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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-dGDP + H2O
8-oxo-dGMP + phosphate
-
-
?
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
-
?
NAADP+ + H2O
nicotinic acid mononucleotide + phosphate
-
-
?
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 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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
NAADP+ + 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
-
-
-
?
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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.
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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
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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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