3.6.1.55: 8-oxo-dGTP diphosphatase
This is an abbreviated version!
For detailed information about 8-oxo-dGTP diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.55
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3.6.1.55
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glycosylase
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sanitize
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8-oxoguanine
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nudix
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misincorporation
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8-oxo-dgmp
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8-oxo-7,8-dihydro-2'-deoxyguanosine
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8-oxo-7,8-dihydrodeoxyguanosine
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mutyh
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promutagenic
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8-oxo-7,8-dihydroguanine
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8-oxodgtpase
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antimutator
- 3.6.1.55
- glycosylase
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sanitize
- 8-oxoguanine
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nudix
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misincorporation
- 8-oxo-dgmp
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8-oxo-7,8-dihydro-2'-deoxyguanosine
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8-oxo-7,8-dihydrodeoxyguanosine
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mutyh
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promutagenic
- 8-oxo-7,8-dihydroguanine
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8-oxodgtpase
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antimutator
Reaction
Synonyms
7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase, 8-oxo-2'-deoxyguanosine triphosphatase, 8-oxo-dG triphosphatase, 8-oxo-dGTP diphosphatase, 8-oxo-dGTP hydrolase, 8-oxo-dGTPase, AK369000, CiMutT, MTH1, MuT, MutT, MutT homolog 1, MutT homologue 1, MutT2, Nudix hydrolase, NUDT1, Nudx12
ECTree
3.6.1.55 8-oxo-dGTP diphosphataseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.6.1.55 - 8-oxo-dGTP diphosphatase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7,8-dihydro-8-oxo-GTP + H2O
7,8-dihydro-8-oxo-GMP + diphosphate
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-
-
?
5-methyl-dCTP + H2O
5-methyl-dCMP + diphosphate
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-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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the specific activity for 8-oxo-dGTP is greater than that for unoxidized dATP and dGTP
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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8-oxo-dGTP i.e. 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
MutT exhibits high substrate specificity for 8-oxoguanine nucleotides by the ligand-induced conformational change
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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specfic for the MutT protein hydrolyses other dNTPs and GTP with lower Vmax and extremely high Km-values
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
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-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
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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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
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the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state
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-
?
additional information
?
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no activity with ATP, 2-hydroxy-ATP, and 2-hydroxy-dATP
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-
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additional information
?
-
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no activity with ATP, 2-hydroxy-ATP, and 2-hydroxy-dATP
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-
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additional information
?
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in addition the enzyme hydrolyzes all four of the unoxidized nucleoside triphosphates, with a preference for dATP
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-
?
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
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-
?
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
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-
?
additional information
?
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enzyme additionally shows Ap4A and guanosine-3',5'-tetraphosphate diphosphohydrolase activities
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-
?
