The enzyme catalyses the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP thereby preventing translational errors caused by oxidative damage. The preferred in vivo substrate is not known. The enzyme does not degrade 8-oxo-dGTP and 8-oxo-GTP to the monophosphates (cf. EC 3.6.1.55, 8-oxo-dGTP diphosphatase) [1,2]. Ribonucleotide diphosphates and deoxyribonucleotide diphosphates are hydrolysed with broad specificity. The bifunctional enzyme NUDT5 also hydrolyses ADP-ribose to AMP and D-ribose 5-phosphate (cf. EC 3.6.1.13, ADP-ribose diphosphatase) . The human enzyme NUDT18 also hydrolyses 8-oxo-dADP and 2-hydroxy-dADP, the latter at a slower rate .
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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SYSTEMATIC NAME
IUBMB Comments
8-oxo-dGDP phosphohydrolase
The enzyme catalyses the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP thereby preventing translational errors caused by oxidative damage. The preferred in vivo substrate is not known. The enzyme does not degrade 8-oxo-dGTP and 8-oxo-GTP to the monophosphates (cf. EC 3.6.1.55, 8-oxo-dGTP diphosphatase) [1,2]. Ribonucleotide diphosphates and deoxyribonucleotide diphosphates are hydrolysed with broad specificity. The bifunctional enzyme NUDT5 also hydrolyses ADP-ribose to AMP and D-ribose 5-phosphate (cf. EC 3.6.1.13, ADP-ribose diphosphatase) [4]. The human enzyme NUDT18 also hydrolyses 8-oxo-dADP and 2-hydroxy-dADP, the latter at a slower rate [6].
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
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
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
the knockdown of the MTH1, MTH2, and NUDT5 proteins increases the A:T to C:G substitution mutations induced by 8-hydroxy-dGTP. In addition, the increase in the induced mutation frequency is more evident in the triple-knockdown cells
is produced in cells by reactive oxygen species normally formed during cellular metabolic processes. This oxidized base can pair with both adenine and cytosine, and thus the existence of this base in messenger RNA would cause translational errors. The elimination of 8-oxoguanine-containing ribonucleotides from the precursor pool is important to ensure accurate protein synthesis. Both NUDT5 and MTH1 are involved in this process in human cells
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of full-length hNUDT5 are grown at 4°C using the hanging-drop vapor diffusion method. Crystal structures of hNUDT5 in apo form, in complex with ADP-ribose, and in complex with AMP with bound Mg2+
the increase in the production of erroneous proteins by oxidative damage is 28fold over the wild-type cells in Escherichia coli mutT deficient cells. By the expression of NUDT5 in the cells, it is reduced to 1.4fold
when NUDT5 is expressed in Escherichia coli mutT-cells as a His-tagged protein, the increased frequency of spontaneous mutations is decreased to normal levels
Suppression of mutagenesis by 8-hydroxy-2'-deoxyguanosine 5'-triphosphate (7,8-dihydro-8-oxo-2'-deoxyguanosine 5'-triphosphate) by human MTH1, MTH2, and NUDT5
NDX-1 protein hydrolyzes 8-oxo-7,8-dihydrodeoxyguanosine-5-diphosphate to sanitize oxidized nucleotides and prevent oxidative stress in Caenorhabditis elegans
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3.6.1.58 8-oxo-dGDP phosphatase
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