BRENDA - Enzyme Database show
show all sequences of 3.6.1.55

Structure of a Nudix hydrolase (MutT) in the Mg2+-bound state from Bartonella henselae, the bacterium responsible for cat scratch fever

Buchko, G.W.; Edwards, T.E.; Abendroth, J.; Arakaki, T.L.; Law, L.; Napuli, A.J.; Hewitt, S.N.; Van Voorhis, W.C.; Stewart, L.J.; Staker, B.L.; Myler, P.J.; Acta Crystallogr. Sect. F 67, 1078-1083 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3)-R3-pRARE2 cells
Bartonella henselae
Crystallization (Commentary)
Crystallization
Organism
sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 4000, 0.1 M MgCl2
Bartonella henselae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
the enzyme binds catalytically essential Mg2+
Bartonella henselae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bartonella henselae
Q6G5F4
-
-
Purification (Commentary)
Commentary
Organism
nickel Sepharose column chromatography and Superdex 75 gel filtration
Bartonella henselae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7,8-dihydro-8-oxo-GTP + H2O
-
718500
Bartonella henselae
7,8-dihydro-8-oxo-GMP + diphosphate
-
-
-
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
-
the enzyme irreversibly unfolds and precipitates out of solution upon heating, with a melting temperature of 60°C
Bartonella henselae
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3)-R3-pRARE2 cells
Bartonella henselae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 4000, 0.1 M MgCl2
Bartonella henselae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
the enzyme binds catalytically essential Mg2+
Bartonella henselae
Purification (Commentary) (protein specific)
Commentary
Organism
nickel Sepharose column chromatography and Superdex 75 gel filtration
Bartonella henselae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7,8-dihydro-8-oxo-GTP + H2O
-
718500
Bartonella henselae
7,8-dihydro-8-oxo-GMP + diphosphate
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
60
-
the enzyme irreversibly unfolds and precipitates out of solution upon heating, with a melting temperature of 60°C
Bartonella henselae
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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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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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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1
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715113
Yonekura
CiMutT, an asidian MutT homolo ...
Ciona intestinalis
Genes Genet. Syst.
85
287-295
2010
-
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1
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1
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1
1
2
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4
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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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5
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1
1
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1
1
1
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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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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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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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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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715439
Fujikawa
The oxidized forms of dATP are ...
Escherichia coli
J. Biol. Chem.
274
18201-18205
1999
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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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