3.6.1.55 5-methyl-dCTP + H2O - Mycolicibacterium smegmatis 5-methyl-dCMP + diphosphate - ? 422679 3.6.1.55 5-methyl-dCTP + H2O - Mycolicibacterium smegmatis mc(2)155 5-methyl-dCMP + diphosphate - ? 422679 3.6.1.55 7,8-dihydro-8-oxo-GTP + H2O - Bartonella henselae 7,8-dihydro-8-oxo-GMP + diphosphate - ? 420144 3.6.1.55 7-deaza-dGTP + H2O - Escherichia coli 7-deaza-dGMP + diphosphate - ? 455120 3.6.1.55 8-bromo-dGTP + H2O high activity Escherichia coli 8-bromo-dGMP + diphosphate - ? 455126 3.6.1.55 8-bromo-dITP + H2O low activity Escherichia coli 8-bromo-dIMP + diphosphate - ? 455127 3.6.1.55 8-chloro-dGTP + H2O high activity Escherichia coli 8-choro-dGMP + diphosphate - ? 455128 3.6.1.55 8-oxo-dGDP + H2O - Escherichia coli 8-oxo-dGMP + phosphate - ? 384011 3.6.1.55 8-oxo-dGDP + H2O - Hordeum vulgare subsp. vulgare 8-oxo-dGMP + phosphate - ? 384011 3.6.1.55 8-oxo-dGTP + H2O - Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O - Homo sapiens 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O - Ciona intestinalis 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O - Arabidopsis thaliana 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O - Mycolicibacterium smegmatis 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O high activity Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O 8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O 8-oxoguanine (8-oxo-7,8-dihydroguanine) is produced in nucleic acids as well as in nucleotide pools of cells, by reactive oxygen species normally formed during cellular metabolic processes. MutT protein of Escherichia coli specifically degrades 8-oxoGua-containing deoxyribo- and ribonucleoside triphosphates to corresponding nucleoside monophosphates, thereby preventing misincorporation of 8-oxoguanine into DNA and RNA, which would cause mutation and phenotypic suppression, respectively Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O prevents replicational errors by degrading 8-oxo-dGTP, a potent mutagenic substrate for DNA synthesis. Elimination from the nucleotide pool of the oxidized form of guanine nucleotide is important for the high fidelity of DNA synthesis Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O the MutT protein specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP), which are otherwise incorporated in DNA and RNA opposite template A. This cleaning of the nucleotide pools decreases both DNA replication and transcription errors Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O the oxidized nucleotide precursors 8-oxo-dGTP is readily incorporated into nascent DNA strands during replication, which would cause base substitution mutations. 8-oxo-dGTP diphosphatase (8-oxo-dGTP diphosphatase) enzyme has the potential to prevent mutations by 8-oxo-dGTP in Ciona intestinalis Ciona intestinalis 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O experimental thermodynamic data of 8-oxo-dGMP and dGMP binding to MutT show largely different affinities, even though the difference of chemical structures of the two molecules is very small. Enthalpic and entropic components of the binding free energy suggest drastically different conformational responses of MutT for binding the two molecules. These different conformational responses appear to be the mechanism for the enhanced recognition/discrimination between the two molecules despite a small difference of the chemical structures. Transition between two minimum energy substrates, both existing in the native state of the protein, is involved in high-resolution molecular recognition Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O MutT exhibits high substrate specificity for 8-oxoguanine nucleotides by the ligand-induced conformational change Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O specfic for the MutT protein hydrolyses other dNTPs and GTP with lower Vmax and extremely high Km-values Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O the MutT protein has an ability to cleave the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates. 8-oxo-dGTP is hydrolysed with the highest efficiency Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O the specific activity for 8-oxo-dGTP is greater than that for unoxidized dATP and dGTP Ciona intestinalis 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O the unusually high affinity of MutT for 8-oxo-nucleotides is due not only to interactions with the altered 8-oxo or 7-NH positions on guanine, but results primarily from diffuse structural changes which tighten the protein structure around the 8-oxo-nucleotide Escherichia coli 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O - Mycolicibacterium smegmatis mc(2)155 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O - Escherichia coli CC101 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dGTP + H2O MutT molecules are needed for keeping the spontaneous mutation frequency at the normal level. The MutT functions are not needed under anaerobic condition, yet the level of the MutT protein in cell is kept constant, probably for preparing for sudden changes of oxygen pressure Escherichia coli CC101 8-oxo-dGMP + diphosphate - ? 165301 3.6.1.55 8-oxo-dITP + H2O high activity Escherichia coli 8-oxo-dIMP + diphosphate - ? 455129 3.6.1.55 8-oxo-GDP + H2O - Escherichia coli 8-oxo-GMP + phosphate - ? 384012 3.6.1.55 8-oxo-GDP + H2O - Homo sapiens 8-oxo-GMP + phosphate - ? 384012 3.6.1.55 8-oxo-GTP + H2O - Escherichia coli 8-oxo-GMP + diphosphate - ? 165300 3.6.1.55 8-oxo-GTP + H2O - Arabidopsis thaliana 8-oxo-GMP + diphosphate - ? 165300 3.6.1.55 8-oxo-GTP + H2O the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state Escherichia coli 8-oxo-GMP + diphosphate - ? 165300 3.6.1.55 8-thio-dGTP + H2O highest activity Escherichia coli 8-thio-dGMP + diphosphate - ? 455132 3.6.1.55 8-thio-dITP + H2O high activity Escherichia coli 8-thio-dIMP + diphosphate - ? 455133 3.6.1.55 9-deaza-dGTP + H2O high activity Escherichia coli 9-deaza-dGMP + diphosphate - ? 455134 3.6.1.55 CTP + H2O - Mycolicibacterium smegmatis CMP + diphosphate - ? 141405 3.6.1.55 CTP + H2O - Mycolicibacterium smegmatis mc(2)155 CMP + diphosphate - ? 141405 3.6.1.55 dATP + H2O - Arabidopsis thaliana dAMP + diphosphate - ? 141404 3.6.1.55 dCTP + H2O - Mycolicibacterium smegmatis dCMP + diphosphate - ? 141201 3.6.1.55 dCTP + H2O - Mycolicibacterium smegmatis mc(2)155 dCMP + diphosphate - ? 141201 3.6.1.55 dGDP + H2O - Escherichia coli dGMP + phosphate - ? 384600 3.6.1.55 dGTP + H2O - Escherichia coli dGMP + diphosphate - ? 141253 3.6.1.55 dGTP + H2O - Arabidopsis thaliana dGMP + diphosphate - ? 141253 3.6.1.55 dGTP + H2O low activity Escherichia coli dGMP + diphosphate - ? 141253 3.6.1.55 GDP + H2O - Escherichia coli GMP + phosphate - ? 93274 3.6.1.55 GTP + H2O - Escherichia coli GMP + diphosphate - ? 141252 3.6.1.55 GTP + H2O - Arabidopsis thaliana GMP + diphosphate - ? 141252 3.6.1.55 additional information no activity with dITP Escherichia coli ? - - 89 3.6.1.55 additional information in addition the enzyme hydrolyzes all four of the unoxidized nucleoside triphosphates, with a preference for dATP Ciona intestinalis ? - ? 89 3.6.1.55 additional information no hydrolysis of 2-hydroxy-dATP Escherichia coli ? - ? 89 3.6.1.55 additional information no hydrolysis of 2-hydroxy-dATP and 8-oxo-dATP, (R)-8,5'-cyclo-dATP, other forms of oxidized dATP, 5-oxo-dCTP and 5-formyl-dUTP are not hydrolyzed by the MutT enzyme Escherichia coli ? - ? 89 3.6.1.55 additional information no hydrolysis of 2-hydroxy-dATP, 8-oxo-dGDP and 2-oxo-dAMP. The enzyme oxidizes all four unoxidized nucleoside triphosphates with a preference for dATP Ciona intestinalis ? - ? 89 3.6.1.55 additional information the enzyme does not cleave 8-oxo-dGDP Homo sapiens ? - ? 89 3.6.1.55 additional information enzyme additionally shows Ap4A and guanosine-3',5'-tetraphosphate diphosphohydrolase activities Hordeum vulgare subsp. vulgare ? - ? 89 3.6.1.55 additional information no activity with ATP, 2-hydroxy-ATP, and 2-hydroxy-dATP Arabidopsis thaliana ? - - 89