2-hydroxy-dATP diphosphatase

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2-hydroxy-dATP diphosphatase
Identifiers
EC number 3.6.1.56
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

2-hydroxy-dATP diphosphatase (EC 3.6.1.56, NUDT1, MTH1, MTH2, oxidized purine nucleoside triphosphatase, (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase) is an enzyme with systematic name 2-hydroxy-dATP diphosphohydrolase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

2-hydroxy-dATP + H2O 2-hydroxy-dAMP + diphosphate

The enzyme hydrolyses oxidizes purine nucleoside triphosphates.

References[edit]

  1. ^ Sakumi, K.; Furuichi, M.; Tsuzuki, T.; Kakuma, T.; Kawabata, S.; Maki, H.; Sekiguchi, M. (1993). "Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis". J. Biol. Chem. 268 (31): 23524–23530. PMID 8226881. 
  2. ^ Kakuma, T.; Nishida, J.; Tsuzuki, T.; Sekiguchi, M. (1995). "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 (43): 25942–25948. doi:10.1074/jbc.270.43.25942. PMID 7592783. 
  3. ^ Fujikawa, K.; Kamiya, H.; Yakushiji, H.; Fujii, Y.; Nakabeppu, Y.; Kasai, H. (1999). "The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein". J. Biol. Chem. 274 (26): 18201–18205. doi:10.1074/jbc.274.26.18201. PMID 10373420. 
  4. ^ Sakai, Y.; Furuichi, M.; Takahashi, M.; Mishima, M.; Iwai, S.; Shirakawa, M.; Nakabeppu, Y. (2002). "A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1". J. Biol. Chem. 277: 8579–8587. doi:10.1074/jbc.M110566200. PMID 11756418. 
  5. ^ Fujikawa, K.; Kamiya, H.; Yakushiji, H.; Nakabeppu, Y.; Kasai, H. (2001). "Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP". Nucleic Acids Res. 29: 449–454. doi:10.1093/nar/29.2.449. PMC 29672Freely accessible. PMID 11139615. 

External links[edit]