UniProt functional annotation for P08337

UniProt code: P08337.

Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
Function:		Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate. {ECO:0000269|PubMed:1309939, ECO:0000269|PubMed:15850400}.
Catalytic activity:		Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+); Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55; Evidence={ECO:0000269|PubMed:15850400};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
Biophysicochemical properties:		Kinetic parameters: KM=0.058 uM for 8-oxo-dGDP {ECO:0000269|PubMed:15850400}; KM=170 uM for dGDP {ECO:0000269|PubMed:15850400}; KM=0.081 uM for 8-oxo-dGTP {ECO:0000269|PubMed:15850400}; KM=1100 uM for GTP {ECO:0000269|PubMed:15850400}; KM=0.045 uM for 8-oxo-GDP {ECO:0000269|PubMed:15850400}; KM=0.26 uM for 8-oxo-GTP {ECO:0000269|PubMed:15850400}; Vmax=3.7 pmol/min/ng enzyme toward 8-oxo-dGDP {ECO:0000269|PubMed:15850400}; Vmax=5.9 pmol/min/ng enzyme toward dGDP {ECO:0000269|PubMed:15850400}; Vmax=20 pmol/min/ng enzyme toward 8-oxo-dGTP {ECO:0000269|PubMed:15850400}; Vmax=44 pmol/min/ng enzyme toward GTP {ECO:0000269|PubMed:15850400}; Vmax=4.8 pmol/min/ng enzyme toward 8-oxo-GDP {ECO:0000269|PubMed:15850400}; Vmax=22 pmol/min/ng enzyme toward 8-oxo-GTP {ECO:0000269|PubMed:15850400};
Subunit:		Monomer. {ECO:0000269|PubMed:9063868}.
Similarity:		Belongs to the Nudix hydrolase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.