|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 8-oxo-dGTP diphosphatase
Enzyme Commission Synonyms: MutT, 7,8-dihydro-8-oxoguanine triphosphatase, 8-oxo-dGTPase, 7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase
Enzyme Commission Summary:
The MutT protein hydrolyses the phosphoanhydride bond between the α and β phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA . It does not hydrolyse 2-hydroxy-dATP (cf. EC 126.96.36.199, 2-hydroxy-dATP diphosphatase) [Yonekura10]. Requires Mg2+.
Ito05a: Ito R, Hayakawa H, Sekiguchi M, Ishibashi T (2005). "Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools." Biochemistry 44(17);6670-4. PMID: 15850400
Kang95a: Kang D, Nishida J, Iyama A, Nakabeppu Y, Furuichi M, Fujiwara T, Sekiguchi M, Takeshige K (1995). "Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria." J Biol Chem 270(24);14659-65. PMID: 7782328
Nakamura10a: Nakamura T, Meshitsuka S, Kitagawa S, Abe N, Yamada J, Ishino T, Nakano H, Tsuzuki T, Doi T, Kobayashi Y, Fujii S, Sekiguchi M, Yamagata Y (2010). "Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base." J Biol Chem 285(1);444-52. PMID: 19864691
Yonekura10: Yonekura S, Sanada U, Zhang-Akiyama QM (2010). "CiMutT, an asidian MutT homologue, has a 7, 8-dihydro-8-oxo-dGTP pyrophosphohydrolase activity responsible for sanitization of oxidized nucleotides in Ciona intestinalis." Genes Genet Syst 85(4);287-95. PMID: 21178309
Yoshimura07a: Yoshimura K, Ogawa T, Ueda Y, Shigeoka S (2007). "AtNUDX1, an 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase, is responsible for eliminating oxidized nucleotides in Arabidopsis." Plant Cell Physiol 48(10);1438-49. PMID: 17804481
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