BRENDA - Enzyme Database
show all sequences of 3.5.4.13

Chloroviruses encode a bifunctional dCMP-dCTP deaminase that produces two key intermediates in dTTP formation

Zhang, Y.; Maley, F.; Maley, G.F.; Duncan, G.; Dunigan, D.D.; Van Etten, J.L.; J. Virol. 81, 7662-7671 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dCTP
activates dCMP deamination about 7fold at 0.005-0.1 mM
Paramecium bursaria Chlorella virus 1
Cloned(Commentary)
Commentary
Organism
ORF A596R, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain DH5MCR, phylogenetic analysis
Paramecium bursaria Chlorella virus 1
Inhibitors
Inhibitors
Commentary
Organism
Structure
dTTP
inhibits dCMP deamination, feedback inhibition
Paramecium bursaria Chlorella virus 1
H4dUMP
inhibits both dCTP and dCMP deaminase activities
Paramecium bursaria Chlorella virus 1
PDRP
inhibits both dCTP and dCMP deaminase activities
Paramecium bursaria Chlorella virus 1
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.64
-
dCTP
pH 9.5, 42°C
Paramecium bursaria Chlorella virus 1
0.76
-
dCMP
pH 9.5, 42°C, in presence of 0.1 mM dCTP
Paramecium bursaria Chlorella virus 1
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
can partially substitute for Mg2+
Paramecium bursaria Chlorella virus 1
Mg2+
the enzyme depends on divalent cations, Mg2+ is preferred , but can partially be substituted by Ca2+, Ni2+, or Mn2+
Paramecium bursaria Chlorella virus 1
Mn2+
can partially substitute for Mg2+
Paramecium bursaria Chlorella virus 1
Ni2+
can partially substitute for Mg2+
Paramecium bursaria Chlorella virus 1
Zn2+
the enzyme contains a zinc binding site, but shows less than 6% of maximal activity with Zn2+ as divalent cation
Paramecium bursaria Chlorella virus 1
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17000
-
6 * 17000, SDS-PAGE
Paramecium bursaria Chlorella virus 1
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dCMP + H2O
Paramecium bursaria Chlorella virus 1
-
dUMP + NH3
dUMP is a key intermediate in the synthesis of dTTP and subsequently of DNA synthesis
-
?
dCTP + H2O
Paramecium bursaria Chlorella virus 1
-
dUTP + NH3
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paramecium bursaria Chlorella virus 1
O41078
i.e. PBCV-1 , a chlorovirus from host Chlorella sp. strain NC64A
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, the protein quickly precipitates at concentration higher than 2 mg/ml
Paramecium bursaria Chlorella virus 1
Storage Stability
Storage Stability
Organism
the purified recombinant His-tagged enzyme in stable without precipitation for more than 1 year in 50% glycerol
Paramecium bursaria Chlorella virus 1
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dCMP + H2O
-
688732
Paramecium bursaria Chlorella virus 1
dUMP + NH3
-
-
-
?
dCMP + H2O
-
688732
Paramecium bursaria Chlorella virus 1
dUMP + NH3
dUMP is a key intermediate in the synthesis of dTTP and subsequently of DNA synthesis
-
-
?
dCTP + H2O
-
688732
Paramecium bursaria Chlorella virus 1
dUTP + NH3
-
-
-
?
additional information
the bifunctional dCMP-dCTP deaminase shows dCMP deaminase and dCTP deaminase activities, dCTP serves as a positive heterotropic effector for the dCMP deaminase activity and a positive homotropic effector for the dCTP deaminase activity, and the enzymatic efficiency of the dCMP deaminase activity is about four times higher than that of the dCTP deaminase activity, the same active site is involved in both dCMP and dCTP deaminations
688732
Paramecium bursaria Chlorella virus 1
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
hexamer
6 * 17000, SDS-PAGE
Paramecium bursaria Chlorella virus 1
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
42
-
-
Paramecium bursaria Chlorella virus 1
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
55
-
Paramecium bursaria Chlorella virus 1
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.7
-
dCTP
pH 9.5, 42°C
Paramecium bursaria Chlorella virus 1
24.9
-
dCMP
pH 9.5, 42°C, in presence of 0.1 mM dCTP
Paramecium bursaria Chlorella virus 1
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
dCTP deaminase activity
Paramecium bursaria Chlorella virus 1
9.5
-
dCMP deaminase activity
Paramecium bursaria Chlorella virus 1
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
11
activity range
Paramecium bursaria Chlorella virus 1
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dCTP
activates dCMP deamination about 7fold at 0.005-0.1 mM
Paramecium bursaria Chlorella virus 1
Cloned(Commentary) (protein specific)
Commentary
Organism
ORF A596R, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain DH5MCR, phylogenetic analysis
Paramecium bursaria Chlorella virus 1
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
dTTP
inhibits dCMP deamination, feedback inhibition
Paramecium bursaria Chlorella virus 1
H4dUMP
inhibits both dCTP and dCMP deaminase activities
Paramecium bursaria Chlorella virus 1
PDRP
inhibits both dCTP and dCMP deaminase activities
Paramecium bursaria Chlorella virus 1
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.64
-
dCTP
pH 9.5, 42°C
Paramecium bursaria Chlorella virus 1
0.76
-
dCMP
pH 9.5, 42°C, in presence of 0.1 mM dCTP
Paramecium bursaria Chlorella virus 1
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
can partially substitute for Mg2+
Paramecium bursaria Chlorella virus 1
Mg2+
the enzyme depends on divalent cations, Mg2+ is preferred , but can partially be substituted by Ca2+, Ni2+, or Mn2+
Paramecium bursaria Chlorella virus 1
Mn2+
can partially substitute for Mg2+
Paramecium bursaria Chlorella virus 1
Ni2+
can partially substitute for Mg2+
Paramecium bursaria Chlorella virus 1
Zn2+
the enzyme contains a zinc binding site, but shows less than 6% of maximal activity with Zn2+ as divalent cation
Paramecium bursaria Chlorella virus 1
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
17000
-
6 * 17000, SDS-PAGE
Paramecium bursaria Chlorella virus 1
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dCMP + H2O
Paramecium bursaria Chlorella virus 1
-
dUMP + NH3
dUMP is a key intermediate in the synthesis of dTTP and subsequently of DNA synthesis
-
?
dCTP + H2O
Paramecium bursaria Chlorella virus 1
-
dUTP + NH3
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, the protein quickly precipitates at concentration higher than 2 mg/ml
Paramecium bursaria Chlorella virus 1
Storage Stability (protein specific)
Storage Stability
Organism
the purified recombinant His-tagged enzyme in stable without precipitation for more than 1 year in 50% glycerol
Paramecium bursaria Chlorella virus 1
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dCMP + H2O
-
688732
Paramecium bursaria Chlorella virus 1
dUMP + NH3
-
-
-
?
dCMP + H2O
-
688732
Paramecium bursaria Chlorella virus 1
dUMP + NH3
dUMP is a key intermediate in the synthesis of dTTP and subsequently of DNA synthesis
-
-
?
dCTP + H2O
-
688732
Paramecium bursaria Chlorella virus 1
dUTP + NH3
-
-
-
?
additional information
the bifunctional dCMP-dCTP deaminase shows dCMP deaminase and dCTP deaminase activities, dCTP serves as a positive heterotropic effector for the dCMP deaminase activity and a positive homotropic effector for the dCTP deaminase activity, and the enzymatic efficiency of the dCMP deaminase activity is about four times higher than that of the dCTP deaminase activity, the same active site is involved in both dCMP and dCTP deaminations
688732
Paramecium bursaria Chlorella virus 1
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
hexamer
6 * 17000, SDS-PAGE
Paramecium bursaria Chlorella virus 1
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
42
-
-
Paramecium bursaria Chlorella virus 1
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
55
-
Paramecium bursaria Chlorella virus 1
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.7
-
dCTP
pH 9.5, 42°C
Paramecium bursaria Chlorella virus 1
24.9
-
dCMP
pH 9.5, 42°C, in presence of 0.1 mM dCTP
Paramecium bursaria Chlorella virus 1
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
dCTP deaminase activity
Paramecium bursaria Chlorella virus 1
9.5
-
dCMP deaminase activity
Paramecium bursaria Chlorella virus 1
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
11
activity range
Paramecium bursaria Chlorella virus 1
Other publictions for EC 3.5.4.13
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)
733177
Oehlenschlaeger
Bacillus halodurans strain C12 ...
Bacillus halodurans, Bacillus halodurans C-125
Appl. Environ. Microbiol.
81
3395-3404
2015
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1
1
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12
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684700
Thymark
Mutational analysis of the nuc ...
Escherichia coli
Arch. Biochem. Biophys.
470
20-26
2008
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4
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2
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1
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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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2
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686667
Johansson
Regulation of dCTP deaminase f ...
Escherichia coli
FEBS J.
274
4188-4198
2007
-
-
-
1
3
-
1
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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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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1
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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
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3
2
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5
1
2
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4
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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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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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669375
Johansson
Structures of dCTP deaminase f ...
Escherichia coli
J. Biol. Chem.
280
3051-3059
2005
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1
3
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3
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648212
Huffman
Structural basis for recogniti ...
Methanocaldococcus jannaschii
J. Mol. Biol.
331
885-896
2003
-
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1
1
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2
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1
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652395
Bjornberg
A bifunctional dCTP deaminase- ...
Methanocaldococcus jannaschii
J. Biol. Chem.
278
20667-20672
2003
-
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1
-
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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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2
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1
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2
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
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1
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2
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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
-
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2
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1
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5
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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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3
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-
-
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-
-
-
-
-
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-
209517
Wang
5-Methyl-dCTP deaminase induce ...
Xanthomonas oryzae
J. Virol.
42
42-48
1982
-
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1
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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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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
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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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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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1
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209520
Price
Bacteriophage PBS2-induced deo ...
Bacillus subtilis
J. Virol.
14
1314-1317
1974
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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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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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2
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1
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3
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1
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