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1,Nepsilon-etheno-ADP-ribose + H2O
1,Nepsilon-etheno-AMP-ribose + phosphate
-
fluorogenic substrate
the product is converted to fluorescent 1,Nepsilon-etheno-adenosine by alkaline phosphatase for detection
-
?
2''-O-acetyl-ADP-ribose + H2O
AMP + 2-O-acetyl-D-ribose 5-phosphate
-
-
-
-
?
8-oxo-dADP + H2O
?
-
-
-
?
8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
-
-
-
?
8-oxo-dGDP + H2O
?
-
-
-
?
8-oxo-dGTP + H2O
?
the enzyme hardly acts on 8-oxo-dGTP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP-alpha-D-ribose + H2O
AMP + D-ribose 5-phosphate
ADP-D-ribose + H2O
AMP + D-ribose 5-phosphate
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
ADP-ribose + H2O
AMP + ribose 5-phosphate
ADPribose + H2O
AMP + D-ribose 5-phosphate
ADPribose 2'-phosphate + H2O
adenosine 2',5'-diphosphate + D-ribose 5-phosphate
-
-
-
-
?
cADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP + phosphate
CDP-choline + H2O
CMP + choline phosphate
CDP-choline + H2O
CMP + phosphocholine
reaction of EC 3.6.1.53
-
-
?
CDP-ethanolamine + H2O
CMP + ethanolamine phosphate
-
-
-
?
CDP-glucose + H2O
CMP + glucose 5-phosphate
-
at 5% of the activity with ADPribose
-
-
?
CDP-glycerol + H2O
CMP + glycerol phosphate
-
-
-
?
CDP-ribose + H2O
CMP + D-ribose 5-phosphate
-
kcat/Km is 2.5% of the kcat/Km for ADP-ribose
-
-
?
cyclic ADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP
-
-
-
?
diadenosine 5',5''-diphosphate + H2O
?
20% the activity with ADP-ribose
-
-
?
GDP-glucose + H2O
GMP + glucose 5-phosphate
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
GDP-ribose + H2O
GMP + D-ribose 5-phosphate
-
kcat/Km is 3% of the kcat/Km for ADP-ribose
-
-
?
IDP-ribose + H2O
IMP + D-ribose 5-phosphate
-
138% of the activity with ADPribose
-
-
?
IDP-ribose + H2O
IMP + ribose 5-phosphate
IDPribose + H2O
IMP + D-ribose 5-phosphate
77% of the activity with ADPribose
-
-
?
NAD+ + H2O
?
-
ADPRibase-Mn in presence of Mn2+, no activity with ADPRibase I and ADPRibase II
-
-
?
NAD+ + H2O
AMP + NMN
7% of the activity with ADP-ribose
-
-
?
NADP+ + H2O
nicotinic acid mononucleotide + phosphate
-
-
-
?
NADPH + H2O
AMP + ?
12% of the activity with ADP-ribose
-
-
?
UDP-galactose + H2O
UDP + galactose
7% of the activity with ADP-ribose
-
-
?
UDP-glucose + H2O
UMP + glucose 5-phosphate
UDP-mannose + H2O
UMP + D-mannose 1-phosphate
additional information
?
-
2',3'-cAMP + H2O
3'AMP
-
95% of products
-
?
2',3'-cAMP + H2O
3'AMP
-
-
-
?
ADP-alpha-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-alpha-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADP-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADP-glucose + H2O
?
low activity
-
-
?
ADP-glucose + H2O
?
low activity
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
at 21% of the activity with ADPribose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
56% of the activity with ADP-ribose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
about 70% of the activity with ADP-mannose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
about 70% of the activity with ADP-ribose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
ADPRibase II, very low activity with ADPRibase I
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
9% of the activity with ADPribose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
kcat/Km is 3% of the kcat/Km for ADP-ribose
-
-
?
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
-
-
-
?
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
-
at 70% of the activity with ADPribose
-
-
?
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
103% of the activity with ADP-ribose
-
-
?
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
-
about 80% of the activity with ADP-ribose
-
-
?
ADP-mannose + H2O
AMP + D-mannose 1-phosphate
-
ADPRibase II, low activity with ADPRibase I
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
Growth Factor Gene 1 (GFG1, At4g12720) encodes a nudix hydrolase, that is an NADH pyrophosphatase and ADP-ribose pyrophosphatase
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
AtNUDT10 shows both ADP-ribose and NADH pyrophosphatase activity
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
AtNUDT2 shows both ADP-ribose and NADH pyrophosphatase activity
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
AtNUDT6 shows both ADP-ribose and NADH pyrophosphatase activity
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
AtNUDT7 shows both ADP-ribose and NADH pyrophosphatase activity
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
substrate binding structure, overview
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
preferred substrate
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may have a predominant role in free ADP-ribose turnover and as a protective agent preventing the accumulation of this potential dangerous metabolite
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
protective enzyme whose function is to limit the intracellular accumulation of ADP-ribose
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
the enzyme plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5?-phosphate
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
ADP-ribose pyrophosphatase Sll1054 hydrolyzes ADP-ribose specifically
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
ADP-ribose pyrophosphatase Slr0920 hydrolyzes ADP-ribose specifically
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
ADP-ribose pyrophosphatase Slr1134 hydrolyzes ADP-ribose, NADH and flavin adenine dinucleotide
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
substrate binding structure, overview
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme plays a key role in regulating the intracellular ADPribose levels, and prevents nonenzymatic ADP-ribosylation
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
highly specific substrate
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
interactions responsible for the substrate recognition are located at the terminal moieties of the substrate. The adenine moiety is recognized by Ile-19 and the main chain carbonyl group of Glu-29 and/or Gly-104. The terminal ribose moiety is recognized by the sum of some weak interactions with multiple residues that are close in space. Glu-82 and Glu-86 are essential for catalysis but unlikely to act as a catalytic base. Two-metal ion mechanism for the catalysis of ADPRase in which a water molecule is activated to act as a nucleophile by the cations coordinated by Glu-82 and Glu-86. Arg-54, Glu-70, Arg-81, and Glu-85 are predicted to support this nucleophilic attack on the R-phosphate of the substrate
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
preferred substrate, substrate recognition and binding structure, overview
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme plays a key role in regulating the intracellular ADPribose levels, and prevents nonenzymatic ADP-ribosylation
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
highly specific substrate
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
preferred substrate, substrate recognition and binding structure, overview
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
-
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
the function of the enzyme might be to remove free ADP-ribose arising from NAD+ and protein-bound poly- and non-enzymic protein glycation
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
about 65% of the activity with ADP-mannose
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
ADP-ribose is a better substrate compared with 8-oxo-dGDP
-
-
?
ADP-ribose + H2O
AMP + ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
nucleophilic attack at the adenosyl phosphate. The enzyme cycles between an open free enzyme and a closed substrate-metal complex conformation. This cycling may be important in preventing nonspecific hydrolysis of other nucleotides
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play an important role in the regulation of intracellular steady-state of free ADPribose
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
-
-
?
cADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP + phosphate
-
-
-
?
cADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP + phosphate
-
-
-
?
CDP-choline + H2O
CMP + choline phosphate
-
-
-
?
CDP-choline + H2O
CMP + choline phosphate
-
-
-
?
FAD + H2O
?
-
ADPRibase-Mn and ADPRibase II, very low activity with ADPRibase I in presence of Mn2+
-
-
?
FAD + H2O
?
preferred substrate
-
-
?
FAD + H2O
?
preferred substrate
-
-
?
GDP-glucose + H2O
GMP + glucose 5-phosphate
7% of the activity with ADP-ribose
-
-
?
GDP-glucose + H2O
GMP + glucose 5-phosphate
about 15% of the activity with ADP-mannose
-
-
?
GDP-glucose + H2O
GMP + glucose 5-phosphate
-
about 15% of the activity with ADP-ribose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
-
-
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
at 59% of the activity with ADPribose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
-
at 40% of the activity with ADPribose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
about 15% of the activity with ADP-mannose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
-
about 20% of the activity with ADP-ribose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
-
at 9% of the activity with ADPribose
-
-
?
GDP-mannose + H2O
GMP + D-mannose 1-phosphate
-
at 1% of the activity with ADPribose
-
-
?
IDP-ribose + H2O
IMP + ribose 5-phosphate
-
77% of the activity with ADPribose
-
-
?
IDP-ribose + H2O
IMP + ribose 5-phosphate
-
at 59% of the activity with ADPribose
-
-
?
IDP-ribose + H2O
IMP + ribose 5-phosphate
9% of the activity with ADP-ribose
-
-
?
IDP-ribose + H2O
IMP + ribose 5-phosphate
-
-
-
-
?
NADH + H2O
?
-
-
-
?
NADH + H2O
?
at 2% of the activity with ADPribose
-
-
?
NADH + H2O
?
-
at 9% of the activity with ADPribose
-
-
?
NADH + H2O
?
at 15% of the activity with ADPribose
-
-
?
NADH + H2O
?
-
ADPRibase I, ADPribase II and ADPRibase-Mn in presence of Mn2+
-
-
?
NADH + H2O
?
-
at 12% of the activity with ADPribose
-
-
?
NADH + H2O
AMP + NMNH
-
-
-
?
NADH + H2O
AMP + NMNH
-
-
-
?
NADH + H2O
AMP + NMNH
7% of the activity with ADP-ribose
-
-
?
NADH + H2O
AMP + NMNH
about 12% of the activity with ADP-mannose
-
-
?
NADH + H2O
AMP + NMNH
-
about 15% of the activity with ADP-ribose
-
-
?
UDP-glucose + H2O
UMP + glucose 5-phosphate
-
at 5% of the activity with ADPribose
-
-
?
UDP-glucose + H2O
UMP + glucose 5-phosphate
about 12% of the activity with ADP-mannose
-
-
?
UDP-glucose + H2O
UMP + glucose 5-phosphate
-
about 5% of the activity with ADP-ribose
-
-
?
UDP-mannose + H2O
UMP + D-mannose 1-phosphate
-
at 20% of the activity with ADPribose
-
-
?
UDP-mannose + H2O
UMP + D-mannose 1-phosphate
about 15% of the activity with ADP-mannose
-
-
?
UDP-mannose + H2O
UMP + D-mannose 1-phosphate
-
about 5% of the activity with ADP-ribose
-
-
?
additional information
?
-
no or very poor substrates: ADP-glucose, UDP-glucose, CDP-glucose, CDP, CMP, AMP, and 3',5'-cAMP
-
-
?
additional information
?
-
-
no or very poor substrates: ADP-glucose, UDP-glucose, CDP-glucose, CDP, CMP, AMP, and 3',5'-cAMP
-
-
?
additional information
?
-
the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose diphosphatase, NMN specificity of the enzyme, overview
-
-
?
additional information
?
-
-
the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose diphosphatase, NMN specificity of the enzyme, overview
-
-
?
additional information
?
-
-
no activity with ADPglucose, ADPmannose, UDPglucose
-
-
?
additional information
?
-
-
hNUDT5 can utilize a variety of ADP-sugar conjugates as substrate, with a preference for ADPR
-
-
?
additional information
?
-
hNUDT5 can utilize a variety of ADP-sugar conjugates as substrate, with a preference for ADPR
-
-
?
additional information
?
-
ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cyclic ADP-ribose (cADPR) phosphohydrolase with much lower efficiency than on its major substrates
-
-
-
additional information
?
-
-
three diphosphatases: 1.ADPRibase-I: an ADP-ribose diphosphatase highly specific for ADPribose and IDPribose in presence of Mg2+, but active also on non-reducing ADP-hexoses and dinucleotides, not on NAD+, when Mg2+ is replaced with Mn2+, 2. ADPRibase-Mn: a Mn2+-dependent diphosphatase active on ADPribose and IDPribose, dinucleotides and CDP alcohols, 3. ADPribase-II: a rather unspecific diphosphatase that, with Mg2+, is active on AMP or IMP containing NDP sugars and dinucleotides, not on NAD+, and with Mn2+ also active on non-adenine NDP-sugars and CDP-alcohols
-
-
?
additional information
?
-
the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose diphosphatase, NMN specificity of the enzyme, overview
-
-
?
additional information
?
-
-
the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose diphosphatase, NMN specificity of the enzyme, overview
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.045
2''-O-acetyl-ADP-ribose
-
at pH 7.5 and 37°C
0.0035 - 0.0038
8-oxo-dGDP
0.0209 - 0.3213
ADP-D-ribose
3.16
ADP-glucose
-
25°C, pH 7.6, wild-type enzyme
0.083 - 0.154
ADP-mannose
0.46
ADPribose 2'-phosphate
-
-
3.9 - 31
CDP-ethanolamine
1.36
CDP-ribose
-
25°C, pH 7.6, wild-type enzyme
1.1
GDP-ribose
-
25°C, pH 7.6, wild-type enzyme
additional information
additional information
-
0.76
2',3'-cAMP
wild-type, pH 7.5, temperature not specified in the publication
1.05
2',3'-cAMP
mutant N110A, pH 7.5, 37°C
1.25
2',3'-cAMP
mutant H111A, pH 7.5, 37°C
1.7
2',3'-cAMP
mutant H97A, pH 7.5, temperature not specified in the publication
1.8
2',3'-cAMP
mutant H111N, pH 7.5, 37°C
2.3
2',3'-cAMP
mutant Q27H, pH 7.5, 37°C
2.4
2',3'-cAMP
wild-type, pH 7.5, 37°C
2.5
2',3'-cAMP
mutant F37Y, pH 7.5, 37°C
2.6
2',3'-cAMP
mutant C253A, pH 7.5, 37°C
3.4
2',3'-cAMP
mutant L196A, pH 7.5, 37°C
4.8
2',3'-cAMP
mutant F37A/L196A, pH 7.5, 37°C
5.1
2',3'-cAMP
mutant F37A, pH 7.5, 37°C
5.2
2',3'-cAMP
mutant F37A/L196F/C253A, pH 7.5, 37°C
7.1
2',3'-cAMP
mutant F37A/L196F, pH 7.5, 37°C
7.6
2',3'-cAMP
mutant F210A, pH 7.5, 37°C
7.6
2',3'-cAMP
mutant R43A, pH 7.5, 37°C
0.0035
8-oxo-dGDP
at pH 10.0 and 37°C
0.0038
8-oxo-dGDP
at pH 8.0 and 37°C
2.65
ADP
wild-type, pH 7.5, temperature not specified in the publication
19
ADP
mutant H97A, pH 7.5, temperature not specified in the publication
0.0209
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
0.0223
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
0.0231
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
0.0257
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
0.0279
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
0.0389
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
0.0402
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
0.0434
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
0.0456
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
0.0463
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
0.048
ADP-D-ribose
-
at pH 7.5 and 37°C
0.0702
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
0.0879
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
0.1084
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
0.1197
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
0.1265
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
0.1271
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
0.1283
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
0.1497
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
0.184
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
0.3213
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
0.083
ADP-mannose
pH 7.0, 37°C
0.154
ADP-mannose
-
pH 9.0, 37°C
0.0019
ADP-ribose
at pH 8.0 and 37°C
0.0169
ADP-ribose
-
37°C, pH 8.0, AtNUDT2
0.018
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E70Q
0.0223
ADP-ribose
pH 7.0, 37°C, wild-type enzyme
0.023
ADP-ribose
-
37°C, pH 8.0, AtNUDT6
0.0232
ADP-ribose
-
37°C, pH 8.0, AtNUDT7
0.027
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R81Q
0.0274
ADP-ribose
-
37°C, pH 8.0, AtNUDT10
0.032
ADP-ribose
pH 7.0, 37°C
0.036
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E73Q
0.036
ADP-ribose
at pH 10.0 and 37°C
0.038
ADP-ribose
-
pH 9.0, 37°C
0.043
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E85Q
0.05
ADP-ribose
-
25°C, pH 7.6, mutant enzyme T155A
0.053
ADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.06
ADP-ribose
pH 7.5, 37°C
0.06
ADP-ribose
wild-type, pH 7.5, 37°C
0.06
ADP-ribose
-
25°C, pH 7.6, mutant enzyme T110A
0.065
ADP-ribose
-
37°C, pH 8.0, ADP-ribose pyrophosphatase Slr0920
0.071
ADP-ribose
mutant H97A, pH 7.5, temperature not specified in the publication
0.077
ADP-ribose
mutant F37Y, pH 7.5, 37°C
0.078
ADP-ribose
mutant H111N, pH 7.5, 37°C
0.09
ADP-ribose
-
25°C, pH 7.6, mutant enzyme Y99F
0.094
ADP-ribose
mutant C253A, pH 7.5, 37°C
0.1
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E86Q
0.1
ADP-ribose
-
25°C, pH 7.6, mutant enzyme S153A
0.11
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E82Q
0.11
ADP-ribose
-
25°C, pH 7.6, wild-type enzyme
0.11
ADP-ribose
-
37°C, pH 8.0, ADP-ribose pyrophosphatase Sll1054
0.115
ADP-ribose
mutant R43A, pH 7.5, 37°C
0.12
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R18Q
0.13
ADP-ribose
mutant L196A, pH 7.5, 37°C
0.14
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R27Q
0.14
ADP-ribose
mutant H111A, pH 7.5, 37°C
0.2
ADP-ribose
mutant Q27H, pH 7.5, 37°C
0.204
ADP-ribose
-
pH 8.0
0.24
ADP-ribose
-
25°C, pH 7.6, mutant enzyme Q52A
0.25
ADP-ribose
pH 9.0, 25°C
0.29
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E108Q
0.29
ADP-ribose
-
37°C, pH 8.0, ADP-ribose pyrophosphatase Slr1134
0.29
ADP-ribose
mutant N110A, pH 7.5, 37°C
0.31
ADP-ribose
-
25°C, pH 7.6, mutant enzyme L68A
0.4
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E63Q
0.4
ADP-ribose
-
25°C, pH 7.6, mutant enzyme Y28Q
0.42
ADP-ribose
-
25°C, pH 7.6, mutant enzyme H33A
0.52
ADP-ribose
pH 7.5, 25°C
0.65
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R54Q
0.69
ADP-ribose
-
25°C, pH 7.6, mutant enzyme S102A
1.15
ADP-ribose
mutant F37A, pH 7.5, 37°C
1.15
ADP-ribose
mutant F37A/L196A, pH 7.5, 37°C
1.2
ADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37°C
1.24
ADP-ribose
-
25°C, pH 7.6, mutant enzyme I19A
1.6
ADP-ribose
mutant F37A/L196F, pH 7.5, 37°C
2.1
ADP-ribose
mutant F210A, pH 7.5, 37°C
0.0004
ADPribose
-
pH 7.5, 37°C
0.0005 - 0.001
ADPribose
-
ADPRibase I
0.002 - 0.003
ADPribose
-
-
0.015 - 0.03
ADPribose
-
ADPRibase-Mn
0.031
ADPribose
-
mutant enzyme D126N, in presence of Mg2+
0.044
ADPribose
-
mutant enzyme E129Q, in presence of Mg2+
0.05 - 0.1
ADPribose
-
ADPRibase II
0.058
ADPribose
-
mutant enzyme D128N, in presence of Mg2+
0.071
ADPribose
-
mutant enzyme E127Q, in presence of Mg2+
0.09
ADPribose
-
mutant enzyme E86Q, in presence of Mg2+
0.094
ADPribose
pH 9.5, 37°C
0.11
ADPribose
-
wild-type enzyme, in presence of Mg2+
0.215
ADPribose
-
mutant enzyme E82Q, in presence of Zn2+
0.325
ADPribose
-
mutant enzyme E86Q, in presence of Zn2+
0.36
ADPribose
-
mutant enzyme E82Q, in presence of Mg2+
0.37
ADPribose
-
wild-type enzyme, in presence of Zn2+
0.19
cADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.2
cADP-ribose
mutant C253A, pH 7.5, 37°C
0.46
cADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37°C
0.78
cADP-ribose
wild-type, pH 7.5, 37°C
0.35
CDP-choline
wild-type, pH 7.5, 37°C
0.43
CDP-choline
mutant F37Y, pH 7.5, 37°C
0.47
CDP-choline
mutant L196A, pH 7.5, 37°C
0.5
CDP-choline
mutant C253A, pH 7.5, 37°C
0.97
CDP-choline
mutant F37A, pH 7.5, 37°C
1.25
CDP-choline
mutant F37A/L196A, pH 7.5, 37°C
1.5
CDP-choline
mutant F37A/L196F, pH 7.5, 37°C
1.7
CDP-choline
mutant F37A/L196F/C253A, pH 7.5, 37°C
2.7
CDP-choline
mutant H111N, pH 7.5, 37°C
2.7
CDP-choline
mutant Q27H, pH 7.5, 37°C
4
CDP-choline
mutant N110A, pH 7.5, 37°C
7.5
CDP-choline
mutant H111A, pH 7.5, 37°C
9
CDP-choline
mutant R43A, pH 7.5, 37°C
11
CDP-choline
mutant F210A, pH 7.5, 37°C
12
CDP-choline
wild-type, pH 7.5, temperature not specified in the publication
43
CDP-choline
mutant H97A, pH 7.5, temperature not specified in the publication
3.9
CDP-ethanolamine
wild-type, pH 7.5, temperature not specified in the publication
31
CDP-ethanolamine
mutant H97A, pH 7.5, temperature not specified in the publication
2
CDP-glycerol
wild-type, pH 7.5, temperature not specified in the publication
6.3
CDP-glycerol
mutant H97A, pH 7.5, temperature not specified in the publication
0.3
FAD
pH 7.5, 25°C
additional information
additional information
-
-
-
additional information
additional information
-
effect of N-acetyl-p-benzoquinoneimine on Km
-
additional information
additional information
-
kinetic analysis, Trp28 and Trp46 function synergistically in substrate binding and catalysis, overview
-
additional information
additional information
kinetic analysis, Trp28 and Trp46 function synergistically in substrate binding and catalysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.78
2''-O-acetyl-ADP-ribose
-
at pH 7.5 and 37°C
0.0019 - 13.7
ADP-D-ribose
9.1
ADP-glucose
-
25°C, pH 7.6, wild-type enzyme
1.14
ADPribose 2'-phosphate
-
-
2.1 - 125.2
CDP-ethanolamine
3.36
CDP-ribose
-
25°C, pH 7.6, wild-type enzyme
3.57
GDP-ribose
-
25°C, pH 7.6, wild-type enzyme
additional information
ADP-ribose
-
25°C, pH 7.6, mutant enzyme I19A
0.11
2',3'-cAMP
mutant N110A, pH 7.5, 37°C
0.95
2',3'-cAMP
mutant R43A, pH 7.5, 37°C
2 - 8
2',3'-cAMP
mutant F37A/L196F, pH 7.5, 37°C
2.7
2',3'-cAMP
mutant F210A, pH 7.5, 37°C
3 - 6
2',3'-cAMP
mutant F37A, pH 7.5, 37°C
4.3
2',3'-cAMP
mutant Q27H, pH 7.5, 37°C
7.4
2',3'-cAMP
mutant H111A, pH 7.5, 37°C
16.9
2',3'-cAMP
wild-type, pH 7.5, temperature not specified in the publication
19
2',3'-cAMP
mutant F37A/L196A, pH 7.5, 37°C
20
2',3'-cAMP
mutant F37A/L196F/C253A, pH 7.5, 37°C
29.7
2',3'-cAMP
mutant H97A, pH 7.5, temperature not specified in the publication
30
2',3'-cAMP
mutant L196A, pH 7.5, 37°C
34
2',3'-cAMP
mutant H111N, pH 7.5, 37°C
60
2',3'-cAMP
wild-type, pH 7.5, 37°C
70
2',3'-cAMP
mutant F37Y, pH 7.5, 37°C
83
2',3'-cAMP
mutant C253A, pH 7.5, 37°C
0.2
ADP
mutant H97A, pH 7.5, temperature not specified in the publication
1.8
ADP
wild-type, pH 7.5, temperature not specified in the publication
0.0019
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
0.0069
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
0.058
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
0.1
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
0.18
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
0.32
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
0.41
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
0.94
ADP-D-ribose
-
at pH 7.5 and 37°C
2.7
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
4.5
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
6
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
7.3
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
10.3
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
10.4
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
11.3
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
11.8
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
12.2
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
12.4
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
13.1
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
13.3
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
13.7
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
0.00011
ADP-ribose
-
mutant enzyme E82Q, in presence of Mg2+
0.00014
ADP-ribose
-
mutant enzyme E82Q, in presence of Zn2+
0.00015
ADP-ribose
-
mutant enzyme E86Q, in presence of Mg2+
0.00032
ADP-ribose
-
mutant enzyme E86Q, in presence of Zn2+
0.000939
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E82Q
0.00153
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E86Q
0.003
ADP-ribose
mutant R43A, pH 7.5, 37°C
0.035
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R81Q
0.0411
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R54Q
0.052 - 2.1
ADP-ribose
-
25°C, pH 7.6, mutant enzyme Y28Q
0.057 - 0.65
ADP-ribose
-
25°C, pH 7.6, wild-type enzyme
0.06
ADP-ribose
-
37°C, pH 8.0, AtNUDT10
0.11
ADP-ribose
-
37°C, pH 8.0, AtNUDT6
0.12
ADP-ribose
-
37°C, pH 8.0, AtNUDT2
0.12
ADP-ribose
-
37°C, pH 8.0, AtNUDT7
0.23
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E63Q
0.4
ADP-ribose
mutant H97A, pH 7.5, temperature not specified in the publication
0.41
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E70Q
0.47
ADP-ribose
mutant H111A, pH 7.5, 37°C
0.7
ADP-ribose
-
mutant enzyme D126N, in presence of Mg2+
0.7
ADP-ribose
-
mutant enzyme E129Q, in presence of Mg2+
0.97
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R18Q
1.12
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E85Q
1.4
ADP-ribose
pH 7.5, 25°C
2 - 8
ADP-ribose
-
wild-type enzyme, in presence of Zn2+
2
ADP-ribose
-
37°C, pH 8.0, ADP-ribose pyrophosphatase Slr1134
2.07
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E73Q
2.2
ADP-ribose
-
mutant enzyme D128N, in presence of Mg2+
2.3
ADP-ribose
mutant H111N, pH 7.5, 37°C
2.42
ADP-ribose
-
25°C, pH 7.6, mutant enzyme T155A
2.43
ADP-ribose
-
25°C, pH 7.6, mutant enzyme S102A
2.65
ADP-ribose
-
25°C, pH 7.6, mutant enzyme T110A
2.97
ADP-ribose
-
25°C, pH 7.6, mutant enzyme E108Q
3.3
ADP-ribose
-
25°C, pH 7.6, mutant enzyme S153A
3.32
ADP-ribose
-
25°C, pH 7.6, mutant enzyme Y99F
4.1
ADP-ribose
-
mutant enzyme E127Q, in presence of Mg2+
4.16
ADP-ribose
-
25°C, pH 7.6, mutant enzyme H33A
4.3
ADP-ribose
mutant N110A, pH 7.5, 37°C
4.9
ADP-ribose
pH 9.0, 25°C
5.5
ADP-ribose
pH 7.5, 37°C
5.68
ADP-ribose
-
25°C, pH 7.6, mutant enzyme I19A
5.7
ADP-ribose
-
wild-type enzyme, in presence of Mg2+
5.93
ADP-ribose
-
25°C, pH 7.6, mutant enzyme L68A
6.74
ADP-ribose
-
25°C, pH 7.6, mutant enzyme Q52A
7
ADP-ribose
mutant F37A/L196A, pH 7.5, 37°C
8
ADP-ribose
mutant F37A/L196F, pH 7.5, 37°C
8.6
ADP-ribose
-
37°C, pH 8.0, ADP-ribose pyrophosphatase Slr0920
10
ADP-ribose
mutant Q27H, pH 7.5, 37°C
10.04
ADP-ribose
-
25°C, pH 7.6, mutant enzyme Y28Q
10.65
ADP-ribose
-
25°C, pH 7.6, wild-type enzyme
11.4
ADP-ribose
pH 7.0, 37°C, wild-type enzyme
12.9
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R27Q
13
ADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37°C
14
ADP-ribose
mutant F37A, pH 7.5, 37°C
16
ADP-ribose
mutant L196A, pH 7.5, 37°C
17.05
ADP-ribose
-
25°C, pH 7.6, mutant enzyme R18Q
18
ADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
19
ADP-ribose
mutant F210A, pH 7.5, 37°C
20
ADP-ribose
-
37°C, pH 8.0, ADP-ribose pyrophosphatase Sll1054
35
ADP-ribose
wild-type, pH 7.5, 37°C
50
ADP-ribose
mutant F37Y, pH 7.5, 37°C
97
ADP-ribose
mutant C253A, pH 7.5, 37°C
1.8
ADPribose
pH 9.5, 37°C
0.0005
cADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
3.2
cADP-ribose
wild-type, pH 7.5, 37°C
8.9
cADP-ribose
mutant C253A, pH 7.5, 37°C
16
cADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37°C
0.025
CDP-choline
mutant R43A, pH 7.5, 37°C
0.8
CDP-choline
mutant H97A, pH 7.5, temperature not specified in the publication
2.2
CDP-choline
mutant H111A, pH 7.5, 37°C
5.3
CDP-choline
mutant H111N, pH 7.5, 37°C
5.7
CDP-choline
mutant N110A, pH 7.5, 37°C
25
CDP-choline
mutant F37A/L196A, pH 7.5, 37°C
26
CDP-choline
mutant F37A/L196F, pH 7.5, 37°C
29
CDP-choline
mutant L196A, pH 7.5, 37°C
33
CDP-choline
mutant F37A, pH 7.5, 37°C
37
CDP-choline
mutant F37A/L196F/C253A, pH 7.5, 37°C
39
CDP-choline
mutant Q27H, pH 7.5, 37°C
50
CDP-choline
wild-type, pH 7.5, 37°C
50
CDP-choline
mutant F210A, pH 7.5, 37°C
67.2
CDP-choline
wild-type, pH 7.5, temperature not specified in the publication
76
CDP-choline
mutant F37Y, pH 7.5, 37°C
79
CDP-choline
mutant C253A, pH 7.5, 37°C
2.1
CDP-ethanolamine
mutant H97A, pH 7.5, temperature not specified in the publication
125.2
CDP-ethanolamine
wild-type, pH 7.5, temperature not specified in the publication
0.8
CDP-glycerol
mutant H97A, pH 7.5, temperature not specified in the publication
95.6
CDP-glycerol
wild-type, pH 7.5, temperature not specified in the publication
2.5
FAD
pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
17.3
2''-O-acetyl-ADP-ribose
-
at pH 7.5 and 37°C
0.0027 - 630
ADP-D-ribose
0.007 - 32
CDP-ethanolamine
0.1
2',3'-cAMP
mutant N110A, pH 7.5, 37°C
0.13
2',3'-cAMP
mutant R43A, pH 7.5, 37°C
0.4
2',3'-cAMP
mutant F210A, pH 7.5, 37°C
1.9
2',3'-cAMP
mutant Q27H, pH 7.5, 37°C
3.9
2',3'-cAMP
mutant F37A/L196F, pH 7.5, 37°C
4
2',3'-cAMP
mutant F37A/L196A, pH 7.5, 37°C
4
2',3'-cAMP
mutant F37A/L196F/C253A, pH 7.5, 37°C
6
2',3'-cAMP
mutant H111A, pH 7.5, 37°C
7
2',3'-cAMP
mutant F37A, pH 7.5, 37°C
9
2',3'-cAMP
mutant L196A, pH 7.5, 37°C
18
2',3'-cAMP
mutant H97A, pH 7.5, temperature not specified in the publication
19
2',3'-cAMP
mutant H111N, pH 7.5, 37°C
22
2',3'-cAMP
wild-type, pH 7.5, temperature not specified in the publication
25
2',3'-cAMP
wild-type, pH 7.5, 37°C
28
2',3'-cAMP
mutant F37Y, pH 7.5, 37°C
32
2',3'-cAMP
mutant C253A, pH 7.5, 37°C
0.0011
ADP
mutant H97A, pH 7.5, temperature not specified in the publication
0.66
ADP
wild-type, pH 7.5, temperature not specified in the publication
0.0027
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37°C
0.005
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37°C
0.23
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37°C
1.2
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37°C
1.7
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37°C
4.3
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37°C
13
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37°C
19.6
ADP-D-ribose
-
at pH 7.5 and 37°C
50
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37°C
67
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37°C
72
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37°C
81
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37°C
83
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37°C
89
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37°C
97
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37°C
120
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37°C
230
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37°C
300
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37°C
390
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37°C
530
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37°C
630
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37°C
0.03
ADP-ribose
mutant R43A, pH 7.5, 37°C
3
ADP-ribose
mutant H111A, pH 7.5, 37°C
4.8
ADP-ribose
mutant F37A/L196F, pH 7.5, 37°C
5.9
ADP-ribose
mutant H97A, pH 7.5, temperature not specified in the publication
6
ADP-ribose
mutant F37A/L196A, pH 7.5, 37°C
9
ADP-ribose
mutant F210A, pH 7.5, 37°C
11
ADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37°C
12
ADP-ribose
mutant F37A, pH 7.5, 37°C
15
ADP-ribose
mutant N110A, pH 7.5, 37°C
29
ADP-ribose
mutant H111N, pH 7.5, 37°C
52
ADP-ribose
mutant Q27H, pH 7.5, 37°C
120
ADP-ribose
mutant L196A, pH 7.5, 37°C
340
ADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
590
ADP-ribose
wild-type, pH 7.5, 37°C
650
ADP-ribose
mutant F37Y, pH 7.5, 37°C
1000
ADP-ribose
mutant C253A, pH 7.5, 37°C
0.0001
cADP-ribose
mutant R43A, pH 7.5, 37°C
0.008
cADP-ribose
mutant F210A, pH 7.5, 37°C
0.028
cADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.07
cADP-ribose
mutant H111A, pH 7.5, 37°C
0.13
cADP-ribose
mutant N110A, pH 7.5, 37°C
0.15
cADP-ribose
mutant Q27H, pH 7.5, 37°C
0.29
cADP-ribose
mutant H111N, pH 7.5, 37°C
0.9
cADP-ribose
mutant F37A/L196A, pH 7.5, 37°C
0.9
cADP-ribose
mutant L196A, pH 7.5, 37°C
1.3
cADP-ribose
mutant F37A, pH 7.5, 37°C
1.6
cADP-ribose
mutant F37A/L196F, pH 7.5, 37°C
4
cADP-ribose
wild-type, pH 7.5, 37°C
4.1
cADP-ribose
mutant F37Y, pH 7.5, 37°C
35.5
cADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37°C
44
cADP-ribose
mutant C253A, pH 7.5, 37°C
0.002
CDP-choline
mutant H97A, pH 7.5, temperature not specified in the publication
0.006
CDP-choline
mutant R43A, pH 7.5, 37°C
0.3
CDP-choline
mutant H111A, pH 7.5, 37°C
1.5
CDP-choline
mutant N110A, pH 7.5, 37°C
2
CDP-choline
mutant H111N, pH 7.5, 37°C
4
CDP-choline
mutant F210A, pH 7.5, 37°C
5.6
CDP-choline
wild-type, pH 7.5, temperature not specified in the publication
14
CDP-choline
mutant Q27H, pH 7.5, 37°C
17
CDP-choline
mutant F37A/L196F, pH 7.5, 37°C
21
CDP-choline
mutant F37A/L196A, pH 7.5, 37°C
22
CDP-choline
mutant F37A/L196F/C253A, pH 7.5, 37°C
34
CDP-choline
mutant F37A, pH 7.5, 37°C
62
CDP-choline
mutant L196A, pH 7.5, 37°C
150
CDP-choline
wild-type, pH 7.5, 37°C
160
CDP-choline
mutant C253A, pH 7.5, 37°C
180
CDP-choline
mutant F37Y, pH 7.5, 37°C
0.007
CDP-ethanolamine
mutant H97A, pH 7.5, temperature not specified in the publication
32
CDP-ethanolamine
wild-type, pH 7.5, temperature not specified in the publication
0.12
CDP-glycerol
mutant H97A, pH 7.5, temperature not specified in the publication
48
CDP-glycerol
wild-type, pH 7.5, temperature not specified in the publication
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substrate-docking to zebrafish wild-type protein, and H97A mutant point to a role of His-97 in catalysis by orientation, and to a bidentate water bridging the dinuclear metal center as the potential nucleophile
gadolinium derivative, to 2.0 A resolution. The crystal structure of DR2204 consists of the conserved alpha/beta/alpha sandwich fold typical of Nudix hydrolases, the Nudix box, residues 94-115, holding the alpha1 helix sits between two loops accessible to the solvent, while the other two helices, alpha2 and alpha3, lie on the other side of the central beta-sheet and participate in dimer-interface formation
hanging-drop vapor diffusion at 18°C. The structure of the apo enzyme, the active enzyme and the complex with ADP-ribose are determined to 1.9 A, 2.7 A and 2.3 A, respectively. The Nudix motif residues, folded as a loop-helix-loop tailored for diphosphate hydrolysis, compose the catalytic center
purified recombinant enzyme in complex with the product AMP and Mn2+ ions in its Nudix active site, sitting drop vapor diffusion method, 20°C, 0.001 ml of 15 mg/ml protein solution is mixed with an equal volume of reservoir solution containing 0.1 M Tris, pH 7.5, 200 mM MgCl2, and 19% PEG 3350, with or without 30 mM AMP, equilibration against the reservoir, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method
complexed with 8-oxo-dGMP, 8-oxo-dGDP and 8-oxo-dADP, hanging drop vapor diffusion method, using 0.8 M NaH2PO4/1.2M K2HPO4 and 0.1 M acetate (pH 4.5), and 0.2M ammonium acetate, 35-40% (w/v) polyethylene glycol 3350 and 0.1 M sodium citrate (pH 6.2)
in apo form, in complex with ADP-D-ribose, and in complex with AMP with bound Mg2+, hanging drop vapor diffusion method, using 160 mM sodium acetate (pH 5.5), and 25% (w/v) 2-methyl-2,4-pentanediol, or 300 mM di-ammonium hydrogen citrate, 6% (w/v) n-propanol and 15% (w/v) polyethylene glycol 3350, or 200 mM sodium acetate, 100 mM Tris-HCl (pH 8.0) and 30% (w/v) polyethylene glycol 4000
in complex with alpha,beta-methyleneadenosine diphosphoribose and 3 Mg2+ ions, hanging drop vapor diffusion method, using 250 mM sodium acetate, 100 mM Tris-HCl, pH 8.0, and 29% (w/v) polyethylene glycol 4000
purified recombinant wild-type and truncated mutant NUDT5 in complex with a non-hydrolyzable ADPR analogue, alpha,beta-methyleneadenosine diphosphoribose, and three Mg2+ ions representing the transition state of the enzyme during catalysis, 20 mg/ml protein is incubated with 5 mM AMPCPR and 10 mM MgCl2 at 4 °C overnight, followed by hanging drop vapour diffusion method, wild-type enzyme in complex with AMPCPR, and truncation mutant DELTAhNUDT5 in complex with AMPCPR and Mg2+, 4 °C, mixing of equal volumes of the protein solution and the reservoir solution containing 250 mM NaAc, 100 mM Tris-HCl, pH 8.0, and 29% PEG 4000, ingle crystals of the plate-shape morphology grow after 1 month, X-ray diffraction structure determination and anaylsis at 2.0 A resolution, molecular modelling
substrate docking on a homology model suggests possible interactions of ADP-ribose with seven residues located, with one exception (Cys253), either within the metallo-dependent phosphatases signature (Gln27, Asn110, His111), or in unique structural regions of the ADPRibase-Mn family: s2s3 (Phe37 and Arg43) and h7h8 (Phe210), around the active site entrance. Residue Phe37 is needed for ADP-ribose preference without catalytic effect. Arg43 is essential for catalysis. Cys253 is hindering for cADPR phosphohydrolase
purified recombinant His-tagged enzyme in complex with co-purified NAD and diphosphate complexed in the NadM-domain active site, and with ADPR substrate complexed in the Nudix-domain, hanging drop vapor diffusion method, 0.0015 ml of 15 mg/ml protein solution is mixed with an equal volume of reservoir solution containing 100 mM Tris, pH 7.5, and 1.5 M Li2SO4, 20°C, 3 days to 2 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, selenomethionyl MAD phasing method
crystal structures analysis of Ndx4 in the E-state obtained at 0.91 A resolution, PDB IDs are 2YVM, 1MP2, 1G0S, and 2DSB
crystallized in absence or presence of ADP-ribose by hanging-drop vapour-diffusion method. 1.5 A resolution from the apo form using synchrotron radiation and 2.0 A resolution from the complexed form. Both crystals belong to space group P3(1)21 or P3(2)21 and contain one molecule in the asymmetric unit
in complex with alpha,beta-methyleneadenosine diphosphoribose, sitting drop vapor diffusion method, using 18% (w/v) PEG 4000, 0.1 M sodium acetate buffer pH 5.3, 20% (w/v) glycerol, 0.2 M ammonium sulfate, at 20°C
Ndx2 alone and in complex with Mg2+, with Mg2+ and AMP, and with Mg2+ and a nonhydrolyzable ADPR analogue, hanging-drop vapor diffusion method, 20 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM KCl, 0.001 ml of protein solution is mixed with the equal volume of reservoir solution and equilibrated against the reservoir, containing 0.1 M MES, pH 6.5, 0.16 M sodium acetate or magnesium acetate for the complexed enzyme, 14% PEG 8000, and 20% glycerol, at 20°C, soaking of crystals in 50 mM KAu(CN)2, X-ray diffraction structure determination and anaylsis at 2.0 A resolution, MAD phasing, model building, and refinement
to 2.16 A resolution. The crystal structure shows an unusual asymmetric dimer, with three domains for each chain. The C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose diphosphatase activity. The mechanism for the ADP-ribose diphosphatase reaction involves a rotation of the COG1058 domain dimer as part of the reaction cycle
Zn2+-bound enzyme, binary complex with ADPribose, ternary complex with Zn2+ and ADPribose, ternary complex with Gd3+ and ADPribose, product complex with AMP and Mg2+, product complex with ribose 5'-phosphate and Zn2+, mutant enzyme E82Q with ligands Mg2+ and SO42-, mutant enzyme E86Q with ligands Mg2+ and ADPribose, mutant enzyme E82Q with ligands Zn2+ and SO42-, mutant enzyme E86Q with ligands Zn2+ and ADPribose
-
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H97A
mutant shows 60fold decrease in activity for substrates ADP-ribose and ADP and 300500fold for CDP-alcohols. For H97A, 2',3'-cAMP is a better substrate than ADP-ribose
C253A
mutant displays a tenfold increased efficiency for cADP-ribose, with no or modest effect on the other substrates
D164A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D164N
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E112Q
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
E115Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E116Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E166Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F210A
lowers 40-70fold the catalytic efficiency for ADP-ribose, CDP-choline and 2',3'-cAMP hydrolysis, and 500fold for cADP-ribose
F37A
19fold increased Km for ADP-ribose, with only a 2-3fold increase of the CDP-choline and 2',3'-cAMP Km values
F37A/L196A
mutation lessens the relative preference for ADP-ribose versus cADP-ribose
F37A/L196F
mutation lessens the relative preference for ADP-ribose versus cADP-ribose
F37A/L196F/C253G
site-directed mutagenesis, the mutant with a smaller residue 253 shows increased cADPR specificity
F37A/L196F/D250A/C253G
site-directed mutagenesis, the quadruple mutant shows a detrimental effect of the D250A substitution on the efficiency with all substrates (1.3-3.4fold decrease), and more markedly so for cADPR, such that the substrate efficiency ratios are less favourable than for the triple mutant F37A/L196F/C253G
F37A/L196F/V252A/C253G
site-directed mutagenesis, the mutant with displays the desired specificity, with cADPR kcat/KM is about 20-200fold larger than for any other substrate. The quadruple mutant shows detrimental effects of the V252A substitution on the efficiency with ADP-ribose, CDP-choline and 2',3'-cAMP (1.1-2.8fold decrease) while it increases 2fold the efficiency with cADPR
F37A/L196F/V252A/C253G/T279A
site-directed mutagenesis
F37Y
similar kinetic parameters as the wild type
H111A
marked efficiency decrease with all substrates except 2',3'-cAMP
H111N
marked efficiency decrease with all substrates except 2',3'-cAMP
L196A
mutation causes only a modest 2-5fold decrease of catalytic efficiency with the four substrates tested
N110A
100-250fold reduction in catalytic efficiency for the hydrolysis of CDP-choline or 2',3'-cAMP
Q27H
mutation reduces 11-13-fold the catalytic efficiency of the hydrolysis of ADP-ribose, CDP-choline or 2',3'-cAMP, and 27fold the hydrolysis of cADP-ribose
Q82A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R111Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R43A
drastic decrease of catalytic efficiency
R84Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D126N
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 40% of the of the wild-type enzyme
D128N
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 74% of the of the wild-type enzyme
E108Q
-
kcat/Km is 9.6fold lower than wild-type value
E127Q
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 114% of the of the wild-type enzyme
E129Q
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 32% of the of the wild-type enzyme
E63Q
-
kcat/Km is 173fold lower than wild-type value
E70Q
-
kcat/Km is 8.9fold lower than wild-type value
E73Q
-
kcat/Km is 1.8fold lower than wild-type value
E85Q
-
kcat/Km is 3.8fold lower than wild-type value
H33A
-
kcat/Km is 10fold lower than wild-type value
I19A
-
kcat/Km is 22fold lower than wild-type value
L68A
-
kcat/Km is 5.3fold lower than wild-type value
Q52A
-
kcat/Km is 3.5fold lower than wild-type value
R18Q
-
kcat/Km is 1.5fold higher than wild-type value
R27Q
-
kcat/Km is 1.04fold lower than wild-type value
R54Q
-
kcat/Km is 1589fold lower than wild-type value
R81Q
-
kcat/Km is 77fold lower than wild-type value
S102A
-
kcat/Km is 28.3fold lower than wild-type value
S153A
-
kcat/Km is 2.9fold lower than wild-type value
T110A
-
kcat/Km is 2.3fold lower than wild-type value
T155A
-
kcat/Km is 1.9fold lower than wild-type value
Y28Q
-
kcat/Km is 4fold lower than wild-type value
Y99F
-
kcat/Km is 2.6fold lower than wild-type value
D126N
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 40% of the of the wild-type enzyme
-
D128N
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 74% of the of the wild-type enzyme
-
E127Q
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 114% of the of the wild-type enzyme
-
E129Q
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 32% of the of the wild-type enzyme
-
E86Q
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0034% of the of the wild-type enzyme
-
C139A
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
C139A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D133A
site-directed mutagenesis, mutation causes a 4.0fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
D133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D133N
site-directed mutagenesis, mutation causes a 2.1fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
D133N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E93Q
site-directed mutagenesis, mutation causes a 1.8fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
E93Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F37A/L196F/C253A
cyclic ADP-ribose is the best substrate for the mutant
F37A/L196F/C253A
site-directed mutagenesis, specific cyclic ADP-ribose phosphohydrolase obtained by mutagenic engineering of Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase. Mutagenesis of human ADPRibase-Mn at Phe37, Leu196 and Cys253 alters its specificity, the best substrate of the mutant is cyclic ADP-ribose (cADPR), the Cys253 mutation is essential for cADPR preference. The proximity to the northern ribose of cADPR in docking models indicates Cys253 is a steric constraint for cADPR positioning
L98A
site-directed mutagenesis, mutation of Leu98 to Ala causes a 5.8fold increase in Km but has no effect on kcat compared to the wild-type enzyme
L98A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R196Q
site-directed mutagenesis, mutation causes a 5.5fold increase in Km for ADP-ribose but has no effect on kcat compared to the wild-type enzyme
R196Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R51Q
site-directed mutagenesis, the mutant shows a 14.6fold increased Km and a 17fold decreased kcat for ADP-ribose compared to the wild-type enzyme
R51Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W28A
site-directed mutagenesis, the mutant shows 8.4fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme
W28A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W28A/W46A
site-directed mutagenesis, the mutant shows 53.7fold increased Km and a 219fold decreased kcat for ADP-ribose compared to the wild-type enzyme
W28A/W46A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
W46A
site-directed mutagenesis, the mutant shows 5.7fold increased Km for ADP-ribose, but unaltered kcat compared to the wild-type enzyme
W46A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E82Q
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0006% of the of the wild-type enzyme
E82Q
-
kcat/Km is 118171fold lower than wild-type value
E86Q
-
the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0034% of the of the wild-type enzyme
E86Q
-
kcat/Km is 6722fold lower than wild-type value
additional information
overexpression of AtNUDX7 in Arabidopsis thaliana improves seed parameters, accelerates flowering, and reduces inflorescence height. AtNUDX7 overexpression in Arabixaddopsis might enhance the ADP-ribose recycling step and maintain energy levels by supplying an ATP source in the poly(ADP-ribosyl)ation energy homeostasis pathway. Arabidopsis and maize lines with high, medium and low overexpression levels of the AtNUDX7 gene are analysed in automated platforms and the inhibition of several growth parameters is determined under mild drought stress conditions. The constitutive overexpression of the Arabidopxadsis AtNUDX7 gene in Arabidopsis and maize at varying levels does not improve tolerance to mild drought stress, but knocking down AtNUDX7 expression does, however at the expense of general growth under normal conditions. A loss-of-function mutant line, designated Atnudx7-1 (SALK-046441), has a T-DNA insertion in exon 1 of the AtNUDX7 gene, in the Col-0 background and verified for its T-DNA insertion position, homozygous T-DNA insertion, AtNUDX7 gene expression, and is used as a negative control. Evaluation of the AtNUDX7 overexpression maize lines under mild drought stress
additional information
-
overexpression of AtNUDX7 in Arabidopsis thaliana improves seed parameters, accelerates flowering, and reduces inflorescence height. AtNUDX7 overexpression in Arabixaddopsis might enhance the ADP-ribose recycling step and maintain energy levels by supplying an ATP source in the poly(ADP-ribosyl)ation energy homeostasis pathway. Arabidopsis and maize lines with high, medium and low overexpression levels of the AtNUDX7 gene are analysed in automated platforms and the inhibition of several growth parameters is determined under mild drought stress conditions. The constitutive overexpression of the Arabidopxadsis AtNUDX7 gene in Arabidopsis and maize at varying levels does not improve tolerance to mild drought stress, but knocking down AtNUDX7 expression does, however at the expense of general growth under normal conditions. A loss-of-function mutant line, designated Atnudx7-1 (SALK-046441), has a T-DNA insertion in exon 1 of the AtNUDX7 gene, in the Col-0 background and verified for its T-DNA insertion position, homozygous T-DNA insertion, AtNUDX7 gene expression, and is used as a negative control. Evaluation of the AtNUDX7 overexpression maize lines under mild drought stress
additional information
-
overexpression of AtNUDX7 in Arabidopsis thaliana improves seed parameters, accelerates flowering, and reduces inflorescence height. AtNUDX7 overexpression in Arabixaddopsis might enhance the ADP-ribose recycling step and maintain energy levels by supplying an ATP source in the poly(ADP-ribosyl)ation energy homeostasis pathway. Arabidopsis and maize lines with high, medium and low overexpression levels of the AtNUDX7 gene are analysed in automated platforms and the inhibition of several growth parameters is determined under mild drought stress conditions. The constitutive overexpression of the Arabidopxadsis AtNUDX7 gene in Arabidopsis and maize at varying levels does not improve tolerance to mild drought stress, but knocking down AtNUDX7 expression does, however at the expense of general growth under normal conditions. A loss-of-function mutant line, designated Atnudx7-1 (SALK-046441), has a T-DNA insertion in exon 1 of the AtNUDX7 gene, in the Col-0 background and verified for its T-DNA insertion position, homozygous T-DNA insertion, AtNUDX7 gene expression, and is used as a negative control. Evaluation of the AtNUDX7 overexpression maize lines under mild drought stress
-
additional information
-
construction of a truncation mutant DELTAhNUDT5
additional information
construction of a truncation mutant DELTAhNUDT5
additional information
design of mutations at or near residue 253 of human ADPRibase-Mn, in the vicinity of the adenine N1-linked (northern) ribose of cADPR, for altering the substrate specificity of the enzyme, overview
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Kim, Y.P.; Kahng, J.B.; Choi, J.Y.
Adenosine diphosphate ribose pyrophosphohydrolase in human skin
J. Dermatol.
7
11-15
1980
Homo sapiens
brenda
Wu, J.M.; Lennon, M.B.; Suhadolnik, R.J.
Catabolism of NAD+ in rabbit reticulocyte lysates
Biochim. Biophys. Acta
520
588-597
1978
Oryctolagus cuniculus
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