BRENDA - Enzyme Database show
show all sequences of 3.6.1.55

Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base

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.; J. Biol. Chem. 285, 444-452 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
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
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
8-oxo-dGTP + H2O
Escherichia coli
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
8-oxo-dGMP + diphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P08337
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
8-oxo-dGTP + H2O
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
715573
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-dGTP + H2O
MutT exhibits high substrate specificity for 8-oxoguanine nucleotides by the ligand-induced conformational change
715573
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
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-dGTP + H2O
Escherichia coli
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
8-oxo-dGMP + diphosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
8-oxo-dGTP + H2O
the activity of MutT can prevent the misincorporation of 8-oxoguanine opposite adenine in DNA
715573
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
8-oxo-dGTP + H2O
MutT exhibits high substrate specificity for 8-oxoguanine nucleotides by the ligand-induced conformational change
715573
Escherichia coli
8-oxo-dGMP + diphosphate
-
-
-
?
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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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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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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1
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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
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4
-
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1
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1
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5
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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
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1
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5
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1
1
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1
1
1
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1
1
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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
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1
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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
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2
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4
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4
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1
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1
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1
1
1
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667672
Ito
Multiple enzyme activities of ...
Escherichia coli
Biochemistry
44
6670-6674
2005
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1
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8
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3
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1
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9
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1
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1
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1
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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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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
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1
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1
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3
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1
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1
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-
10
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3
10
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2
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1
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3
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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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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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1
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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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1
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1
1
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