|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 2-hydroxy-dATP diphosphatase
Enzyme Commission Synonyms: NUDT1, MTH1, MTH2, oxidized purine nucleoside triphosphatase, (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase
Enzyme Commission Summary:
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 184.108.40.206, 8-oxo-dGTP diphosphatase) [Fujikawa99].
Fujikawa99: 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);18201-5. PMID: 10373420
Kakuma95: 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);25942-8. PMID: 7592783
Sakai02a: 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(10);8579-87. PMID: 11756418
Sakumi93a: 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);23524-30. PMID: 8226881
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493