3.6.1.58: 8-oxo-dGDP phosphatase
This is an abbreviated version!
For detailed information about 8-oxo-dGDP phosphatase, go to the full flat file.
Reaction
Synonyms
MTH3, MutT homologue 3, NDX-1, NUDT, NUDT5
ECTree
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Substrates Products
Substrates Products on EC 3.6.1.58 - 8-oxo-dGDP phosphatase
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REACTION DIAGRAM
5-formyl-dUDP + H2O
5-formyl-dUMP + phosphate
kcat/KM is 30% of the wild-type value
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8-oxo-dADP + H2O
8-oxo-dAMP + phosphate
8-oxo-dADP is hydrolyzed slightly more efficiently than 8-oxo-dGDP
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8-oxo-dGTP + H2O
8-oxo-dGDP + phosphate
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the enzyme hardly cleaves 8-oxo-dGTP
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2-hydroxy-dADP + H2O
2-hydroxy-dAMP + phosphate
kcat/KM is 15% of the wild-type value
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?
8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
NUDT5 might have a much greater role than MTH1 in preventing the occurrence of mutations that are caused by the misincorporation of 8-oxoguanine in human cells. NUDT5 has another role in promoting the MTH1 reaction, in removing its inhibitor, 8-oxo-dGDP
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8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
8-oxo-dGDP is a specific substrate for the NUDT5 protein
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8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
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ADP-ribose is a better substrate for NUDT5 compared with oxidized guanine nucleotides
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8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
NUDT5 protein is a hydrolyzing enzyme with broad substrate specificity for oxidized deoxyribonucleoside diphosphates
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8-oxo-GDP + H2O
8-oxo-GMP + phosphate
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8-oxoGDP is a specific substrate for the human NUDT5 protein
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8-oxo-GDP + H2O
8-oxo-GMP + phosphate
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the enzyme can degrade 8-oxo-GDP as efficiently as 8-oxo-dGDP
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dGDP + H2O
dGMP + phosphate
poor substrate. Vmax/Km is 32% of value for 8-oxo-dGDP
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NDX-1 does not hydrolyze 8-oxo-dGTP, 2-hydroxy-dATP or 2-hydroxy-dADP
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additional information
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NUDT5 does not degrade 8-oxo-GTP to the monophosphate (Vmax/Km is 0.7% of the activity with 8-oxo-GDP)
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additional information
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NUDT5 hydrolyses 8-oxo-dGTP only at very low levels (Vmax/Km is 0.07% of the value for 8-oxo-dGDP)
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additional information
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the bifunctional enzyme also hydrolyses ADP-ribose to ADP-ribose and ribose 5-phosphate (cf. EC 3.6.1.13)
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additional information
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the hydrolyses of 2-hydroxy-dADP and 5-formyl-dUDP are less effective, with 0.4- and 0.5-fold efficiencies relative to that of 8-oxo-dGDP, respectively. The hydrolyses of the triphosphate derivatives are less efficient than those of the diphosphate counterparts
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