BRENDA - Enzyme Database show
show all sequences of 3.6.1.55

Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools

Ito, R.; Hayakawa, H.; Sekiguchi, M.; Ishibashi, T.; Biochemistry 44, 6670-6674 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
MutT protein is produced as a His-tagged form in Escherichia coli M15
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.000045
-
8-oxo-GDP
pH 8.0, 30C
Escherichia coli
0.000058
-
8-oxo-dGDP
pH 8.0, 30C
Escherichia coli
0.000081
-
8-oxo-dGTP
pH 8.0, 30C
Escherichia coli
0.00026
-
8-oxo-GTP
pH 8.0, 30C
Escherichia coli
0.17
-
dGDP
pH 8.0, 30C
Escherichia coli
0.35
-
GDP
pH 8.0, 30C
Escherichia coli
1
-
GTP
pH 8.0, 30C
Escherichia coli
1.1
-
dGTP
pH 8.0, 30C
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
8-oxo-dGDP + H2O
Escherichia coli
-
8-oxo-dGMP + phosphate
-
-
?
8-oxo-dGTP + H2O
Escherichia coli
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-dGMP + diphosphate
-
-
?
8-oxo-GDP + H2O
Escherichia coli
-
8-oxo-GMP + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
8-oxo-dGDP + H2O
-
667672
Escherichia coli
8-oxo-dGMP + phosphate
-
-
-
?
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
667672
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
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
667672
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-GDP + H2O
-
667672
Escherichia coli
8-oxo-GMP + phosphate
-
-
-
?
8-oxo-GTP + H2O
-
667672
Escherichia coli
8-oxo-GMP + diphosphate
-
-
-
?
dGDP + H2O
-
667672
Escherichia coli
dGMP + phosphate
-
-
-
?
dGTP + H2O
-
667672
Escherichia coli
dGMP + diphosphate
-
-
-
?
GDP + H2O
-
667672
Escherichia coli
GMP + phosphate
-
-
-
?
GTP + H2O
-
667672
Escherichia coli
GMP + diphosphate
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
MutT protein is produced as a His-tagged form in Escherichia coli M15
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.000045
-
8-oxo-GDP
pH 8.0, 30C
Escherichia coli
0.000058
-
8-oxo-dGDP
pH 8.0, 30C
Escherichia coli
0.000081
-
8-oxo-dGTP
pH 8.0, 30C
Escherichia coli
0.00026
-
8-oxo-GTP
pH 8.0, 30C
Escherichia coli
0.17
-
dGDP
pH 8.0, 30C
Escherichia coli
0.35
-
GDP
pH 8.0, 30C
Escherichia coli
1
-
GTP
pH 8.0, 30C
Escherichia coli
1.1
-
dGTP
pH 8.0, 30C
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
8-oxo-dGDP + H2O
Escherichia coli
-
8-oxo-dGMP + phosphate
-
-
?
8-oxo-dGTP + H2O
Escherichia coli
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-dGMP + diphosphate
-
-
?
8-oxo-GDP + H2O
Escherichia coli
-
8-oxo-GMP + phosphate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
8-oxo-dGDP + H2O
-
667672
Escherichia coli
8-oxo-dGMP + phosphate
-
-
-
?
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
667672
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
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
667672
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-GDP + H2O
-
667672
Escherichia coli
8-oxo-GMP + phosphate
-
-
-
?
8-oxo-GTP + H2O
-
667672
Escherichia coli
8-oxo-GMP + diphosphate
-
-
-
?
dGDP + H2O
-
667672
Escherichia coli
dGMP + phosphate
-
-
-
?
dGTP + H2O
-
667672
Escherichia coli
dGMP + diphosphate
-
-
-
?
GDP + H2O
-
667672
Escherichia coli
GMP + phosphate
-
-
-
?
GTP + H2O
-
667672
Escherichia coli
GMP + diphosphate
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Escherichia coli
Other publictions for EC 3.6.1.55
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733536
Tanaka
Structure and molecular charac ...
Hordeum vulgare subsp. vulgare
Biosci. Biotechnol. Biochem.
79
394-401
2015
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1
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1
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1
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1
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1
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1
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1
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1
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2
1
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-
1
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1
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720027
Takagi
Human MTH3 (NUDT18) protein hy ...
Homo sapiens
J. Biol. Chem.
287
21541-21549
2012
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-
1
-
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1
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1
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1
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3
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1
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3
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716070
Higuchi
Enhanced resolution of molecul ...
Escherichia coli
J. Struct. Biol.
173
20-28
2011
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2
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718500
Buchko
Structure of a Nudix hydrolase ...
Bartonella henselae
Acta Crystallogr. Sect. F
67
1078-1083
2011
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1
1
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715113
Yonekura
CiMutT, an asidian MutT homolo ...
Ciona intestinalis
Genes Genet. Syst.
85
287-295
2010
-
-
1
-
-
-
-
1
-
1
1
2
-
4
-
-
1
-
-
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1
-
5
-
1
1
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1
1
1
-
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1
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-
-
-
-
1
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1
1
2
-
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-
1
-
-
1
-
5
-
1
1
-
1
1
1
-
-
-
1
1
-
2
2
715573
Nakamura
Structural and dynamic feature ...
Escherichia coli
J. Biol. Chem.
285
444-452
2010
-
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1
1
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1
-
1
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1
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2
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1
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1
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1
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1
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2
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716300
Setoyama
Molecular actions of Escherich ...
Escherichia coli, Escherichia coli CC101
Mutat. Res.
707
9-14
2010
-
-
-
-
-
-
-
-
-
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2
-
2
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4
-
1
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1
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2
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4
-
1
-
-
-
1
-
-
-
1
1
1
1
-
-
667672
Ito
Multiple enzyme activities of ...
Escherichia coli
Biochemistry
44
6670-6674
2005
-
-
1
-
-
-
-
8
-
-
-
3
-
1
-
-
-
-
-
-
-
-
9
-
1
-
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-
1
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-
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-
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1
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-
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-
8
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3
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9
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1
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1
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-
716365
Ishibashi
Mammalian enzymes for preventi ...
Escherichia coli
Nucleic Acids Res.
33
3779-3784
2005
-
-
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-
-
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1
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1
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2
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2
2
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654634
Saraswat
Interactions of the products, ...
Escherichia coli
Biochemistry
41
15566-15577
2002
-
-
-
-
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-
3
-
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2
-
1
-
1
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-
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-
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3
-
1
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-
-
1
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-
-
10
-
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-
3
10
-
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2
-
1
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-
-
-
-
-
-
-
3
-
1
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-
-
1
-
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715460
Sakai
A molecular basis for the sele ...
Escherichia coli
J. Biol. Chem.
277
8579-8587
2002
-
-
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1
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1
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1
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1
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2
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1
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1
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715439
Fujikawa
The oxidized forms of dATP are ...
Escherichia coli
J. Biol. Chem.
274
18201-18205
1999
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1
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1
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716917
Taddei
Counteraction by MutT protein ...
Escherichia coli
Science
278
128-130
1997
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716320
Maki
MutT protein specifically hydr ...
Escherichia coli
Nature
355
273-275
1992
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1
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