; Liao, X.Q.; Yang, P.C.
Investigation of the role of cholera toxin in assisting the initiation of the antigen-specific Th2 response
Immunol. Invest.
37
782-797
2008
Vibrio cholerae serotype O1
brenda
Jang, H.; Kim, H.S.; Kim, J.A.; Seo, J.H.; Carbis, R.
Improved purification process for cholera toxin and its application to the quantification of residual toxin in cholera vaccines
J. Microbiol. Biotechnol.
19
108-112
2009
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 569B
brenda
Gong, Z.; Long, X.; Pan, L.; Le, Y.; Liu, Q.; Wang, S.; Guo, J.; Xiao, B.; Zhou, M.; Mei, D.
Cloning, expression, purification and characterization of the cholera toxin B subunit and triple glutamic acid decarboxylase epitopes fusion protein in Escherichia coli
Protein Expr. Purif.
191
191-197
2009
Vibrio cholerae serotype O1
brenda
Fieldhouse, R.J.; Jurgensen, R.; Lugo, M.R.; Merrill, A.R.
The 1.8 A cholix toxin crystal structure in complex with NAD+ and evidence for a new kinetic model
J. Biol. Chem.
287
21176-21188
2012
Vibrio cholerae serotype O1
brenda
Lugo, M.R.; Merrill, A.R.
The father, son and cholix toxin: The third member of the dt group mono-ADP-ribosyltransferase toxin family
Toxins
7
2757-2772
2015
Pseudomonas aeruginosa (P11439), Pseudomonas aeruginosa, Vibrio cholerae (Q5EK40), Vibrio cholerae
brenda
Avila, E.E.; Rodriguez, O.I.; Marquez, J.A.; Berghuis, A.M.
An Entamoeba histolytica ADP-ribosyl transferase from the diphtheria toxin family modifies the bacterial elongation factor Tu
Mol. Biochem. Parasitol.
207
68-74
2016
Entamoeba histolytica (C4LWB1), Entamoeba histolytica
brenda
Masuyer, G.
Crystal structure of exotoxin A from Aeromonas pathogenic species
Toxins
12
397
2020
Aeromonas hydrophila
brenda
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