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Information on EC 3.6.1.13 - ADP-ribose diphosphatase
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3.6.1.13 ADP-ribose diphosphataseSpecify your search results
Word Map
- 3.6.1.13
- pyrophosphatases
-
melastatin
-
mutt-related
-
ribose-5'-phosphate
- 8-oxo-dgdp
- adp-sugars
The enzyme appears in viruses and cellular organisms
Synonyms
nudt5, nudt9, adp-ribose pyrophosphatase, adprase, atnudt7, adpribase-mn, atnudx7, adp-ribose hydrolase, nudt5 protein, adpr pyrophosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADP-ribose pyrophosphatase
ADP-ribose pyrophosphatase-I
ADP-ribose/CDP-alcohol diphosphatase
ADP-ribose/NADH pyrophosphohydrolase
ADPR pyrophosphatase
ADPRase
ADPRase-I
AT4G12720
AtNUDX7
CinA
MT1739
MtADPRase
MutT/nudix family protein
NadM-Nudix
Ndx2
Ndx4
NMN adenylyltransferase/ADP-ribose pyrophosphatase
Nudix hydrolase 7
NUDT5
additional information
additional information
-
the enzyme belongs to the Nudix, nucleotide diphosphate X,pyrophosphatase superfamily
additional information
-
the enzyme is a member of a superfamily of Nudix hydrolases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
-
-
-
-
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
molecular catalytic mechanism involving Arg51, Arg111, Glu112, and Glu116, active site structure, substrate binding involving Arg51, Leu98, Trp28 and Trp46 and transition-state structure, structure-function relationship, and kinetic analysis
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
substrate binding mode in the active site of the ADPRase domain and catalytic mechanism
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
substrate binding mode in the active site of the ADPRase domain and catalytic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
ADP-D-ribose ribophosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9024-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
ADPribose 2'-phosphate + H2O
adenosine 2',5'-diphosphate + D-ribose 5-phosphate
-
-
-
?
CDP-glucose + H2O
CMP + glucose 5-phosphate
-
at 5% of the activity with ADPribose
-
?
CDP-ribose + H2O
CMP + D-ribose 5-phosphate
-
kcat/Km is 2.5% of the kcat/Km for ADP-ribose
-
?
diadenosine 5',5''-diphosphate + H2O
?
20% the activity with ADP-ribose
-
?
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
-
?
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
-
?
UDP-galactose + H2O
UDP + galactose
7% of the activity with ADP-ribose
-
?
ADP-alpha-D-ribose + H2O
AMP + D-ribose 5-phosphate
-
-
?
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
-
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
-
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
substrate binding structure, overview
-
?
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 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
-
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
highly specific substrate
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
preferred substrate, substrate recognition and binding structure, overview
-
?
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
-
?
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
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
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
-
-
-
?
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
?
-
ADPRibase-Mn and ADPRibase II, very low activity with ADPRibase I in presence of Mn2+
-
?
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
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
-
?
NADH + H2O
?
-
ADPRibase I, ADPribase II and ADPRibase-Mn in presence of Mn2+
-
?
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
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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-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
-
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the enzyme plays a key role in regulating the intracellular ADPribose levels, and prevents nonenzymatic ADP-ribosylation
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Zn2+
additional information
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+
-
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+
-
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, 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
Mn2+
-
divalent cation required, Mg2+ or Mn2+. Mg2+ is much more effective than Mn2+
Mn2+
the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors
Mn2+
-
maximal activity at 0.02-0.05 mM with a steep decrease at increasing pH-values, Mg2+ or Mn2+ required
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+
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
Mn2+
-
absolute requirement for divalent metal ion is satisfied by Mn2+, Co2+ or 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+
divalent cation required, Zn2+ results in 9% of the activity observed in presence of Mg2+
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-amino-3-(morpholin-4-yl)-1,2,3-oxadiazol-3-ium
-
3-morpholinosynonimine increases Km and slightly decreases Vmax
8-oxo-dGDP
the ADP-ribose cleavage is competitively inhibited by 8-oxo-dGDP (68% relative cleavage efficiency at 0.01 mM)
8-oxo-dGMP
the ADP-ribose cleavage is competitively inhibited by 8-oxo-dGMP (89% relative cleavage efficiency at 0.01 mM)
ADP-ribose
the 8-oxo-dGDP cleavage is competitively inhibited by ADP-ribose (22% relative cleavage efficiency at 0.005 mM)
AMP
the 8-oxo-dGDP cleavage is competitively inhibited by AMP (30% relative cleavage efficiency at 0.005 mM)
fluoride
-
inhibition of Mg2+-dependent activity of ADP-ribose pyrophosphatase. the Mn2+-dependent activity is not affected by fluoride
N-acetyl-p-benzoquinoneimine
1 mM, almost complete inhibition of activity towards ADPribose. The inhibitor is a useful tool for distinguishing the specific ADP-ribose diphosphatase from the less specific ADP-sugar diphosphatases
N-acetyl-p-benzoquinoneimine
-
decreases Vmax to 30% of control values and increases the Km for ADPribose 2-3fold
nitroprusside
-
nitroprusside in presence of dithiothreitol diminishes Vmax and increases Km
nitroprusside
-
sodium nitroprusside increases Km without appreciably affecting Vmax
additional information
no inhibitory effect is observed with 8-oxo-dGMP
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nitric oxide
-
NO stimulates non-enzymatic ADP-ribosylation, at cysteine residues in the presence of reductant, of NUDT5 using ADP-ribose and consequently activates its ADPRase activity. ADPRase activity in J774 macrophage cells is increased by the treatment with SNP, an exogenous NO generator, or TNF-alpha/IFN-gamma, endogenous NO inducers. NO has a regulatory role, overview
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
Molecular docking based virtual screening of the breast cancer target NUDT5.
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.
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.
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
The high expression of MTH1 and NUDT5 predict a poor survival and are associated with malignancy of esophageal squamous cell carcinoma.
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.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.76
2',3'-cAMP
wild-type, pH 7.5, temperature not specified in the publication
1.7
2',3'-cAMP
mutant H97A, pH 7.5, temperature not specified in the publication
0.053
ADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.071
ADP-ribose
mutant H97A, pH 7.5, temperature not specified in the publication
0.19
cADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
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
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.9
2',3'-cAMP
wild-type, pH 7.5, temperature not specified in the publication
29.7
2',3'-cAMP
mutant H97A, pH 7.5, temperature not specified in the publication
0.4
ADP-ribose
mutant H97A, pH 7.5, temperature not specified in the publication
18
ADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.0005
cADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.8
CDP-choline
mutant H97A, pH 7.5, temperature not specified in the publication
67.2
CDP-choline
wild-type, pH 7.5, temperature not specified in the publication
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
2',3'-cAMP
mutant H97A, pH 7.5, temperature not specified in the publication
22
2',3'-cAMP
wild-type, pH 7.5, temperature not specified in the publication
0.0011
ADP
mutant H97A, pH 7.5, temperature not specified in the publication
5.9
ADP-ribose
mutant H97A, pH 7.5, temperature not specified in the publication
340
ADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.028
cADP-ribose
wild-type, pH 7.5, temperature not specified in the publication
0.002
CDP-choline
mutant H97A, pH 7.5, temperature not specified in the publication
5.6
CDP-choline
wild-type, pH 7.5, temperature not specified in the publication
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
activity at pH 8.0 is about 90% of the activity at pH 6.5 and at pH 9.0, activity with ADP-ribose
7 - 9
8.2
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10
pH 4.5: about 55% of maximal activity, pH 10.0: about 50% of maximal activity, activity with ADP-mannose
6 - 10
pH 6.0: about 25% of maximal activity, pH 10.0: about 60% of maximal activity, activity with ADP-ribose
7 - 9
-
linearly decreasing activity profile from pH 7 to pH 9, with activity at pH 9 being 50% of that at pH 7
7.5 - 10
-
pH 7.5: about 60% of maximal activity with ADP-ribose, about 50% of maximal activity with ADP-mannose, pH 10.0: about 70% of maximal activity with activity with ADP-ribose or ADP-mannose
8 - 10
pH 8.0: about 40% of maximal activity, pH 10.0: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 75
-
rate of hydrolysis of ADPribose is 15fold higher than at 37°C, incubations at higher temperatures are impractical because of the spontaneous hydrolysis of the substrate
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities
UniProt
brenda
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity in leaves is lower than in stem and root, AtNUDT10
brenda
-
activity in roots is lower than in leaves and stem, AtNUDT6
brenda
-
activity in leaves is lower than in stem and root, AtNUDT10
brenda
-
activity in roots is lower than in leaves and stem, AtNUDT6
brenda
-
activity in leaves is lower than in stem and root, AtNUDT10
brenda
-
activity in roots is lower than in leaves and stem, AtNUDT6
brenda