Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + phosphate
-
-
-
?
diadenosine 5',5''-diphosphate + H2O
?
20% the activity with ADP-ribose
-
-
?
GDP-glucose + H2O
GMP + glucose
7% of 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
-
-
-
?
NADP+ + H2O
nicotinic 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
-
-
-
?
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
-
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
-
-
-
?
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
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.
ADP-alpha-D-ribose + H2O
AMP + D-ribose 5-phosphate
ADP-D-ribose + H2O
AMP + D-ribose 5-phosphate
ADP-ribose + H2O
AMP + D-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
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
CDP-choline + H2O
CMP + phosphocholine
reaction of EC 3.6.1.53
-
-
?
cyclic ADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP + phosphate
-
-
-
?
NADP+ + H2O
nicotinic acid mononucleotide + phosphate
-
-
-
?
NADP+ + H2O
nicotinic mononucleotide + phosphate
-
-
-
?
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
-
-
-
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-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
-
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 + 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
-
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
-
-
-
?
ADPribose + H2O

AMP + D-ribose 5-phosphate
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
the enzyme may play a role in tellurite resistance
-
-
?
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
-
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play a role in tellurite resistance
-
-
?
ADPribose + H2O
AMP + D-ribose 5-phosphate
-
the enzyme may play a role in tellurite resistance
-
-
?
FAD + H2O

?
preferred substrate
-
-
?
FAD + H2O
?
preferred substrate
-
-
?
NADH + H2O

AMP + NMNH
-
-
-
?
NADH + H2O
AMP + NMNH
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+

-
marginally effective in activation
Co2+
-
absolute requirement for divalent metal ion is satisfied by Mn2+, Co2+ or Mg2+
Mg2+

-
divalent cation required, Mg2+ or Mn2+. Mg2+ is much more effective than Mn2+
Mg2+
-
absolutely required, activates at 5 mM
Mg2+
1 mM required for optimal activity
Mg2+
-
maximal activity at 16 mM
Mg2+
-
maximal activity at 2 mM, Mg2+ or Mn2+ required
Mg2+
optimal activity with 2.5-5 mM Mg2+ or 0.1-0.25 mM Mn2+
Mg2+
-
strictly requires Mg2+ (more than 1 mM) or Mn2+ for full activity. Treatment with H2O2 changes the specificity of both ADP-ribose activities for the activating divalent cation, giving them a marked preference for Mn2+ and rendering them virtually inactive with Mg2+
Mg2+
-
5 mM required for optimal activity
Mg2+
-
absolute requirement for divalent metal ion is satisfied by Mn2+, Co2+ or Mg2+
Mg2+
-
ADPRibase-I is highly specific for ADPribose and IDPribose in presence of Mg2+, but active also on non-reducing ADP-hexoses and dinucleotides when Mg2+ is replaced with Mn2+. ADPRibase-Mn is a Mn2+-dependent diphosphatase active on ADPribose and IDPribose, dinucleotides and CDP alcohols. ADPribase-II is a rather unspecific diphosphatase that, with Mg2+, is active on AMP or IMP containing NDP sugars and dinucleotides, and with Mn2+ also active on non-adenine NDP-sugars and CDP-alcohols
Mg2+
divalent cation required, Mg2+ is most effective
Mg2+
-
divalent cation required, Mg2+ is most effective, ADP-ribose pyrophosphatase Sll1054
Mg2+
-
divalent cation required, Mg2+ is most effective, ADP-ribose pyrophosphatase Slr0920
Mg2+
-
divalent cation required, Mg2+ is most effective, ADP-ribose pyrophosphatase Slr1134
Mg2+
dependent on Mg2+ or Zn2+
Mg2+
binding structure, overview
Mn2+

-
divalent cation required, Mg2+ or Mn2+. Mg2+ is much more effective than Mn2+
Mn2+
required for full activity
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
can partially substitute for Mg2+
Mn2+
-
50% of maximal activity at 5 mM
Mn2+
-
maximal activity at 0.02-0.05 mM with a steep decrease at increasing pH-values, Mg2+ or Mn2+ required
Mn2+
optimal activity with 2.5-5 mM Mg2+ or 0.1-0.25 mM Mn2+
Mn2+
-
strictly requires Mg2+ or Mn2+ (0.05 mM) for full activity. Treatment with H2O2 changes the specificity of both ADP-ribose activities for the activating divalent cation, giving them a marked preference for Mn2+ and rendering them virtually inactive with Mg2+
Mn2+
dependent on, dinuclear metal centre
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
-
can partially substitute for Mg2+
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
-
absolute requirement for divalent metal ion is satisfied by Mn2+, Co2+ or Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
ADPRibase-I is highly specific for ADPribose and IDPribose in presence of Mg2+, but active also on non-reducing ADP-hexoses and dinucleotides when Mg2+ is replaced with Mn2+. ADPRibase-Mn is a Mn2+-dependent diphosphatase active on ADPribose and IDPribose, dinucleotides and CDP alcohols. ADPribase-II is a rather unspecific diphosphatase that, with Mg2+, is active on AMP or IMP containing NDP sugars and dinucleotides, and with Mn2+ also active on non-adenine NDP-sugars and CDP-alcohols
Mn2+
divalent cation required, Mn2+ results in 22% of the activity observed in presence of Mg2+
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Two Mn2+ ions are inserted consecutively into the catalytic center of the ES-state and ligated by Glu86 and Glu82, which are highly conserved among the Nudix family, in the ESM- and ESMM-states
Zn2+

can partially substitute for Mg2+
Zn2+
-
marginally effective in activation
Zn2+
-
can partially substitute for Mg2+
Zn2+
divalent cation required, Zn2+ results in 9% of the activity observed in presence of Mg2+
Zn2+
dependent on Mg2+ or Zn2+
additional information

-
the ADPR-hydrolysis reaction of ADPRase from Thermus thermophilus strain HB8 (TtADPRase) requires divalent metal cations such as Mn2+, Zn2+, or Mg2+ as cofactors
additional information
the ADPR-hydrolysis reaction of ADPRase from Thermus thermophilus strain HB8 (TtADPRase) requires divalent metal cations such as Mn2+, Zn2+, or Mg2+ as cofactors
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.
Breast Neoplasms
Author Correction: Targeted NUDT5 inhibitors block hormone signaling in breast cancer cells.
Breast Neoplasms
Expression of Oncogenic Drivers in 3D Cell Culture Depends on Nuclear ATP Synthesis by NUDT5.
Breast Neoplasms
Identification of NUDT5 Inhibitors From Approved Drugs.
Breast Neoplasms
Molecular docking based virtual screening of the breast cancer target NUDT5.
Breast Neoplasms
NUDT5 as a novel drug target and prognostic biomarker for ER-positive breast cancer.
Breast Neoplasms
Role of the NUDT Enzymes in Breast Cancer.
Breast Neoplasms
Targeted NUDT5 inhibitors block hormone signaling in breast cancer cells.
Breast Neoplasms
The high expression of NUDT5 indicates poor prognosis of breast cancer by modulating AKT / Cyclin D signaling.
Carcinogenesis
The high expression of MTH1 and NUDT5 promotes tumor metastasis and indicates a poor prognosis in patients with non-small-cell lung cancer.
Carcinoma
The high expression of MTH1 and NUDT5 predict a poor survival and are associated with malignancy of esophageal squamous cell carcinoma.
Colorectal Neoplasms
MutT-related proteins are novel progression and prognostic markers for colorectal cancer.
Cysts
Specific ADP-ribose pyrophosphatase from Artemia cysts and rat liver: effects of nitroprusside, fluoride and ionic strength.
Diabetes Mellitus, Type 2
No evidence of diabetes-specific CD38 (ADP ribosil cyclase/cyclic ADP-ribose hydrolase) autoantibodies by liquid-phase immunoprecipitation.
Endometrial Neoplasms
Differential expression of NUDT9 at different phases of the menstrual cycle and in different components of normal and neoplastic human endometrium.
Esophageal Squamous Cell Carcinoma
The high expression of MTH1 and NUDT5 predict a poor survival and are associated with malignancy of esophageal squamous cell carcinoma.
Infections
AtNUDT7, a negative regulator of basal immunity in Arabidopsis, modulates two distinct defense response pathways and is involved in maintaining redox homeostasis.
Lung Neoplasms
The high expression of MTH1 and NUDT5 promotes tumor metastasis and indicates a poor prognosis in patients with non-small-cell lung cancer.
Lymphatic Metastasis
MutT-related proteins are novel progression and prognostic markers for colorectal cancer.
Neoplasm Metastasis
Expression of Oncogenic Drivers in 3D Cell Culture Depends on Nuclear ATP Synthesis by NUDT5.
Neoplasm Metastasis
MutT-related proteins are novel progression and prognostic markers for colorectal cancer.
Neoplasm Metastasis
The high expression of MTH1 and NUDT5 promotes tumor metastasis and indicates a poor prognosis in patients with non-small-cell lung cancer.
Neoplasms
Expression of Oncogenic Drivers in 3D Cell Culture Depends on Nuclear ATP Synthesis by NUDT5.
Neoplasms
NUDT expression is predictive of prognosis in patients with clear cell renal cell carcinoma.
Neoplasms
NUDT5 as a novel drug target and prognostic biomarker for ER-positive breast cancer.
Neoplasms
Role of the NUDT Enzymes in Breast Cancer.
Neoplasms
The high expression of MTH1 and NUDT5 predict a poor survival and are associated with malignancy of esophageal squamous cell carcinoma.
Neoplasms
The high expression of MTH1 and NUDT5 promotes tumor metastasis and indicates a poor prognosis in patients with non-small-cell lung cancer.
Neoplasms
The high expression of NUDT5 indicates poor prognosis of breast cancer by modulating AKT / Cyclin D signaling.
Tuberculosis
High precision multi-genome scale reannotation of enzyme function by EFICAz.
Tuberculosis
Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification, and A to C mutation avoidance.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.045
2''-O-acetyl-ADP-ribose
-
at pH 7.5 and 37ưC
0.0035 - 0.0038
8-oxo-dGDP
0.0209 - 0.3213
ADP-D-ribose
3.16
ADP-glucose
-
25ưC, 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
-
25ưC, pH 7.6, wild-type enzyme
1.1
GDP-ribose
-
25ưC, 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, 37ưC
1.25
2',3'-cAMP
mutant H111A, pH 7.5, 37ưC
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, 37ưC
2.3
2',3'-cAMP
mutant Q27H, pH 7.5, 37ưC
2.4
2',3'-cAMP
wild-type, pH 7.5, 37ưC
2.5
2',3'-cAMP
mutant F37Y, pH 7.5, 37ưC
2.6
2',3'-cAMP
mutant C253A, pH 7.5, 37ưC
3.4
2',3'-cAMP
mutant L196A, pH 7.5, 37ưC
4.8
2',3'-cAMP
mutant F37A/L196A, pH 7.5, 37ưC
5.1
2',3'-cAMP
mutant F37A, pH 7.5, 37ưC
5.2
2',3'-cAMP
mutant F37A/L196F/C253A, pH 7.5, 37ưC
7.1
2',3'-cAMP
mutant F37A/L196F, pH 7.5, 37ưC
7.6
2',3'-cAMP
mutant F210A, pH 7.5, 37ưC
7.6
2',3'-cAMP
mutant R43A, pH 7.5, 37ưC
0.0035
8-oxo-dGDP

at pH 10.0 and 37ưC
0.0038
8-oxo-dGDP
at pH 8.0 and 37ưC
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 37ưC
0.0223
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37ưC
0.0231
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37ưC
0.0257
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37ưC
0.0279
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37ưC
0.0389
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37ưC
0.0402
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37ưC
0.0434
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37ưC
0.0456
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37ưC
0.0463
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37ưC
0.048
ADP-D-ribose
-
at pH 7.5 and 37ưC
0.0702
ADP-D-ribose
mutant enzyme E112Q, at pH 7.0 and 37ưC
0.0879
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37ưC
0.1084
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37ưC
0.1197
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37ưC
0.1265
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37ưC
0.1271
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37ưC
0.1283
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37ưC
0.1497
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37ưC
0.184
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37ưC
0.3213
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37ưC
0.083
ADP-mannose

pH 7.0, 37ưC
0.154
ADP-mannose
-
pH 9.0, 37ưC
0.0019
ADP-ribose

at pH 8.0 and 37ưC
0.0169
ADP-ribose
-
37ưC, pH 8.0, AtNUDT2
0.018
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E70Q
0.0223
ADP-ribose
pH 7.0, 37ưC, wild-type enzyme
0.023
ADP-ribose
-
37ưC, pH 8.0, AtNUDT6
0.0232
ADP-ribose
-
37ưC, pH 8.0, AtNUDT7
0.027
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme R81Q
0.0274
ADP-ribose
-
37ưC, pH 8.0, AtNUDT10
0.032
ADP-ribose
pH 7.0, 37ưC
0.036
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E73Q
0.036
ADP-ribose
at pH 10.0 and 37ưC
0.038
ADP-ribose
-
pH 9.0, 37ưC
0.043
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E85Q
0.05
ADP-ribose
-
25ưC, 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, 37ưC
0.06
ADP-ribose
wild-type, pH 7.5, 37ưC
0.06
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme T110A
0.065
ADP-ribose
-
37ưC, 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, 37ưC
0.078
ADP-ribose
mutant H111N, pH 7.5, 37ưC
0.09
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme Y99F
0.094
ADP-ribose
mutant C253A, pH 7.5, 37ưC
0.1
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E86Q
0.1
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme S153A
0.11
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E82Q
0.11
ADP-ribose
-
25ưC, pH 7.6, wild-type enzyme
0.11
ADP-ribose
-
37ưC, pH 8.0, ADP-ribose pyrophosphatase Sll1054
0.115
ADP-ribose
mutant R43A, pH 7.5, 37ưC
0.12
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme R18Q
0.13
ADP-ribose
mutant L196A, pH 7.5, 37ưC
0.14
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme R27Q
0.14
ADP-ribose
mutant H111A, pH 7.5, 37ưC
0.2
ADP-ribose
mutant Q27H, pH 7.5, 37ưC
0.204
ADP-ribose
-
pH 8.0
0.24
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme Q52A
0.25
ADP-ribose
pH 9.0, 25ưC
0.29
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E108Q
0.29
ADP-ribose
-
37ưC, pH 8.0, ADP-ribose pyrophosphatase Slr1134
0.29
ADP-ribose
mutant N110A, pH 7.5, 37ưC
0.31
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme L68A
0.4
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E63Q
0.4
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme Y28Q
0.42
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme H33A
0.52
ADP-ribose
pH 7.5, 25ưC
0.65
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme R54Q
0.69
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme S102A
1.15
ADP-ribose
mutant F37A, pH 7.5, 37ưC
1.15
ADP-ribose
mutant F37A/L196A, pH 7.5, 37ưC
1.2
ADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37ưC
1.24
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme I19A
1.6
ADP-ribose
mutant F37A/L196F, pH 7.5, 37ưC
2.1
ADP-ribose
mutant F210A, pH 7.5, 37ưC
0.0004
ADPribose

-
pH 7.5, 37ưC
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, 37ưC
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, 37ưC
0.46
cADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37ưC
0.78
cADP-ribose
wild-type, pH 7.5, 37ưC
0.35
CDP-choline

wild-type, pH 7.5, 37ưC
0.43
CDP-choline
mutant F37Y, pH 7.5, 37ưC
0.47
CDP-choline
mutant L196A, pH 7.5, 37ưC
0.5
CDP-choline
mutant C253A, pH 7.5, 37ưC
0.97
CDP-choline
mutant F37A, pH 7.5, 37ưC
1.25
CDP-choline
mutant F37A/L196A, pH 7.5, 37ưC
1.5
CDP-choline
mutant F37A/L196F, pH 7.5, 37ưC
1.7
CDP-choline
mutant F37A/L196F/C253A, pH 7.5, 37ưC
2.7
CDP-choline
mutant H111N, pH 7.5, 37ưC
2.7
CDP-choline
mutant Q27H, pH 7.5, 37ưC
4
CDP-choline
mutant N110A, pH 7.5, 37ưC
7.5
CDP-choline
mutant H111A, pH 7.5, 37ưC
9
CDP-choline
mutant R43A, pH 7.5, 37ưC
11
CDP-choline
mutant F210A, pH 7.5, 37ưC
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, 25ưC
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 37ưC
0.0019 - 13.7
ADP-D-ribose
9.1
ADP-glucose
-
25ưC, pH 7.6, wild-type enzyme
1.14
ADPribose 2'-phosphate
-
-
2.1 - 125.2
CDP-ethanolamine
3.36
CDP-ribose
-
25ưC, pH 7.6, wild-type enzyme
3.57
GDP-ribose
-
25ưC, pH 7.6, wild-type enzyme
additional information
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme I19A
0.11
2',3'-cAMP

mutant N110A, pH 7.5, 37ưC
0.95
2',3'-cAMP
mutant R43A, pH 7.5, 37ưC
2 - 8
2',3'-cAMP
mutant F37A/L196F, pH 7.5, 37ưC
2.7
2',3'-cAMP
mutant F210A, pH 7.5, 37ưC
3 - 6
2',3'-cAMP
mutant F37A, pH 7.5, 37ưC
4.3
2',3'-cAMP
mutant Q27H, pH 7.5, 37ưC
7.4
2',3'-cAMP
mutant H111A, pH 7.5, 37ưC
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, 37ưC
20
2',3'-cAMP
mutant F37A/L196F/C253A, pH 7.5, 37ưC
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, 37ưC
34
2',3'-cAMP
mutant H111N, pH 7.5, 37ưC
60
2',3'-cAMP
wild-type, pH 7.5, 37ưC
70
2',3'-cAMP
mutant F37Y, pH 7.5, 37ưC
83
2',3'-cAMP
mutant C253A, pH 7.5, 37ưC
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 37ưC
0.0069
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37ưC
0.058
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37ưC
0.1
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37ưC
0.18
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37ưC
0.32
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37ưC
0.41
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37ưC
0.94
ADP-D-ribose
-
at pH 7.5 and 37ưC
2.7
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37ưC
4.5
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37ưC
6
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37ưC
7.3
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37ưC
10.3
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37ưC
10.4
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37ưC
11.3
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37ưC
11.8
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37ưC
12.2
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37ưC
12.4
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37ưC
13.1
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37ưC
13.3
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37ưC
13.7
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37ưC
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
-
25ưC, pH 7.6, mutant enzyme E82Q
0.00153
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E86Q
0.003
ADP-ribose
mutant R43A, pH 7.5, 37ưC
0.035
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme R81Q
0.0411
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme R54Q
0.052 - 2.1
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme Y28Q
0.057 - 0.65
ADP-ribose
-
25ưC, pH 7.6, wild-type enzyme
0.06
ADP-ribose
-
37ưC, pH 8.0, AtNUDT10
0.11
ADP-ribose
-
37ưC, pH 8.0, AtNUDT6
0.12
ADP-ribose
-
37ưC, pH 8.0, AtNUDT2
0.12
ADP-ribose
-
37ưC, pH 8.0, AtNUDT7
0.23
ADP-ribose
-
25ưC, 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
-
25ưC, pH 7.6, mutant enzyme E70Q
0.47
ADP-ribose
mutant H111A, pH 7.5, 37ưC
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
-
25ưC, pH 7.6, mutant enzyme R18Q
1.12
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E85Q
1.4
ADP-ribose
pH 7.5, 25ưC
2 - 8
ADP-ribose
-
wild-type enzyme, in presence of Zn2+
2
ADP-ribose
-
37ưC, pH 8.0, ADP-ribose pyrophosphatase Slr1134
2.07
ADP-ribose
-
25ưC, 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, 37ưC
2.42
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme T155A
2.43
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme S102A
2.65
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme T110A
2.97
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme E108Q
3.3
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme S153A
3.32
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme Y99F
4.1
ADP-ribose
-
mutant enzyme E127Q, in presence of Mg2+
4.16
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme H33A
4.3
ADP-ribose
mutant N110A, pH 7.5, 37ưC
4.9
ADP-ribose
pH 9.0, 25ưC
5.5
ADP-ribose
pH 7.5, 37ưC
5.68
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme I19A
5.7
ADP-ribose
-
wild-type enzyme, in presence of Mg2+
5.93
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme L68A
6.74
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme Q52A
7
ADP-ribose
mutant F37A/L196A, pH 7.5, 37ưC
8
ADP-ribose
mutant F37A/L196F, pH 7.5, 37ưC
8.6
ADP-ribose
-
37ưC, pH 8.0, ADP-ribose pyrophosphatase Slr0920
10
ADP-ribose
mutant Q27H, pH 7.5, 37ưC
10.04
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme Y28Q
10.65
ADP-ribose
-
25ưC, pH 7.6, wild-type enzyme
11.4
ADP-ribose
pH 7.0, 37ưC, wild-type enzyme
12.9
ADP-ribose
-
25ưC, pH 7.6, mutant enzyme R27Q
13
ADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37ưC
14
ADP-ribose
mutant F37A, pH 7.5, 37ưC
16
ADP-ribose
mutant L196A, pH 7.5, 37ưC
17.05
ADP-ribose
-
25ưC, 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, 37ưC
20
ADP-ribose
-
37ưC, pH 8.0, ADP-ribose pyrophosphatase Sll1054
35
ADP-ribose
wild-type, pH 7.5, 37ưC
50
ADP-ribose
mutant F37Y, pH 7.5, 37ưC
97
ADP-ribose
mutant C253A, pH 7.5, 37ưC
1.8
ADPribose

pH 9.5, 37ưC
0.0005
cADP-ribose

wild-type, pH 7.5, temperature not specified in the publication
3.2
cADP-ribose
wild-type, pH 7.5, 37ưC
8.9
cADP-ribose
mutant C253A, pH 7.5, 37ưC
16
cADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37ưC
0.025
CDP-choline

mutant R43A, pH 7.5, 37ưC
0.8
CDP-choline
mutant H97A, pH 7.5, temperature not specified in the publication
2.2
CDP-choline
mutant H111A, pH 7.5, 37ưC
5.3
CDP-choline
mutant H111N, pH 7.5, 37ưC
5.7
CDP-choline
mutant N110A, pH 7.5, 37ưC
25
CDP-choline
mutant F37A/L196A, pH 7.5, 37ưC
26
CDP-choline
mutant F37A/L196F, pH 7.5, 37ưC
29
CDP-choline
mutant L196A, pH 7.5, 37ưC
33
CDP-choline
mutant F37A, pH 7.5, 37ưC
37
CDP-choline
mutant F37A/L196F/C253A, pH 7.5, 37ưC
39
CDP-choline
mutant Q27H, pH 7.5, 37ưC
50
CDP-choline
wild-type, pH 7.5, 37ưC
50
CDP-choline
mutant F210A, pH 7.5, 37ưC
67.2
CDP-choline
wild-type, pH 7.5, temperature not specified in the publication
76
CDP-choline
mutant F37Y, pH 7.5, 37ưC
79
CDP-choline
mutant C253A, pH 7.5, 37ưC
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, 25ưC
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 37ưC
0.0027 - 630
ADP-D-ribose
0.007 - 32
CDP-ethanolamine
0.1
2',3'-cAMP

mutant N110A, pH 7.5, 37ưC
0.13
2',3'-cAMP
mutant R43A, pH 7.5, 37ưC
0.4
2',3'-cAMP
mutant F210A, pH 7.5, 37ưC
1.9
2',3'-cAMP
mutant Q27H, pH 7.5, 37ưC
3.9
2',3'-cAMP
mutant F37A/L196F, pH 7.5, 37ưC
4
2',3'-cAMP
mutant F37A/L196A, pH 7.5, 37ưC
4
2',3'-cAMP
mutant F37A/L196F/C253A, pH 7.5, 37ưC
6
2',3'-cAMP
mutant H111A, pH 7.5, 37ưC
7
2',3'-cAMP
mutant F37A, pH 7.5, 37ưC
9
2',3'-cAMP
mutant L196A, pH 7.5, 37ưC
18
2',3'-cAMP
mutant H97A, pH 7.5, temperature not specified in the publication
19
2',3'-cAMP
mutant H111N, pH 7.5, 37ưC
22
2',3'-cAMP
wild-type, pH 7.5, temperature not specified in the publication
25
2',3'-cAMP
wild-type, pH 7.5, 37ưC
28
2',3'-cAMP
mutant F37Y, pH 7.5, 37ưC
32
2',3'-cAMP
mutant C253A, pH 7.5, 37ưC
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 37ưC
0.005
ADP-D-ribose
mutant enzyme W28A/W46A, at pH 7.0 and 37ưC
0.23
ADP-D-ribose
mutant enzyme E116Q, at pH 7.0 and 37ưC
1.2
ADP-D-ribose
mutant enzyme R51Q, at pH 7.0 and 37ưC
1.7
ADP-D-ribose
mutant enzyme R84Q, at pH 7.0 and 37ưC
4.3
ADP-D-ribose
mutant enzyme E166Q, at pH 7.0 and 37ưC
13
ADP-D-ribose
mutant enzyme R111Q, at pH 7.0 and 37ưC
19.6
ADP-D-ribose
-
at pH 7.5 and 37ưC
50
ADP-D-ribose
mutant enzyme R196Q, at pH 7.0 and 37ưC
67
ADP-D-ribose
mutant enzyme E115Q, at pH 7.0 and 37ưC
72
ADP-D-ribose
mutant enzyme W28A, at pH 7.0 and 37ưC
81
ADP-D-ribose
mutant enzyme Q82A, at pH 7.0 and 37ưC
83
ADP-D-ribose
mutant enzyme D133A, at pH 7.0 and 37ưC
89
ADP-D-ribose
mutant enzyme W46A, at pH 7.0 and 37ưC
97
ADP-D-ribose
mutant enzyme L98A, at pH 7.0 and 37ưC
120
ADP-D-ribose
mutant enzyme E93Q, at pH 7.0 and 37ưC
230
ADP-D-ribose
mutant enzyme D133N, at pH 7.0 and 37ưC
300
ADP-D-ribose
mutant enzyme C139A, at pH 7.0 and 37ưC
390
ADP-D-ribose
mutant enzyme D164A, at pH 7.0 and 37ưC
530
ADP-D-ribose
wild type enzyme, at pH 7.0 and 37ưC
630
ADP-D-ribose
mutant enzyme D164N, at pH 7.0 and 37ưC
0.03
ADP-ribose

mutant R43A, pH 7.5, 37ưC
3
ADP-ribose
mutant H111A, pH 7.5, 37ưC
4.8
ADP-ribose
mutant F37A/L196F, pH 7.5, 37ưC
5.9
ADP-ribose
mutant H97A, pH 7.5, temperature not specified in the publication
6
ADP-ribose
mutant F37A/L196A, pH 7.5, 37ưC
9
ADP-ribose
mutant F210A, pH 7.5, 37ưC
11
ADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37ưC
12
ADP-ribose
mutant F37A, pH 7.5, 37ưC
15
ADP-ribose
mutant N110A, pH 7.5, 37ưC
29
ADP-ribose
mutant H111N, pH 7.5, 37ưC
52
ADP-ribose
mutant Q27H, pH 7.5, 37ưC
120
ADP-ribose
mutant L196A, pH 7.5, 37ưC
340
ADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
590
ADP-ribose
wild-type, pH 7.5, 37ưC
650
ADP-ribose
mutant F37Y, pH 7.5, 37ưC
1000
ADP-ribose
mutant C253A, pH 7.5, 37ưC
0.0001
cADP-ribose

mutant R43A, pH 7.5, 37ưC
0.008
cADP-ribose
mutant F210A, pH 7.5, 37ưC
0.028
cADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.07
cADP-ribose
mutant H111A, pH 7.5, 37ưC
0.13
cADP-ribose
mutant N110A, pH 7.5, 37ưC
0.15
cADP-ribose
mutant Q27H, pH 7.5, 37ưC
0.29
cADP-ribose
mutant H111N, pH 7.5, 37ưC
0.9
cADP-ribose
mutant F37A/L196A, pH 7.5, 37ưC
0.9
cADP-ribose
mutant L196A, pH 7.5, 37ưC
1.3
cADP-ribose
mutant F37A, pH 7.5, 37ưC
1.6
cADP-ribose
mutant F37A/L196F, pH 7.5, 37ưC
4
cADP-ribose
wild-type, pH 7.5, 37ưC
4.1
cADP-ribose
mutant F37Y, pH 7.5, 37ưC
35.5
cADP-ribose
mutant F37A/L196F/C253A, pH 7.5, 37ưC
44
cADP-ribose
mutant C253A, pH 7.5, 37ưC
0.002
CDP-choline

mutant H97A, pH 7.5, temperature not specified in the publication
0.006
CDP-choline
mutant R43A, pH 7.5, 37ưC
0.3
CDP-choline
mutant H111A, pH 7.5, 37ưC
1.5
CDP-choline
mutant N110A, pH 7.5, 37ưC
2
CDP-choline
mutant H111N, pH 7.5, 37ưC
4
CDP-choline
mutant F210A, pH 7.5, 37ưC
5.6
CDP-choline
wild-type, pH 7.5, temperature not specified in the publication
14
CDP-choline
mutant Q27H, pH 7.5, 37ưC
17
CDP-choline
mutant F37A/L196F, pH 7.5, 37ưC
21
CDP-choline
mutant F37A/L196A, pH 7.5, 37ưC
22
CDP-choline
mutant F37A/L196F/C253A, pH 7.5, 37ưC
34
CDP-choline
mutant F37A, pH 7.5, 37ưC
62
CDP-choline
mutant L196A, pH 7.5, 37ưC
150
CDP-choline
wild-type, pH 7.5, 37ưC
160
CDP-choline
mutant C253A, pH 7.5, 37ưC
180
CDP-choline
mutant F37Y, pH 7.5, 37ưC
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
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.