Information on EC 3.6.1.55 - 8-oxo-dGTP diphosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.6.1.55
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RECOMMENDED NAME
GeneOntology No.
8-oxo-dGTP diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oxidized GTP and dGTP detoxification
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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+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Q6G5F4
UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Escherichia coli strain CC101
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-
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydro-8-oxo-GTP + H2O
7,8-dihydro-8-oxo-GMP + diphosphate
show the reaction diagram
Q6G5F4
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-
-
?
8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
show the reaction diagram
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
show the reaction diagram
8-oxo-GDP + H2O
8-oxo-GMP + phosphate
show the reaction diagram
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
show the reaction diagram
dGDP + H2O
dGMP + phosphate
show the reaction diagram
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-
-
-
?
dGTP + H2O
dGMP + diphosphate
show the reaction diagram
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-
-
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?
GDP + H2O
GMP + phosphate
show the reaction diagram
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-
-
-
?
GTP + H2O
GMP + diphosphate
show the reaction diagram
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-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
8-oxo-dGDP + H2O
8-oxo-dGMP + phosphate
show the reaction diagram
-
-
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
show the reaction diagram
8-oxo-GDP + H2O
8-oxo-GMP + phosphate
show the reaction diagram
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-
-
-
?
8-oxo-GTP + H2O
8-oxo-GMP + diphosphate
show the reaction diagram
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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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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-oxo-dGMP
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noncompetitive inhibitor of dGTP hydrolysis
dGMP
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noncompetitive inhibitor of dGTP hydrolysis
diphosphate
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linear uncompetitive inhibitor of dGTP hydrolysis
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000058
8-oxo-dGDP
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pH 8.0, 30C
0.000081 - 0.48
8-oxo-dGTP
0.000045 - 0.0117
8-oxo-GDP
0.00026
8-oxo-GTP
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pH 8.0, 30C
0.17
dGDP
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pH 8.0, 30C
1.1
dGTP
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pH 8.0, 30C
0.35
GDP
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pH 8.0, 30C
1
GTP
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pH 8.0, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.55
8-oxo-dGTP
Ciona intestinalis
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pH 9.5, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15 - 150
8-oxo-dGTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000049 - 0.00162
8-oxo-dGMP
1.74 - 14.5
dGMP
0.413 - 4.95
diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.8
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pH 9.5, 30C, 8-oxo-dGTP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 10.5
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pH 8.5: about 60% of maximal activity, pH 10.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
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assay at
37
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 38
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20C: about 50% of maximal activity, 38C: about 80% of maximal activity
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20400
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 4000, 0.1 M MgCl2
Q6G5F4
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
Q6G5F4
the enzyme irreversibly unfolds and precipitates out of solution upon heating, with a melting temperature of 60C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography, HiTrap heparin column chromatography, and Mono S column chromatography
nickel Sepharose column chromatography and Superdex 75 gel filtration
Q6G5F4
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3)-R3-pRARE2 cells
Q6G5F4
expression in Escherichia coli
expression in Escherichia coli CC101 mttT mutant; expression in Escherichia coli mutT mutant. CiMutT significantly suppressed the mutator activity of Escherichia coli mutT mutant
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MutT protein is produced as a His-tagged form in Escherichia coli M15
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is upregulated by drought and UV-C stress
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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