EC 3.6.1.56 - 2-hydroxy-dATP diphosphatase

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IntEnz Enzyme Nomenclature
EC 3.6.1.56

Names

Accepted name:
2-hydroxy-dATP diphosphatase
Other names:
NUDT1
MTH1
MTH2
oxidized purine nucleoside triphosphatase
(2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase
Systematic name:
2-hydroxy-dATP diphosphohydrolase

Reaction

Comments:

The enzyme hydrolyses oxidized purine nucleoside triphosphates such as 2-hydroxy-dATP, thereby preventing their misincorporation into DNA. It can also recognize 8-oxo-dGTP and 8-oxo-dATP, but with lower efficiency (cf. EC 3.6.1.55, 8-oxo-dGTP diphosphatase) [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008828
UniProtKB/Swiss-Prot:

References

  1. Sakumi, K., Furuichi, M., Tsuzuki, T., Kakuma, T., Kawabata, S., Maki, H., Sekiguchi, M.
    Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis.
    J. Biol. Chem. 268 : 23524-23530 (1993). [PMID: 8226881]
  2. Kakuma, T., Nishida, J., Tsuzuki, T., Sekiguchi, M.
    Mouse MTH1 protein with 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphatase activity that prevents transversion mutation. cDNA cloning and tissue distribution.
    J. Biol. Chem. 270 : 25942-25948 (1995). [PMID: 7592783]
  3. Fujikawa, K., Kamiya, H., Yakushiji, H., Fujii, Y., Nakabeppu, Y., Kasai, H.
    The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein.
    J. Biol. Chem. 274 : 18201-18205 (1999). [PMID: 10373420]
  4. Sakai, Y., Furuichi, M., Takahashi, M., Mishima, M., Iwai, S., Shirakawa, M., Nakabeppu, Y.
    A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1.
    J. Biol. Chem. 277 : 8579-8587 (2002). [PMID: 11756418]
  5. Fujikawa, K., Kamiya, H., Yakushiji, H., Nakabeppu, Y., Kasai, H.
    Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP.
    Nucleic Acids Res. 29 : 449-454 (2001). [PMID: 11139615]

[EC 3.6.1.56 created 2011]