Member database | CDD |
CDD type | domain |
Short name | MutT_pyrophosphohydrolase |
Set | Nudix_Hydrolase |
Description
The MutT pyrophosphohydrolase is a prototypical Nudix hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the Nudix motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.
[3, 5, 1, 2, 4]References
1.The role of the mutT gene of Escherichia coli in maintaining replication fidelity. Fowler RG, Schaaper RM. FEMS Microbiol Rev 21, 43-54, (1997). PMID: 9299701
2.MutT-related error avoidance mechanism for DNA synthesis. Sekiguchi M. Genes Cells 1, 139-45, (1996). PMID: 9140059
3.The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). McLennan AG. Int. J. Mol. Med. 4, 79-89, (1999). PMID: 10373642
4.The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). Michaels ML, Miller JH. J. Bacteriol. 174, 6321-5, (1992). View articlePMID: 1328155
External Links
Representative structure
7ww6: Crystal structure of MutT-8-oxo-dGTP complex: Reaction for 20 min in 5 mM Mn2+