EC - 8-oxo-dGDP phosphatase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
8-oxo-dGDP phosphatase
Other name:
Systematic name:
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, 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, ADP-ribose diphosphatase) [4]. The human enzyme NUDT18 also hydrolyses 8-oxo-dADP and 2-hydroxy-dADP, the latter at a slower rate [6].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0044716 , GO:0044715
UniProtKB/Swiss-Prot: (13) [show] [UniProt]


  1. Ishibashi, T., Hayakawa, H., Ito, R., Miyazawa, M., Yamagata, Y., Sekiguchi, M.
    Mammalian enzymes for preventing transcriptional errors caused by oxidative damage.
    Nucleic Acids Res. 33 : 3779-3784 (2005). [PMID: 16002790]
  2. Ishibashi, T., Hayakawa, H., Sekiguchi, M.
    A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides.
    EMBO Rep. 4 : 479-483 (2003). [PMID: 12717453]
  3. Kamiya, H., Hori, M., Arimori, T., Sekiguchi, M., Yamagata, Y., Harashima, H.
    NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad substrate specificity.
    DNA Repair (Amst.) 8 : 1250-1254 (2009). [PMID: 19699693]
  4. Ito, R., Sekiguchi, M., Setoyama, D., Nakatsu, Y., Yamagata, Y., Hayakawa, H.
    Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 protein.
    J. Biochem. 149 : 731-738 (2011). [PMID: 21389046]
  5. Zha, M., Zhong, C., Peng, Y., Hu, H., Ding, J.
    Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity.
    J. Mol. Biol. 364 : 1021-1033 (2006). [PMID: 17052728]

[EC created 2012]