Data extracted from this reference:
Crystallization (Commentary)
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
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
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]
additional information
additional information
enzyme kinetics and equilibrium binding
Escherichia coli
Metals/Ions
Natural Substrates/ Products (Substrates)
dCTP + H2O
Escherichia coli
dUTP + NH3
?
Organism
Substrates and Products (Substrate)
dCTP + H2O
686667
Escherichia coli
dUTP + NH3
?
Temperature Optimum [°C]
37
assay at
Escherichia coli
pH Optimum
6.8
assay at
Escherichia coli
Crystallization (Commentary) (protein specific)
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)
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)
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)
additional information
additional information
enzyme kinetics and equilibrium binding
Escherichia coli
Metals/Ions (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
dCTP + H2O
Escherichia coli
dUTP + NH3
?
Substrates and Products (Substrate) (protein specific)
dCTP + H2O
686667
Escherichia coli
dUTP + NH3
?
Temperature Optimum [°C] (protein specific)
37
assay at
Escherichia coli
pH Optimum (protein specific)
6.8
assay at
Escherichia coli
Other publictions for EC
733177
Oehlenschlaeger
Bacillus halodurans strain C12 ...
Bacillus halodurans, Bacillus halodurans C-125
Appl. Environ. Microbiol.
81
3395-3404
2015
1
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12
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-
-
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-
684700
Thymark
Mutational analysis of the nuc ...
Escherichia coli
Arch. Biochem. Biophys.
470
20-26
2008
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1
4
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2
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1
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2
1
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688399
Helt
Mechanism of dTTP inhibition o ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Mol. Biol.
376
554-569
2008
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1
1
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6
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686667
Johansson
Regulation of dCTP deaminase f ...
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FEBS J.
274
4188-4198
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1
3
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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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1
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688732
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Chloroviruses encode a bifunct ...
Paramecium bursaria Chlorella virus 1
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7662-7671
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1
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1
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1
2
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1
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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
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2
2
1
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-
-
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-
669375
Johansson
Structures of dCTP deaminase f ...
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J. Biol. Chem.
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2005
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-
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1
3
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3
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1
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1
3
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648212
Huffman
Structural basis for recogniti ...
Methanocaldococcus jannaschii
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331
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-
-
1
1
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-
-
-
-
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-
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2
-
-
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1
-
-
-
-
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1
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-
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-
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-
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1
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1
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-
-
-
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-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
652395
Bjornberg
A bifunctional dCTP deaminase- ...
Methanocaldococcus jannaschii
J. Biol. Chem.
278
20667-20672
2003
-
-
1
-
-
-
2
1
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1
2
1
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4
-
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1
-
-
-
-
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4
1
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-
-
-
-
-
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2
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1
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-
-
-
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2
2
1
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1
2
1
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-
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1
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-
-
-
4
1
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-
-
-
-
-
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209525
Estevenon
An Escherichia coli strain def ...
Escherichia coli
Mol. Gen. Genet.
246
514-518
1995
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-
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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-
-
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
-
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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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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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-
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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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3
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1
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4
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1
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1
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1
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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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1
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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1
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3
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3
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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-
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-
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209519
Beck
Deoxycytidine triphosphate dea ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Biol. Chem.
250
609-616
1975
-
-
-
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7
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4
1
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1
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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7
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4
1
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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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1
-
-
-
-
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-
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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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1
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1
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1
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7
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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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209521
Tomita
A novel enzyme, dCTP deaminase ...
Bacillus subtilis
Biochim. Biophys. Acta
179
18-27
1969
-
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3
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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