8-oxo-dGTP diphosphatase

8-oxo-dGTP diphosphatase (EC 3.6.1.55, MutT, 7,8-dihydro-8-oxoguanine triphosphatase, 8-oxo-dGTPase, 7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase) is an enzyme with systematic name 8-oxo-dGTP diphosphohydrolase.[1][2][3][4] This enzyme catalyses the following chemical reaction:

8-oxo-dGTP diphosphatase
Identifiers
EC no.3.6.1.55
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
8-oxo-dGTP + H2O 8-oxo-dGMP + diphosphate

This enzyme requires Mg2+.

References

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  1. ^ Ito R, Hayakawa H, Sekiguchi M, Ishibashi T (May 2005). "Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools". Biochemistry. 44 (17): 6670–4. doi:10.1021/bi047550k. PMID 15850400.
  2. ^ Yoshimura K, Ogawa T, Ueda Y, Shigeoka S (October 2007). "AtNUDX1, an 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase, is responsible for eliminating oxidized nucleotides in Arabidopsis". Plant & Cell Physiology. 48 (10): 1438–49. doi:10.1093/pcp/pcm112. PMID 17804481.
  3. ^ 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 (January 2010). "Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base". The Journal of Biological Chemistry. 285 (1): 444–52. doi:10.1074/jbc.m109.066373. PMC 2804192. PMID 19864691.
  4. ^ 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 & Genetic Systems. 85 (4): 287–95. doi:10.1266/ggs.85.287. PMID 21178309.
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