BRENDA - Enzyme Database
show all sequences of 3.5.4.13

Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme

Johansson, E.; Thymark, M.; Bynck, J.H.; Fanoe, M.; Larsen, S.; Willemoes, M.; FEBS J. 274, 4188-4198 (2007)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
mutant E138A bound to dTTP and mutant H121A bound to dCTP, hanging drop vapour diffusion method, 3.7 mg/ml E138A or 5.1 mg/ml H121A in 20 mM magnesium chloride, 50 mM HEPES, pH 6.8, and 5 mM nucleotide, mixing of 0.002 ml of protein solution with an equal volume of reservoir solution containing 34% PEG 400, 0.2 mM MgCl2, and 0.1 m HEPES, pH 7.5, equilibration against 1 ml of mother liquor, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.6-2.7 A resolution
Escherichia coli
Engineering
Protein Variants
Commentary
Organism
E138A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
Escherichia coli
H121A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
Escherichia coli
V122G
site-directed mutagenesis, inactive mutant
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
dTTP
inhibits the enzyme in a nonallosterical way, cooperative kinetics are imposed by a dTTP-dependent lag of product formation observed in presteady-state kinetics, the lag may be derived from a slow equilibration between an inactive and an active conformation of dCTP deaminase represented by the dTTP complex and the dUTP/dCTP complex, respectively, steady-state kinetic analysis of dTTP inhibition, overview
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
enzyme kinetics and equilibrium binding
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
dCTP + H2O
Escherichia coli
-
dUTP + NH3
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P28248
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
dCTP + H2O
-
686667
Escherichia coli
dUTP + NH3
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
assay at
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
mutant E138A bound to dTTP and mutant H121A bound to dCTP, hanging drop vapour diffusion method, 3.7 mg/ml E138A or 5.1 mg/ml H121A in 20 mM magnesium chloride, 50 mM HEPES, pH 6.8, and 5 mM nucleotide, mixing of 0.002 ml of protein solution with an equal volume of reservoir solution containing 34% PEG 400, 0.2 mM MgCl2, and 0.1 m HEPES, pH 7.5, equilibration against 1 ml of mother liquor, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.6-2.7 A resolution
Escherichia coli
Engineering (protein specific)
Protein Variants
Commentary
Organism
E138A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
Escherichia coli
H121A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
Escherichia coli
V122G
site-directed mutagenesis, inactive mutant
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
dTTP
inhibits the enzyme in a nonallosterical way, cooperative kinetics are imposed by a dTTP-dependent lag of product formation observed in presteady-state kinetics, the lag may be derived from a slow equilibration between an inactive and an active conformation of dCTP deaminase represented by the dTTP complex and the dUTP/dCTP complex, respectively, steady-state kinetic analysis of dTTP inhibition, overview
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
enzyme kinetics and equilibrium binding
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
dCTP + H2O
Escherichia coli
-
dUTP + NH3
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
dCTP + H2O
-
686667
Escherichia coli
dUTP + NH3
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
assay at
Escherichia coli
Other publictions for EC
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
Synonyms
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)
733177
Oehlenschlaeger
Bacillus halodurans strain C12 ...
Bacillus halodurans, Bacillus halodurans C-125
Appl. Environ. Microbiol.
81
3395-3404
2015
1
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1
1
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1
-
-
-
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2
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12
-
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1
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2
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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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-
-
-
-
-
-
-
-
-
-
-
-
-
684700
Thymark
Mutational analysis of the nuc ...
Escherichia coli
Arch. Biochem. Biophys.
470
20-26
2008
-
-
-
1
4
-
1
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1
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1
-
3
-
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2
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1
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1
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1
4
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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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2
1
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-
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-
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-
-
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688399
Helt
Mechanism of dTTP inhibition o ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Mol. Biol.
376
554-569
2008
-
-
-
-
-
-
1
1
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6
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2
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-
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-
-
-
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-
686667
Johansson
Regulation of dCTP deaminase f ...
Escherichia coli
FEBS J.
274
4188-4198
2007
-
-
-
1
3
-
1
1
-
1
-
1
-
2
-
-
-
-
-
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-
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1
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1
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1
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1
3
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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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-
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-
-
-
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688732
Zhang
Chloroviruses encode a bifunct ...
Paramecium bursaria Chlorella virus 1
J. Virol.
81
7662-7671
2007
1
-
1
-
-
-
3
2
-
5
1
2
-
4
-
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1
-
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1
4
1
1
1
1
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2
2
1
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1
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1
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3
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2
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5
1
2
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1
-
-
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1
4
1
1
1
-
2
2
1
-
-
-
-
-
-
-
-
669375
Johansson
Structures of dCTP deaminase f ...
Escherichia coli
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280
3051-3059
2005
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1
3
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3
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1
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648212
Huffman
Structural basis for recogniti ...
Methanocaldococcus jannaschii
J. Mol. Biol.
331
885-896
2003
-
-
1
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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-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
652395
Bjornberg
A bifunctional dCTP deaminase- ...
Methanocaldococcus jannaschii
J. Biol. Chem.
278
20667-20672
2003
-
-
1
-
-
-
2
1
-
1
2
1
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4
-
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1
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4
1
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2
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1
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2
1
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1
2
1
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1
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4
1
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209525
Estevenon
An Escherichia coli strain def ...
Escherichia coli
Mol. Gen. Genet.
246
514-518
1995
-
-
1
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2
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1
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209524
Weiss
De novo synthesis of thymidyla ...
Escherichia coli
J. Bacteriol.
176
2194-2199
1994
-
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2
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1
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-
-
-
-
209522
Wang
Dcd (dCTP deaminase) gene of E ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
J. Bacteriol.
174
5647-5653
1992
-
-
2
-
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1
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5
-
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2
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2
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209523
Speed
Deamination of deoxycytidine n ...
Escherichia coli, Rickettsia prowazekii, Salmonella enterica subsp. enterica serovar Typhimurium
J. Bacteriol.
173
4902-4903
1991
-
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5
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3
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209517
Wang
5-Methyl-dCTP deaminase induce ...
Xanthomonas oryzae
J. Virol.
42
42-48
1982
-
-
-
-
-
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4
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209518
Neuhard
dCTP Deaminase from Salmonella ...
Salmonella enterica subsp. enterica serovar Typhimurium
Methods Enzymol.
51
418-423
1978
-
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3
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3
1
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2
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209519
Beck
Deoxycytidine triphosphate dea ...
Salmonella enterica subsp. enterica serovar Typhimurium
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250
609-616
1975
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1
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209520
Price
Bacteriophage PBS2-induced deo ...
Bacillus subtilis
J. Virol.
14
1314-1317
1974
-
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7
1
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1
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3
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209521
Tomita
A novel enzyme, dCTP deaminase ...
Bacillus subtilis
Biochim. Biophys. Acta
179
18-27
1969
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1
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