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2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
2-hydroxy-dATP + 2 H2O
2-hydroxy-dAMP + 2 phosphate
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
2-hydroxy-rATP + H2O
2-hydroxy-rAMP + diphosphate
-
-
-
?
2-oxo-dATP + H2O
2-oxo-dAMP + diphosphate
-
-
-
-
?
8-oxo-ATP + H2O
8-oxo-AMP + diphosphate
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
-
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-GDP + H2O
8-oxo-GMP + phosphate
-
Vmax/Km is 4% of the value for 8-oxo-GTP
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
8-oxo-rATP + H2O
8-oxo-rAMP + diphosphate
-
-
-
?
8-oxo-rGTP + H2O
8-oxo-rGMP + diphosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
Ap4A + H2O
AMP + ?
-
-
-
-
?
ATP + H2O
AMP + diphosphate
-
-
-
-
?
dADP + H2O
dAMP + phosphate
-
-
-
-
?
dATP + H2O
dAMP + diphosphate
-
-
-
-
?
dGDP + H2O
dGMP + phosphate
-
-
-
-
?
dGTP + H2O
dGMP + diphosphate
GDP + H2O
GMP + phosphate
-
-
-
-
?
GTP + H2O
GMP + diphosphate
additional information
?
-
2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
-
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
-
-
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
-
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
-
-
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
-
-
-
?
2-hydroxy-dATP + 2 H2O
2-hydroxy-dAMP + 2 phosphate
-
-
-
-
?
2-hydroxy-dATP + 2 H2O
2-hydroxy-dAMP + 2 phosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 protein is an antimutagenic (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase that prevents the incorporation of oxidatively modified nucleotides into nucleic acids. It decomposes most specifically the miscoding products of oxidative damage to purine nucleic acid precursors (e.g. 8-oxo-dGTP, 2-hydroxy-dATP, 2-hydroxy-ATP, 8-oxo-GTP) that may cause point mutations or transcription errors when incorporated into DNA and RNA, respectively
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
human MTH1 hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-oxo-dATP, to monophosphates, thereby preventing the misincorporation of these oxidized nucleotides during replication
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
MTH1 protects cells from H2O2-induced cell dysfunction and death by hydrolyzing oxidized purine nucleotides including 8-oxo-dGTP and 2-OH-dATP. These alterations may be partly attributed to a mitochondrial dysfunction
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
hydrolyzed more efficiently and with higher affinity than 8-oxo-dATP. Preferential hydrolysis of 2-oxo-dATP over 8-oxo-dGTP is observed at all of the pH values tested (pH 7.2 to pH 8.8). A 5fold difference in the hydrolysis efficiencies for 2-oxo-dATP over 8-oxo-dGTP is found at pH 7.2. In addition to the normal form of hMTH1 (valine 83), the variant form of the protein (methionine 83) also hydrolyzes 2-oxo-dATP more efficiently than 8-oxo-dGTP
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
is more efficiently hydrolyzed to the monophosphate than is 8-oxo-dGTP
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
is more efficiently hydrolyzed to the monophosphate than is 8-oxo-dGTP
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
-
?
8-oxo-ATP + H2O
8-oxo-AMP + diphosphate
-
-
-
-
?
8-oxo-ATP + H2O
8-oxo-AMP + diphosphate
-
-
poor substrate
-
?
8-oxo-ATP + H2O
8-oxo-AMP + diphosphate
-
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
hydrolyzed as efficiently as 8-oxo-dGTP
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate is produced during cellular metabolism, and its misincorporation into DNA causes mutation. MTH1 hydrolyzes 8-oxo-dGTP to the corresponding nucleoside monophosphate, thereby preventing misincorporation of 8-oxo-7,8-dihydroguanine into DNA. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
human MTH1 hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-oxo-dATP, to monophosphates, thereby preventing the misincorporation of these oxidized nucleotides during replication. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the enzyme is responsible for preventing misincorporation of 8-oxoguanine into DNA. The enzyme protects genetic information from the untoward effects of endogenous oxygen radicals. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
this enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
this enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP. Trp117 is essential for MTH1 to recognize both 8-oxodGTP and 2-hydroxy-dATP, whereas Asp119 is only essential for recognizing 2-hydroxy-dATP, thus suggesting that origins of the substrate-binding pockets for MTH1 and MutT (from Escherichia coli) are different
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
MTH1 catalyzes hydrolysis of 8-oxo-dGTP through nucleophilic substitution of water at the beta-phosphate. The side chains of Asp119 and Asn33 play an essential role in 2-OH-dATP recognition, whereas the indole ring of Trp117 may be important for interacting with the purine bases of substrate nucleotides. Solution structure of MTH1 solved by multidimensional heteronuclear NMR spectroscopy, identification of the substrate interaction pocket. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP) is formed in the nucleotide pool of a cell during normal cellular metabolism, and when it is incorporated into DNA causes mutation. Organisms possess 8-oxo-dGTPase, an enzyme that specifically degrades 8-oxo-dGTP to 8-oxo-dGMP. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 protein is an antimutagenic (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase that prevents the incorporation of oxidatively modified nucleotides into nucleic acids. It decomposes most specifically the miscoding products of oxidative damage to purine nucleic acid precursors (e.g. 8-oxo-dGTP, 2-hydroxy-dATP, 2-hydroxy-ATP, 8-oxo-GTP) that may cause point mutations or transcription errors when incorporated into DNA and RNA, respectively. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. The MTH2 protein prevents mutations caused by 8-oxoguanine nucleotides. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
highest specific activity toward 8-oxo-dGTP
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
poor substrate
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
this enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
the MTH1 protein has the ability to cleave the phosphoanhydride bond between the alpha and the beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
?
dGTP + H2O
dGMP + diphosphate
-
poor substrate
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
?
dGTP + H2O
dGMP + diphosphate
-
-
-
-
?
GTP + H2O
GMP + diphosphate
-
Vmax/Km is 31% of the value for 8-oxo-GTP
-
-
?
GTP + H2O
GMP + diphosphate
-
-
-
-
?
additional information
?
-
-
no hydrolysis of (R)-8,5'-cyclodATP, 5-oxo-dCTP, and 5-formyl-dUTP
-
-
?
additional information
?
-
-
Vmax/Km for GDP is 0.3% of the value for 8-oxo-GTP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-hydroxy-ATP + H2O
2-hydroxy-AMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration
-
-
?
2-hydroxy-dATP + 2 H2O
2-hydroxy-dAMP + 2 phosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 protein is an antimutagenic (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase that prevents the incorporation of oxidatively modified nucleotides into nucleic acids. It decomposes most specifically the miscoding products of oxidative damage to purine nucleic acid precursors (e.g. 8-oxo-dGTP, 2-hydroxy-dATP, 2-hydroxy-ATP, 8-oxo-GTP) that may cause point mutations or transcription errors when incorporated into DNA and RNA, respectively
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
2-oxo-dATP + H2O
2-oxo-dAMP + diphosphate
-
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
this enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
-
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
human MTH1 hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-oxo-dATP, to monophosphates, thereby preventing the misincorporation of these oxidized nucleotides during replication
-
-
?
2-hydroxy-dATP + H2O
2-hydroxy-dAMP + diphosphate
MTH1 protects cells from H2O2-induced cell dysfunction and death by hydrolyzing oxidized purine nucleotides including 8-oxo-dGTP and 2-OH-dATP. These alterations may be partly attributed to a mitochondrial dysfunction
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
-
-
-
-
?
8-oxo-dATP + H2O
8-oxo-dAMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate is produced during cellular metabolism, and its misincorporation into DNA causes mutation. MTH1 hydrolyzes 8-oxo-dGTP to the corresponding nucleoside monophosphate, thereby preventing misincorporation of 8-oxo-7,8-dihydroguanine into DNA. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy-ATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
human MTH1 hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-oxo-dATP, to monophosphates, thereby preventing the misincorporation of these oxidized nucleotides during replication. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the enzyme is responsible for preventing misincorporation of 8-oxoguanine into DNA. The enzyme protects genetic information from the untoward effects of endogenous oxygen radicals. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
this enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate (8-oxo-dGTP) is formed in the nucleotide pool of a cell during normal cellular metabolism, and when it is incorporated into DNA causes mutation. Organisms possess 8-oxo-dGTPase, an enzyme that specifically degrades 8-oxo-dGTP to 8-oxo-dGMP. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. MTH1 protein is an antimutagenic (2'-deoxy) ribonucleoside 5'-triphosphate pyrophosphohydrolase that prevents the incorporation of oxidatively modified nucleotides into nucleic acids. It decomposes most specifically the miscoding products of oxidative damage to purine nucleic acid precursors (e.g. 8-oxo-dGTP, 2-hydroxy-dATP, 2-hydroxy-ATP, 8-oxo-GTP) that may cause point mutations or transcription errors when incorporated into DNA and RNA, respectively. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate. This enzyme is a 2-hydroxy-dATP diphosphatase that also exhibits activity with 8-oxo-dGTP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2Z)-2-methyl-4-[(9H-purin-6-yl)amino]but-2-en-1-ol
-
2'-deoxy-8-hydroxyguanosine 5'-triphosphate
-
-
2-(dimethylamino)-9-methyl-1,9-dihydro-6H-purin-6-one
-
2-amino-9-methyl-1,9-dihydro-6H-purin-6-one
-
2-amino-9-methyl-7,9-dihydro-1H-purine-6,8-dione
-
2-chloro-6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
-
2-hydroxy-dADP
-
competitively inhibits both the 2-hydroxy-dATP hydrolase and 8-hydroxy-dGTP hydrolase activities of hMTH1
2-hydroxy-dATP
the hydrolysis of 8-oxo-dGTP (0.01 mM) by wild type and F27A decreases to 42% and 44% of the control in the presence of 0.01 mM 2-hydroxy-dATP. 8-oxo-dGTPase activities of D119A and D119N mutants are not altered in the presence of 2-hydroxy-dATP up to 0.1 mM
2-[2-[(6-methoxy-3-methyl-1H-pyrazolo[3,4-b]quinolin-4-yl)amino]ethoxy]ethanol
i.e. SCH-51344
3-[(2-amino-6-methylpyrimidin-4-yl)oxy]propan-1-ol
-
6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
-
6-(2,3-dichlorophenyl)-N4-methylpyrimidine-2,4-diamine
6-(methylamino)pyrimidine-2,4(1H,3H)-dione
-
8-oxo-dGDP
-
competitively inhibits both the 2-hydroxy-dATP hydrolase and 8-hydroxy-dGTP hydrolase activities of hMTH1
9-methyl-2-(methylamino)-1,9-dihydro-6H-purin-6-one
-
dATP
the 8-oxo-dGTPase activity of wild type hMTH1 decreases to 79.6% of the control in the presence of 0.1 mM dATP
N-(1-methyl-1H-benzimidazol-5-yl)acetamide
-
N-(2-phenylethyl)-9H-purin-6-amine
-
N-[(2H-1,3-benzodioxol-5-yl)methyl]-9H-purin-6-amine
-
N-[(furan-2-yl)methyl]-9-methyl-9H-purin-6-amine
-
N-[(furan-2-yl)methyl]-9H-purin-6-amine
-
N-[3-[(propan-2-yl)oxy]propyl]-9H-purin-6-amine
NPD15095, competitive inhibition
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
N6-(2-methoxyethyl)-9H-purine-2,6-diamine
-
N6-(2-phenylethyl)-9H-purine-2,6-diamine
-
N6-benzyl-9H-purine-2,6-diamine
-
N6-[2-(3,4-dimethoxyphenyl)ethyl]-9H-purine-2,6-diamine
-
N6-[3-[(propan-2-yl)oxy]propyl]-9H-purine-2,6-diamine
-
6-(2,3-dichlorophenyl)-N4-methylpyrimidine-2,4-diamine
i.e. TH287
6-(2,3-dichlorophenyl)-N4-methylpyrimidine-2,4-diamine
-
i.e. TH287
8-oxo-dGTP
-
-
8-oxo-dGTP
the hydrolysis of 2-hydroxy-dATP (0.01 mM) by wild type hMTH1 is inhibited to 50% of the control in the presence of 0.017 mM 8-oxo-dGTP, whereas the W117Y mutant efficiently hydrolyzes 2-hydroxy-dATP even in the presence of 0.1 mM 8-oxodGTP and its initial velocity is 57% of the control
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
i.e. TH588
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
i.e. TH588
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
-
i.e. TH588
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
i.e. TH588
TH1579
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-hydroxy-datp diphosphatase deficiency
hMTH1 and GPX1 expression in human thyroid tissue is interrelated to prevent oxidative DNA damage.
Adenoma
HMTH1 induces the metastasis and recurrence of the parotid adenoma by repairing DNA damage.
Alzheimer Disease
Expression of hMTH1 in the hippocampi of control and Alzheimer's disease.
Brain Neoplasms
Accumulation of 8-oxo-2'-deoxyguanosine and increased expression of hMTH1 protein in brain tumors.
Brain Neoplasms
Expression of human MutT homologue (hMTH1) protein in primary non-small-cell lung carcinomas and histologically normal surrounding tissue.
Breast Neoplasms
Biological characterisation and application of human MTH1 and monoclonal antibody preparation.
Breast Neoplasms
Expression of human MutT homologue (hMTH1) protein in primary non-small-cell lung carcinomas and histologically normal surrounding tissue.
Carcinogenesis
Mutation analysis of the hMTH1 gene in sporadic human ovarian cancer.
Carcinoma
Expression of human MutT homologue (hMTH1) protein in primary non-small-cell lung carcinomas and histologically normal surrounding tissue.
Carcinoma
Overexpression of human mutT homologue gene messenger RNA in renal-cell carcinoma: evidence of persistent oxidative stress in cancer.
Carcinoma, Hepatocellular
Expression of DNA repair enzyme hMTH1 mRNA and protein in hepatocellular carcinoma.
Carcinoma, Hepatocellular
[Potential role of human DNA-repair enzymes hMTH1, hOGG1 and hMYHalpha in the hepatocarcinogenesis]
Carcinoma, Non-Small-Cell Lung
Expression of human MutT homologue (hMTH1) protein in primary non-small-cell lung carcinomas and histologically normal surrounding tissue.
Carcinoma, Non-Small-Cell Lung
Great potential of a panel of multiple hMTH1, SPD, ITGA11 and COL11A1 markers for diagnosis of patients with non-small cell lung cancer.
Carcinoma, Renal Cell
Expression of human MutT homologue (hMTH1) protein in primary non-small-cell lung carcinomas and histologically normal surrounding tissue.
Colorectal Neoplasms
Polymorphisms and probable lack of mutation in a human mutT homolog, hMTH1, in hereditary nonpoliposis colorectal cancer.
Colorectal Neoplasms
The oxidized deoxynucleoside triphosphate pool is a significant contributor to genetic instability in mismatch repair-deficient cells.
Colorectal Neoplasms, Hereditary Nonpolyposis
Polymorphisms and probable lack of mutation in a human mutT homolog, hMTH1, in hereditary nonpoliposis colorectal cancer.
Diabetes Mellitus, Type 2
Combined analysis of polymorphism variants in hMTH1, hOGG1 and MUTYH genes on the risk of type 2 diabetes in the Chinese population.
Dystonia
A role for oxidized DNA precursors in Huntington's disease-like striatal neurodegeneration.
Glioma
Accumulation of 8-oxo-2'-deoxyguanosine and increased expression of hMTH1 protein in brain tumors.
Huntington Disease
A role for oxidized DNA precursors in Huntington's disease-like striatal neurodegeneration.
Huntington Disease
Oxidized purine nucleotides, genome instability and neurodegeneration.
Idiopathic Pulmonary Fibrosis
Oxidative stress in lung epithelial cells from patients with idiopathic interstitial pneumonias.
Leukemia
Inhibition of 8-oxo-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase (8-oxo-dGTPase) activity of the antimutagenic human MTH1 protein by nucleoside 5'-diphosphates.
Lung Diseases, Interstitial
Oxidative stress in lung epithelial cells from patients with idiopathic interstitial pneumonias.
Lung Neoplasms
Contribution of hMTH1 to the maintenance of 8-oxoguanine levels in lung DNA of non-small-cell lung cancer patients.
Lung Neoplasms
Expression of human MutT homologue (hMTH1) protein in primary non-small-cell lung carcinomas and histologically normal surrounding tissue.
Lung Neoplasms
Great potential of a panel of multiple hMTH1, SPD, ITGA11 and COL11A1 markers for diagnosis of patients with non-small cell lung cancer.
Lung Neoplasms
Overexpression of hMTH1 mRNA: a molecular marker of oxidative stress in lung cancer cells.
Lymphatic Metastasis
Great potential of a panel of multiple hMTH1, SPD, ITGA11 and COL11A1 markers for diagnosis of patients with non-small cell lung cancer.
Meningioma
Accumulation of 8-oxo-2'-deoxyguanosine and increased expression of hMTH1 protein in brain tumors.
Neoplasm Metastasis
Great potential of a panel of multiple hMTH1, SPD, ITGA11 and COL11A1 markers for diagnosis of patients with non-small cell lung cancer.
Neoplasm Metastasis
HMTH1 induces the metastasis and recurrence of the parotid adenoma by repairing DNA damage.
Neoplasm Metastasis
hMTH1 is required for maintaining migration and invasion potential of human thyroid cancer cells.
Neoplasms
A variant form of hMTH1, a human homologue of the E coli mutT gene, correlates with somatic mutation in the p53 tumour suppressor gene in gastric cancer patients.
Neoplasms
Accumulation of 8-oxo-2'-deoxyguanosine and increased expression of hMTH1 protein in brain tumors.
Neoplasms
Bacterial DNA repair genes and their eukaryotic homologues: 2. Role of bacterial mutator gene homologues in human disease. Overview of nucleotide pool sanitization and mismatch repair systems.
Neoplasms
Contribution of hMTH1 to the maintenance of 8-oxoguanine levels in lung DNA of non-small-cell lung cancer patients.
Neoplasms
Development of Damaged Nucleoside Mimics for Inhibition of Their Repair Enzymes.
Neoplasms
Expression of DNA repair enzyme hMTH1 mRNA and protein in hepatocellular carcinoma.
Neoplasms
Frequent microsatellite instabilities and analyses of the related genes in familial gastric cancers.
Neoplasms
Hexabromocyclododecane-induced Genotoxicity in Cultured Human Breast Cells through DNA Damage.
Neoplasms
hMTH1 and GPX1 expression in human thyroid tissue is interrelated to prevent oxidative DNA damage.
Neoplasms
hMTH1 is required for maintaining migration and invasion potential of human thyroid cancer cells.
Neoplasms
hMYH and hMTH1 cooperate for survival in mismatch repair defective T-cell acute lymphoblastic leukemia.
Neoplasms
Inhibitory Effect of 8-Halogenated 7-Deaza-2'-deoxyguanosine Triphosphates on Human 8-Oxo-2'-deoxyguanosine Triphosphatase, hMTH1, Activities.
Neoplasms
Overexpression of human mutT homologue gene messenger RNA in renal-cell carcinoma: evidence of persistent oxidative stress in cancer.
Neoplasms
Polymorphisms and probable lack of mutation in a human mutT homolog, hMTH1, in hereditary nonpoliposis colorectal cancer.
Neoplasms
Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.
Neoplasms, Neuroepithelial
Accumulation of 8-oxo-2'-deoxyguanosine and increased expression of hMTH1 protein in brain tumors.
Neurilemmoma
Accumulation of 8-oxo-2'-deoxyguanosine and increased expression of hMTH1 protein in brain tumors.
Ovarian Neoplasms
Mutation analysis of the hMTH1 gene in sporadic human ovarian cancer.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
hMYH and hMTH1 cooperate for survival in mismatch repair defective T-cell acute lymphoblastic leukemia.
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
hMYH and hMTH1 cooperate for survival in mismatch repair defective T-cell acute lymphoblastic leukemia.
Stomach Neoplasms
A variant form of hMTH1, a human homologue of the E coli mutT gene, correlates with somatic mutation in the p53 tumour suppressor gene in gastric cancer patients.
Thyroid Neoplasms
hMTH1 and GPX1 expression in human thyroid tissue is interrelated to prevent oxidative DNA damage.
Thyroid Neoplasms
hMTH1 is required for maintaining migration and invasion potential of human thyroid cancer cells.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0043
2-hydroxy-ATP
-
pH 8.0, 30°C
0.0043 - 5.7
2-hydroxy-dATP
0.0134
2-hydroxy-rATP
at pH 7.4, temperature not specified in the publication
0.0052 - 0.0318
2-oxo-dATP
0.051
8-oxo-ATP
-
pH 8.0, 30°C
0.027
8-oxo-dGDP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
0.044
8-oxo-GDP
-
pH 8.0, 30°C
0.24
8-oxo-rATP
at pH 7.4, temperature not specified in the publication
0.082
8-oxo-rGTP
at pH 7.4, temperature not specified in the publication
1.173
ADP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.385
Ap4A
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.455
ATP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.447
dADP
-
in the presence of 5 mM Mg2+, at pH 8.0 and 37°C
0.298
dATP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.134
dGDP
-
in the presence of 5 mM Mg2+, at pH 8.0 and 37°C
0.319
GDP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.0043
2-hydroxy-dATP
-
pH and temperature not specified in the publication
0.0083
2-hydroxy-dATP
-
pH 8.0, 30°C
0.0087
2-hydroxy-dATP
pH 8.0, 30°C, wild-type enzyme
0.014
2-hydroxy-dATP
at pH 7.4, temperature not specified in the publication
0.017
2-hydroxy-dATP
pH 8.0, 30°C, mutant enzyme F27A
0.025
2-hydroxy-dATP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
5.7
2-hydroxy-dATP
-
pH 7.2, 30°C
0.0052
2-oxo-dATP
-
wild type enzyme, at pH 7.5 and 22°C
0.006
2-oxo-dATP
-
mutant enzyme D120N, at pH 7.5 and 22°C
0.0318
2-oxo-dATP
-
mutant enzyme D120A, at pH 7.5 and 22°C
0.0076
8-oxo-dATP
at pH 7.4, temperature not specified in the publication
0.0139
8-oxo-dATP
-
pH 8.0, 30°C
0.03
8-oxo-dATP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
0.0084
8-oxo-dGTP
-
wild type enzyme, at pH 7.5 and 22°C
0.0113
8-oxo-dGTP
at pH 7.4, temperature not specified in the publication
0.0151
8-oxo-dGTP
pH 8.0, 30°C, wild-type enzyme
0.0152
8-oxo-dGTP
-
pH 8.0, 30°C
0.027
8-oxo-dGTP
-
in the presence of 0.25 mM Mn2+, at pH 8.0 and 37°C
0.0302
8-oxo-dGTP
pH 8.0, 30°C, mutant enzyme D119A
0.032
8-oxo-dGTP
pH and temperature not specified in the publication
0.0403
8-oxo-dGTP
pH 8.0, 30°C, mutant enzyme F27A
0.0412
8-oxo-dGTP
-
mutant enzyme D120N, at pH 7.5 and 22°C
0.0444
8-oxo-dGTP
-
mutant enzyme D120A, at pH 7.5 and 22°C
12.8
8-oxo-dGTP
-
pH 7.2, 30°C
0.055
8-oxo-GTP
-
pH 8.0, 30°C
0.29
8-oxo-GTP
-
pH 8.0, 30°C
0.046
dGTP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
0.258
dGTP
-
pH 8.0, 30°C
0.42
dGTP
at pH 7.4, temperature not specified in the publication
0.598
GTP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.7
2-hydroxy-ATP
-
pH 8.0, 30°C
0.097 - 31
2-hydroxy-dATP
1.1
8-oxo-ATP
-
pH 8.0, 30°C
0.273
8-oxo-dGDP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
2.6
8-oxo-GTP
-
pH 8.0, 30°C
0.102
ADP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.103
Ap4A
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.158
ATP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.143
dADP
-
in the presence of 5 mM Mg2+, at pH 8.0 and 37°C
0.15
dATP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.128
dGDP
-
in the presence of 5 mM Mg2+, at pH 8.0 and 37°C
0.187
GDP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.338
GTP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.097
2-hydroxy-dATP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
4.7
2-hydroxy-dATP
-
pH 7.2, 30°C
13.9
2-hydroxy-dATP
-
pH 8.0, 30°C
28.7
2-hydroxy-dATP
pH 8.0, 30°C, wild-type enzyme
31
2-hydroxy-dATP
pH 8.0, 30°C, mutant enzyme F27A
21.1
2-oxo-dATP
-
wild type enzyme, at pH 7.5 and 22°C
21.1
2-oxo-dATP
-
mutant enzyme D120N, at pH 7.5 and 22°C
34.4
2-oxo-dATP
-
mutant enzyme D120A, at pH 7.5 and 22°C
0.103
8-oxo-dATP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
10.8
8-oxo-dATP
-
pH 8.0, 30°C
1.13
8-oxo-dGTP
-
in the presence of 0.25 mM Mn2+, at pH 8.0 and 37°C
2.1
8-oxo-dGTP
-
pH 7.2, 30°C
4.6
8-oxo-dGTP
-
mutant enzyme D120N, at pH 7.5 and 22°C
9.54
8-oxo-dGTP
pH 8.0, 30°C, mutant enzyme D119A
9.7
8-oxo-dGTP
-
mutant enzyme D120A, at pH 7.5 and 22°C
12.3
8-oxo-dGTP
-
pH 8.0, 30°C
20.7
8-oxo-dGTP
-
wild type enzyme, at pH 7.5 and 22°C
25.1
8-oxo-dGTP
pH 8.0, 30°C, mutant enzyme F27A
25.9
8-oxo-dGTP
pH 8.0, 30°C, wild-type enzyme
0.308
dGTP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1093
2-hydroxy-ATP
-
pH 8.0, 30°C
0.00168 - 3300
2-hydroxy-dATP
22
8-oxo-ATP
-
pH 8.0, 30°C
10.2
8-oxo-dGDP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
47
8-oxo-GTP
-
pH 8.0, 30°C
0.09
ADP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.27
Ap4A
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
3.5
ATP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
3.2
dADP
-
in the presence of 5 mM Mg2+, at pH 8.0 and 37°C
5
dATP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.95
dGDP
-
in the presence of 5 mM Mg2+, at pH 8.0 and 37°C
5.8
GDP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.6
GTP
-
in the presence of 5 mM Mn2+, at pH 8.0 and 37°C
0.00168
2-hydroxy-dATP
-
pH and temperature not specified in the publication
3.8
2-hydroxy-dATP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
83
2-hydroxy-dATP
-
pH 7.2, 30°C
168
2-hydroxy-dATP
-
pH 8.0, 30°C
1680
2-hydroxy-dATP
-
pH 8.0, 30°C
1820
2-hydroxy-dATP
pH 8.0, 30°C, mutant enzyme F27A
3300
2-hydroxy-dATP
pH 8.0, 30°C, wild-type enzyme
1.1
2-oxo-dATP
-
mutant enzyme D120A, at pH 7.5 and 22°C
3.5
2-oxo-dATP
-
mutant enzyme D120N, at pH 7.5 and 22°C
4.1
2-oxo-dATP
-
wild type enzyme, at pH 7.5 and 22°C
3.5
8-oxo-dATP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
78
8-oxo-dATP
-
pH 8.0, 30°C
780
8-oxo-dATP
-
pH 8.0, 30°C
0.1
8-oxo-dGTP
-
mutant enzyme D120N, at pH 7.5 and 22°C
0.2
8-oxo-dGTP
-
mutant enzyme D120A, at pH 7.5 and 22°C
2.5
8-oxo-dGTP
-
wild type enzyme, at pH 7.5 and 22°C
16
8-oxo-dGTP
-
pH 7.2, 30°C
41.7
8-oxo-dGTP
-
in the presence of 0.25 mM Mn2+, at pH 8.0 and 37°C
81
8-oxo-dGTP
-
pH 8.0, 30°C
310
8-oxo-dGTP
pH 8.0, 30°C, mutant enzyme D119A
620
8-oxo-dGTP
pH 8.0, 30°C, mutant enzyme F27A
810
8-oxo-dGTP
-
pH 8.0, 30°C
1710
8-oxo-dGTP
pH 8.0, 30°C, wild-type enzyme
6
dGTP
-
pH 8.0, 30°C
6.7
dGTP
-
in the presence of 1 mM Mn2+, at pH 8.0 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.014 - 0.022
(2Z)-2-methyl-4-[(9H-purin-6-yl)amino]but-2-en-1-ol
0.1
2-(dimethylamino)-9-methyl-1,9-dihydro-6H-purin-6-one
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
2-amino-9-methyl-1,9-dihydro-6H-purin-6-one
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
2-amino-9-methyl-7,9-dihydro-1H-purine-6,8-dione
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.00023 - 0.00035
2-chloro-6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
0.0045
3-[(2-amino-6-methylpyrimidin-4-yl)oxy]propan-1-ol
Homo sapiens
pH and temperature not specified in the publication
0.00021 - 0.00038
6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
0.0015
6-(methylamino)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.059
9-methyl-2-(methylamino)-1,9-dihydro-6H-purin-6-one
Homo sapiens
pH and temperature not specified in the publication
0.08
N-(1-methyl-1H-benzimidazol-5-yl)acetamide
Homo sapiens
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.0028 - 0.0039
N-(2-phenylethyl)-9H-purin-6-amine
0.02 - 0.028
N-[(2H-1,3-benzodioxol-5-yl)methyl]-9H-purin-6-amine
1
N-[(furan-2-yl)methyl]-9-methyl-9H-purin-6-amine
Homo sapiens
IC50 above 1.0 mM, with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.02 - 0.029
N-[(furan-2-yl)methyl]-9H-purin-6-amine
0.00333 - 0.0067
N-[3-[(propan-2-yl)oxy]propyl]-9H-purin-6-amine
0.000004 - 0.000138
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
0.0048 - 0.0091
N6-(2-methoxyethyl)-9H-purine-2,6-diamine
0.00029 - 0.0005
N6-(2-phenylethyl)-9H-purine-2,6-diamine
0.00063 - 0.00113
N6-benzyl-9H-purine-2,6-diamine
0.00042 - 0.021
N6-[2-(3,4-dimethoxyphenyl)ethyl]-9H-purine-2,6-diamine
0.0019 - 0.0028
N6-[3-[(propan-2-yl)oxy]propyl]-9H-purine-2,6-diamine
0.0000022 - 0.000132
TH1579
-
0.014
(2Z)-2-methyl-4-[(9H-purin-6-yl)amino]but-2-en-1-ol
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.022
(2Z)-2-methyl-4-[(9H-purin-6-yl)amino]but-2-en-1-ol
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.00023
2-chloro-6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.00035
2-chloro-6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.00021
6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.00038
6-(1,3,3-trimethyl-6-azabicyclo[3.2.1]octan-6-yl)-9H-purine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.0028
N-(2-phenylethyl)-9H-purin-6-amine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.0039
N-(2-phenylethyl)-9H-purin-6-amine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.02
N-[(2H-1,3-benzodioxol-5-yl)methyl]-9H-purin-6-amine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.028
N-[(2H-1,3-benzodioxol-5-yl)methyl]-9H-purin-6-amine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.02
N-[(furan-2-yl)methyl]-9H-purin-6-amine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.029
N-[(furan-2-yl)methyl]-9H-purin-6-amine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.00333
N-[3-[(propan-2-yl)oxy]propyl]-9H-purin-6-amine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.0067
N-[3-[(propan-2-yl)oxy]propyl]-9H-purin-6-amine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.000004
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
Canis lupus familiaris
wild type enzyme, at pH 8.0 and 22°C
0.0000068
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
Homo sapiens
wild type enzyme, at pH 8.0 and 22°C
0.0000225
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
Homo sapiens
mutant enzyme M116L, at pH 8.0 and 22°C
0.000032
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
Mus musculus
mutant enzyme L116M, at pH 8.0 and 22°C
0.000138
N4-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine
Mus musculus
wild type enzyme, at pH 8.0 and 22°C
0.0048
N6-(2-methoxyethyl)-9H-purine-2,6-diamine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.0091
N6-(2-methoxyethyl)-9H-purine-2,6-diamine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.00029
N6-(2-phenylethyl)-9H-purine-2,6-diamine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.0005
N6-(2-phenylethyl)-9H-purine-2,6-diamine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.00063
N6-benzyl-9H-purine-2,6-diamine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.00113
N6-benzyl-9H-purine-2,6-diamine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.00042
N6-[2-(3,4-dimethoxyphenyl)ethyl]-9H-purine-2,6-diamine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.021
N6-[2-(3,4-dimethoxyphenyl)ethyl]-9H-purine-2,6-diamine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.0019
N6-[3-[(propan-2-yl)oxy]propyl]-9H-purine-2,6-diamine
Homo sapiens
with 8-oxo-dGTP as substrate, at pH 7.5, temperature not specified in the publication
0.0028
N6-[3-[(propan-2-yl)oxy]propyl]-9H-purine-2,6-diamine
Homo sapiens
with 2-hydroxy-dATP as substrate, at pH 7.5, temperature not specified in the publication
0.0000022
TH1579
Homo sapiens
wild type enzyme, at pH 8.0 and 22°C
-
0.0000039
TH1579
Canis lupus familiaris
wild type enzyme, at pH 8.0 and 22°C
-
0.000132
TH1579
Mus musculus
wild type enzyme, at pH 8.0 and 22°C
-
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malfunction
-
MTH1-null mouse embryo fibroblasts are highly susceptible to cell dysfunction and death caused by exposure to H2O2, with condensed nuclei and degenerated mitochondria in which electron dense deposits are seen in place of intact cristae. The cell death observed is not dependent on either poly(ADP-ribose) polymerase or caspases. A continuous accumulation of 8-oxoG, both in the nuclear and mitochondrial DNA, is observed after exposure to H2O2. All of the H2O2-induced alterations observed in MTH1-null MEFs are effectively suppressed by the expression of wild-type human MTH1
malfunction
the knockdown of the MTH1, MTH2, and NUDT5 proteins increases the A:T to C:G substitution mutations induced by 8-hydroxy-dGTP. In addition, the increase in the induced mutation frequency is more evident in the triple-knockdown cells
physiological function
all three of the human MTH1, MTH2, and NUDT5 proteins act as a defense against the mutagenesis induced by oxidized dGTP
physiological function
-
is produced in cells by reactive oxygen species normally formed during cellular metabolic processes. This oxidized base can pair with both adenine and cytosine, and thus the existence of this base in messenger RNA would cause translational errors. The elimination of 8-oxoguanine-containing ribonucleotides from the precursor pool is important to ensure accurate protein synthesis. Both NUDT5 and MTH1 are involved in this process in human cells
physiological function
-
MTH1 efficiently suppresses the accumulation of 8-oxoguanine in both cellular DNA and RNA in the hippocampus, especially in microglia, caused by excitotoxicity (caused by the systemic administration of kainate)
physiological function
MTH1 hydrolyzes oxidized purine nucleoside triphosphates such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxydATP, and 2-hydroxy-rATP to monophosphates, and thus avoids errors caused by their misincorporation during DNA replication or transcription, which may result in carcinogenesis or neurodegeneration
physiological function
MTH1 protects the dopamine neurons from oxidative damage in the nucleic acids, especially in the mitochondrial DNA of striatal nerve terminals of dopamine neurons
physiological function
-
MTH1, a major sanitizing enzyme for oxidized nucleotide pools plays a crucial role by suppressing their accumulation in cellular DNA. In addition to oxidized purine deoxyribonucleoside triphosphates, MTH1 efficiently hydrolyzes oxidized purine ribonucleoside triphosphates such as 2-hydroxy-ATP, 8-oxo-ATP and, to a lesser extent, 8-oxo-GTP
physiological function
-
MTH1, a major sanitizing enzyme for oxidized nucleotide pools plays a crucial role by suppressing their accumulation in cellular DNA. In addition to oxidized purine deoxyribonucleoside triphosphates, MTH1 efficiently hydrolyzes oxidized purine ribonucleoside triphosphates such as 2-hydroxy-ATP, 8-oxo-ATP and, to a lesser extent, 8-oxo-GTP
physiological function
the enzyme prevents the incorporation of oxidized nucleotides such as 2-hydroxy-ATP and 8-oxo-dGTP during DNA replication by hydrolysing them into their corresponding monophosphates
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D120A
-
the mutant shows 8% of wild type activity
D120N
-
the mutant shows 4% of wild type activity
L150A
mutant enzyme with decrased thermostability. Tm-value is 50°C compared to 65°C for the wild-type enzyme
M116L
the mutation causes a considerable drop in activity with dGTP compared to the wild type enzyme
N33A
mutation decreases catalytic activity toward 2-hydroxy-dATP to 5% of the wild-type activity. The mutant shows 14% of the wild-type 8-oxo-dGTP activity
N33E
mutation decreases catalytic activity toward 2-hydroxy-dATP to 53% of the wild-type activity. Activity towards 8-oxo-dGTP is totally abolished
V156A
mutant enzyme with decrased thermostability. Tm-value is 61°C compared to 65°C for the wild-type enzyme
V83M
-
Met83-MTH1 is more thermolabile than that of Val83-MTH1. Substitution of valine for methionine at the residue 83 of MTH1 protein appears to lead to alteration in the secondary structure which renders the protein more labile than the normal type protein
L116M
the mutation causes a considerable drop in activity with dGTP compared to the wild type enzyme
A84G
-
the mutant shows about 70% of wild type activity
A84G/G90E
-
the mutant shows about 110% of wild type activity
G90E
-
the mutant shows about 130% of wild type activity
additional information
sequence comparison with the Escherichia coli homolog, MutT, which hydrolyzes only 8-oxo-dGTP and 8-oxo-GTP but not oxidized forms of dATP or ATP. Neither a replacement of the phosphohydrolase module of MTH1 with that of MutT nor deletions of the C-terminal region of MTH1, which is unique for MTH1, alter the substrate specificity of MTH1. In contrast, the substitution of residues at position Trp117 and Asp119 of MTH1, which show apparent chemical shift perturbations with 8-oxo-dGDP in NMR analyses but are not conserved in MutT, affected the substrate specificity. Trp117 is essential for MTH1 to recognize both 8-oxo-dGTP and 2-hydroxy-dATP, whereas Asp119 is only essential for recognizing 2-hydroxy-dATP, thus suggesting that origins of the substrate-binding pockets for MTH1 and MutT are different
D119A
mutant enzyme shows no hydrolytic activity with 2-hydroxy-dATP. Specific activity with 8-oco-dGTP is 139% of wild-type activity
D119A
mutation completely abolishes the 2-hydroxy-dATP-hydrolyzing ability, whereas the mutant retains substantial levels of 8-oxo-dGTPase activity
D119A
the mutant enzyme has about half of the wild-type activity for 8-oxo-dGTP but shows almost no activity for 2-hydroxy-dATP
D119N
mutation completely abolishes the 2-hydroxy-dATP-hydrolyzing ability, whereas the mutant retains substantial levels of 8-oxo-dGTPase activity
D119N
the mutant enzyme has about half of the wild-type activity for 8-oxo-dGTP but shows almost no activity for 2-hydroxy-dATP
W117A
the fluorescence of the modified protein is weaker than that of wild-type MTH1. The modified protein exhibits no hydrolysis of either 8-oxo-dGTP or 2-hydroxy-dATP
W117A
the specific activities for 2-hydroxy-dATPase and 8-oxo-dGTPase is decreased significantly compared to wild-type activity. About 10% levels of 2-hydroxy-dATPase and 8-oxo-dGTPase activities compared with wild type hMTH1 are detected in the crude extracts, whereas no activity is detected in the purified preparation
W117Y
mutant enzyme shows hydrolytic acitivity with 8-oxo-dGTP. Specific activity with 2-hydroxy-dATP is 86% of wild-type activity
W117Y
the specific activities for 8-oxo-dGTPase is decreased significantly compared to wild-type activity, 2-hydroxy-dATPase activity exceeds wild type level
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Yamaguchi, H.; Kajitani, K.; Dan, Y.; Furuichi, M.; Ohno, M.; Sakumi, K.; Kang, D.; Nakabeppu, Y.
MTH1, an oxidized purine nucleoside triphosphatase, protects the dopamine neurons from oxidative damage in nucleic acids caused by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
Cell Death Differ.
13
551-563
2006
Homo sapiens (P36639), Mus musculus (P53368)
brenda
Kajitani, K.; Yamaguchi, H.; Dan, Y.; Furuichi, M.; Kang, D.; Nakabeppu, Y.
MTH1, an oxidized purine nucleoside triphosphatase, suppresses the accumulation of oxidative damage of nucleic acids in the hippocampal microglia during kainate-induced excitotoxicity
J. Neurosci.
26
1688-1698
2006
Mus musculus
brenda
Cai, J.P.; Ishibashi, T.; Takagi, Y.; Hayakawa, H.; Sekiguchi, M.
Mouse MTH2 protein which prevents mutations caused by 8-oxoguanine nucleotides
Biochem. Biophys. Res. Commun.
305
1073-1077
2003
Mus musculus (Q8BG93)
brenda
Bialkowski, K.; Kasprzak, K.S.
Cellular 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase activity of human and mouse MTH1 proteins does not depend on the proliferation rate
Free Radic. Biol. Med.
37
1534-1541
2004
Homo sapiens, Mus musculus
brenda
Hori, M.; Satou, K.; Harashima, H.; Kamiya, H.
Suppression of mutagenesis by 8-hydroxy-2'-deoxyguanosine 5'-triphosphate (7,8-dihydro-8-oxo-2'-deoxyguanosine 5'-triphosphate) by human MTH1, MTH2, and NUDT5
Free Radic. Biol. Med.
48
1197-1201
2010
Homo sapiens (P36639)
brenda
Sakumi, K.; Furuichi, M.; Tsuzuki, T.; Kakuma, T.; Kawabata, S.; Maki, H.; Sekiguchi, M.
Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
J. Biol. Chem.
268
23524-23530
1993
Homo sapiens (P36639)
brenda
Kakuma, T.; Nishida, J.; Tsuzuki, T.;, Sekiguchi, M.
Mouse MTH1 protein with 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphatase activity that prevents transversion mutation. cDNA cloning and tissue distribution
J. Biol. Chem.
270
25942-25948
1995
Mus musculus (P53368)
brenda
Fujikawa, K.; Kamiya, H.; Yakushiji, H.; Fujii, Y.; Nakabeppu, Y.; Kasai, H.
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
J. Biol. Chem.
274
18201-18205
1999
Homo sapiens
brenda
Sakai, Y.; Furuichi, M.; Takahashi, M.; Mishima, M.; Iwai, S.; Shirakawa, M.; Nakabeppu, Y.
A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1
J. Biol. Chem.
277
8579-8587
2002
Homo sapiens (P36639)
brenda
Mishima, M.; Sakai, Y.; Itoh, N.; Kamiya, H.; Furuichi, M.; Takahashi, M.; Yamagata, Y.; Iwai, S.; Nakabeppu, Y.; Shirakawa, M.
Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates
J. Biol. Chem.
279
33806-33815
2004
Homo sapiens (P36639)
brenda
Takahashi, M.; Maraboeuf, F.; Sakai, Y.; Yakushiji, H.; Mishima, M.; Shirakawa, M.; Iwai, S.; Hayakawa, H.; Sekiguchi, M.; Nakabeppu, Y.
Role of tryptophan residues in the recognition of mutagenic oxidized nucleotides by human antimutator MTH1 protein
J. Mol. Biol.
319
129-139
2002
Homo sapiens (P36639)
brenda
Yakushiji, H.; Maraboeuf, F.; Takahashi, M.; Deng, Z.S.; Kawabata, S.; Nakabeppu, Y.; Sekiguchi, M.
Biochemical and physicochemical characterization of normal and variant forms of human MTH1 protein with antimutagenic activity
Mutat. Res.
384
181-194
1997
Homo sapiens
brenda
Nakabeppu, Y.; Oka, S.; Sheng, Z.; Tsuchimoto, D.; Sakumi, K.
Programmed cell death triggered by nucleotide pool damage and its prevention by MutT homolog-1 (MTH1) with oxidized purine nucleoside triphosphatase
Mutat. Res.
703
51-58
2010
Homo sapiens, Mus musculus
brenda
Song, X.N.; Zhang, L.Q.; Liu, D.G.; Lin, J.; Zheng, J.D.; Dai, D.P.; Hei, A.L.; Hayakawa, H.; Sekiguchi, M.; Cai, J.P.
Oxidative damage to RNA and expression patterns of MTH1 in the hippocampi of senescence-accelerated SAMP8 mice and Alzheimer's disease patients
Neurochem. Res.
36
1558-1565
2011
Homo sapiens, Mus musculus, Mus musculus SAMP8
brenda
Fujikawa, K.; Kamiya, H.; Yakushiji, H.; Nakabeppu, Y.; Kasai, H.
Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP
Nucleic Acids Res.
29
449-454
2011
Homo sapiens
brenda
Ishibashi, T.; Hayakawa, H.; Ito, R.; Miyazawa, M.; Yamagata, Y.; Sekiguchi, M.
Mammalian enzymes for preventing transcriptional errors caused by oxidative damage
Nucleic Acids Res.
33
3779-3784
2005
Homo sapiens
brenda
Bialkowski, K.; Szpila, A.; Kasprzak, K.S.
Up-regulation of 8-oxo-dGTPase activity of MTH1 protein in the brain, testes and kidneys of mice exposed to (137)Cs gamma radiation
Radiat. Res.
172
187-197
2009
Mus musculus
brenda
Narwal, M.; Jemth, A.S.; Gustafsson, R.; Almloef, I.; Warpman Berglund, U.; Helleday, T.; Stenmark, P.
Crystal structures and inhibitor interactions of mouse and dog MTH1 reveal species-specific differences in affinity
Biochemistry
57
593-603
2018
Canis lupus familiaris (F1P963), Homo sapiens (P36639), Mus musculus (P53368)
brenda
Kumar, A.; Kawamura, T.; Kawatani, M.; Osada, H.; Zhang, K.
Identification and structure-activity relationship of purine derivatives as novel MTH1 inhibitors
Chem. Biol. Drug Des.
89
862-869
2017
Homo sapiens (P36639)
brenda
Waz, S.; Nakamura, T.; Hirata, K.; Koga-Ogawa, Y.; Chirifu, M.; Arimori, T.; Tamada, T.; Ikemizu, S.; Nakabeppu, Y.; Yamagata, Y.
Structural and kinetic studies of the human Nudix hydrolase MTH1 reveal the mechanism for its broad substrate specificity
J. Biol. Chem.
292
2785-2794
2017
Homo sapiens
brenda
Kimura, Y.; Kajimoto, S.; Yamamoto, Y.; Tanaka, N.
Enzymatic characteristics of Nudix hydrolase 2 (Nud2), an 8-oxo-dGTP hydrolase from Myxococcus xanthus
J. Gen. Appl. Microbiol.
66
46-50
2020
Myxococcus xanthus
brenda
Nissink, J.W.; Bista, M.; Breed, J.; Carter, N.; Embrey, K.; Read, J.; Winter-Holt, J.J.
MTH1 substrate recognition - an example of specific promiscuity
PLoS ONE
11
e0151154
2016
Homo sapiens (P36639)
brenda