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Information on EC 3.6.1.55 - 8-oxo-dGTP diphosphatase and Organism(s) Escherichia coli and UniProt Accession P08337
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3.6.1.55 8-oxo-dGTP diphosphataseIUBMB Comments
This enzyme hydrolyses the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA. It does not hydrolyse 2-hydroxy-dATP (cf. EC 3.6.1.56, 2-hydroxy-dATP diphosphatase) . Requires Mg2+.
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Word Map
- 3.6.1.55
- glycosylase
-
sanitize
- 8-oxoguanine
-
nudix
-
misincorporation
- 8-oxo-dgmp
-
8-oxo-7,8-dihydro-2'-deoxyguanosine
-
8-oxo-7,8-dihydrodeoxyguanosine
-
mutyh
-
promutagenic
- 8-oxo-7,8-dihydroguanine
-
8-oxodgtpase
-
antimutator
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
8-oxo-dgtpase, nudt1, mutt homolog 1, mutt2, mutt homologue 1, cimutt, 8-oxo-dgtp hydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
8-oxo-dGTP diphosphohydrolase
This enzyme hydrolyses the phosphoanhydride bond between the alpha and beta phosphate of 8-oxoguanine-containing nucleoside di- and triphosphates thereby preventing misincorporation of the oxidized purine nucleoside triphosphates into DNA. It does not hydrolyse 2-hydroxy-dATP (cf. EC 3.6.1.56, 2-hydroxy-dATP diphosphatase) [4]. Requires Mg2+.
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
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
MutT exhibits high substrate specificity for 8-oxoguanine nucleotides by the ligand-induced conformational change
-
-
?
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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
specfic for the MutT protein hydrolyses other dNTPs and GTP with lower Vmax and extremely high Km-values
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
-
the MutT protein eliminates 8-oxoGTP and prevents the occurrence of transcriptional errors, which are induced particularly in the aerobic state
-
-
?
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-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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
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
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the increase in the production of erroneous proteins by oxidative damage is 28fold over the wild-type cells in Escherichia coli mutT deficient cells
physiological function
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 MutT protein of Escherichia coli degrades 8-oxoGua-containing ribonucleoside di- and triphosphates to the monophosphate, thereby preventing the misincorporation of 8-oxoGua into RNA
physiological function
-
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
physiological function
-
the enzyme 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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structures of MutT in the apo and holo forms and in the binary and ternary forms complexed with the product 8-oxo-dGMP and 8-oxo-dGMP plus Mn2+, respectively, are determined
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saraswat, V.; Massiah, M.A.; Lopez, G.; Amzel, L.M.; Mildvan, A.S.
Interactions of the products, 8-oxo-dGMP, dGMP, and pyrophosphate with the MutT nucleoside triphosphate pyrophosphohydrolase
Biochemistry
41
15566-15577
2002
Escherichia coli
Ito, R.; Hayakawa, H.; Sekiguchi, M.; Ishibashi, T.
Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools
Biochemistry
44
6670-6674
2005
Escherichia coli
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
Escherichia coli
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
Escherichia coli
Nakamura, T.; Meshitsuka, S.; Kitagawa, S.; Abe, N.; Yamada, J.; Ishino, T.; Nakano, H.; Tsuzuki, T.; Doi, T.; Kobayashi, Y.; Fujii, S.; Sekiguchi, M.; Yamagata, Y.
Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base
J. Biol. Chem.
285
444-452
2010
Escherichia coli (P08337)
Higuchi, M.; Fujii, J.; Yonetani, Y.; Kitao, A.; Go, N.
Enhanced resolution of molecular recognition to distinguish structurally similar molecules by different conformational responses of a protein upon ligand binding
J. Struct. Biol.
173
20-28
2011
Escherichia coli
Setoyama, D.; Ito, R.; Takagi, Y.; Sekiguchi, M.
Molecular actions of Escherichia coli MutT for control of spontaneous mutagenesis
Mutat. Res.
707
9-14
2010
Escherichia coli, Escherichia coli CC101
Maki, H.; Sekiguchi, M.
MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
Nature
355
273-275
1992
Escherichia coli
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
Escherichia coli
Taddei, F.; Hayakawa, H.; Bouton, M.; Cirinesi, A.; Matic, I.; Sekiguchi, M.; Radman, M.
Counteraction by MutT protein of transcriptional errors caused by oxidative damage
Science
278
128-130
1997
Escherichia coli
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