BRENDA - Enzyme Database
show all sequences of 2.7.4.25

Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme

Bertrand, T.; Briozzo, P.; Assairi, L.; Ofiteru, A.; Bucurenci, N.; Munier-Lehmann, H.; Golinelli-Pimpaneau, B.; Barzu, O.; Gilles, A.M.; J. Mol. Biol. 315, 1099-1110 (2002)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli BL21(DE3) cells
Escherichia coli
Crystallization (Commentary)
Crystallization (Commentary)
Organism
in complex with substrates CMP, dCMP, ara-CMP and 2’,3’-dideoxy-CMP, hanging drop vapor diffusion method, using ammonium sulfate in a 50 mM Tris-HCl buffer (pH 7.4), at 20°C
Escherichia coli
Engineering
Protein Variants
Commentary
Organism
D185A
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
Escherichia coli
R181M
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
Escherichia coli
S101A
the mutation reduces CMP phosphorylation only moderately, but dramatically reduces dCMP phosphorylation
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.08
-
CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.094
-
dCMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.15
-
2',3'-dideoxy-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.19
-
CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.19
-
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.24
-
dCMP
mutant enzyme D185A, at 30°C and pH 7.4; mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.46
-
2',3'-dideoxy-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.47
-
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.47
-
CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.53
-
ara-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.54
-
2',3'-dideoxy-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.65
-
2',3'-dideoxy-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.79
-
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
1
-
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required for activity
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + CMP
Escherichia coli
-
ADP + CDP
-
-
?
ATP + dCMP
Escherichia coli
Escherichia coli CMPK phosphorylates dCMP nearly as well as it does CMP
ADP + dCDP
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
A0A140N8S7
-
-
Purification (Commentary)
Purification (Commentary)
Organism
Ni-NTA column chromatography
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + 2',3'-dideoxy-CMP
2’,3’-dideoxy-CMP is a poor substrate
712736
Escherichia coli
ADP + ?
-
-
-
?
ATP + ara-CMP
ara-CMP is a poor substrate
712736
Escherichia coli
ADP + ara-CDP
-
-
-
?
ATP + CMP
-
712736
Escherichia coli
ADP + CDP
-
-
-
?
ATP + dCMP
Escherichia coli CMPK phosphorylates dCMP nearly as well as it does CMP
712736
Escherichia coli
ADP + dCDP
-
-
-
?
ATP + UMP
bacterial CMP kinases phosphorylate UMP with very low rates
712736
Escherichia coli
ADP + UDP
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
CMP kinase
-
Escherichia coli
CMPK
-
Escherichia coli
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
52
-
the melting temperature of the wild type enzyme is at 52°C
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0083
-
2',3'-dideoxy-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.047
-
2',3'-dideoxy-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.071
-
dCMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.08
-
CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.085
-
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.12
-
2',3'-dideoxy-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.19
-
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.26
-
CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.45
-
dCMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.47
-
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.65
-
2',3'-dideoxy-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
1.36
-
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
1.38
-
CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
56
-
ara-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
103
-
CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
109
-
dCMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
in complex with substrates CMP, dCMP, ara-CMP and 2’,3’-dideoxy-CMP, hanging drop vapor diffusion method, using ammonium sulfate in a 50 mM Tris-HCl buffer (pH 7.4), at 20°C
Escherichia coli
Engineering (protein specific)
Protein Variants
Commentary
Organism
D185A
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
Escherichia coli
R181M
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
Escherichia coli
S101A
the mutation reduces CMP phosphorylation only moderately, but dramatically reduces dCMP phosphorylation
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.035
-
CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.08
-
CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.094
-
dCMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.15
-
2',3'-dideoxy-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.19
-
CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.19
-
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.24
-
dCMP
mutant enzyme D185A, at 30°C and pH 7.4; mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.46
-
2',3'-dideoxy-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.47
-
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.47
-
CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.53
-
ara-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.54
-
2',3'-dideoxy-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.65
-
2',3'-dideoxy-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.79
-
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
1
-
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required for activity
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + CMP
Escherichia coli
-
ADP + CDP
-
-
?
ATP + dCMP
Escherichia coli
Escherichia coli CMPK phosphorylates dCMP nearly as well as it does CMP
ADP + dCDP
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
Ni-NTA column chromatography
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + 2',3'-dideoxy-CMP
2’,3’-dideoxy-CMP is a poor substrate
712736
Escherichia coli
ADP + ?
-
-
-
?
ATP + ara-CMP
ara-CMP is a poor substrate
712736
Escherichia coli
ADP + ara-CDP
-
-
-
?
ATP + CMP
-
712736
Escherichia coli
ADP + CDP
-
-
-
?
ATP + dCMP
Escherichia coli CMPK phosphorylates dCMP nearly as well as it does CMP
712736
Escherichia coli
ADP + dCDP
-
-
-
?
ATP + UMP
bacterial CMP kinases phosphorylate UMP with very low rates
712736
Escherichia coli
ADP + UDP
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
52
-
the melting temperature of the wild type enzyme is at 52°C
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0083
-
2',3'-dideoxy-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.047
-
2',3'-dideoxy-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
0.071
-
dCMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.08
-
CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.085
-
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.12
-
2',3'-dideoxy-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.19
-
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.26
-
CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli
0.45
-
dCMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
0.47
-
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
0.65
-
2',3'-dideoxy-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli
1.36
-
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
1.38
-
CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli
56
-
ara-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
103
-
CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
109
-
dCMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.083
-
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli K-12
0.3
-
dCMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli K-12
0.54
-
CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli K-12
1.7
-
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli K-12
1.9
-
dCMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli K-12
6.1
-
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli K-12
7.4
-
CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli K-12
7.5
-
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli K-12
105
-
ara-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli K-12
697
-
CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli K-12
1160
-
dCMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli K-12
2940
-
CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli K-12
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.083
-
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli K-12
0.3
-
dCMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli K-12
0.54
-
CMP
mutant enzyme D185A, at 30°C and pH 7.4
Escherichia coli K-12
1.7
-
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli K-12
1.9
-
dCMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli K-12
6.1
-
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli K-12
7.4
-
CMP
mutant enzyme R181M, at 30°C and pH 7.4
Escherichia coli K-12
7.5
-
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli K-12
105
-
ara-CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli K-12
697
-
CMP
mutant enzyme S101A, at 30°C and pH 7.4
Escherichia coli K-12
1160
-
dCMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli K-12
2940
-
CMP
wild type enzyme, at 30°C and pH 7.4
Escherichia coli K-12
Other publictions for EC 2.7.4.25
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)
712276
Thum
The Rv1712 locus from Mycobact ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Bacteriol.
191
2884-2887
2009
-
-
1
-
-
-
-
3
-
-
3
-
-
172
-
-
1
-
-
-
-
2
6
1
2
-
-
-
3
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
3
-
-
3
-
-
-
-
1
-
-
-
2
6
1
-
-
-
3
-
-
-
-
-
1
1
-
3
3
693707
Caceres
Molecular modeling and dynamic ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Mol. Model.
14
427-434
2008
-
-
1
-
-
-
-
-
-
1
-
2
-
6
-
-
-
-
-
-
-
-
6
1
9
-
-
-
-
-
-
-
1
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
6
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673586
Wang
The role of Ureaplasma nucleos ...
Ureaplasma parvum
FEBS J.
274
1983-1990
2007
-
-
1
-
-
-
-
-
-
1
1
-
-
1
-
-
1
-
-
-
-
-
4
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
676227
Alexandre
Enantioselectivity of human AM ...
Escherichia coli
Nucleic Acids Res.
35
4895-4904
2007
-
-
1
1
7
-
-
23
-
-
-
-
-
1
-
-
1
-
-
-
-
-
3
-
3
-
-
6
-
-
-
-
-
-
-
-
-
-
1
-
1
7
-
-
-
-
23
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
692282
Ofiteru
Structural and functional cons ...
Escherichia coli, Escherichia coli K-12
FEBS J.
274
3363-3373
2007
-
-
2
2
14
1
-
27
-
1
1
3
-
2
-
-
1
-
-
-
1
-
8
-
2
-
-
1
26
-
-
-
2
-
-
-
-
-
2
2
2
14
1
-
-
-
27
-
1
1
3
-
-
-
1
-
-
1
-
8
-
-
-
1
26
-
-
-
-
-
-
-
-
23
23
675215
Lee
-
Recombinant Escherichia coli-c ...
Escherichia coli
J. Ind. Eng. Chem.
12
757-761
2006
-
1
1
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
713473
Yu
Solution structure and functio ...
Streptococcus pneumoniae TIGR4
Protein Sci.
12
2613-2621
2003
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
712736
Bertrand
Sugar specificity of bacterial ...
Escherichia coli
J. Mol. Biol.
315
1099-1110
2002
-
-
1
1
3
-
-
15
-
1
-
2
-
1
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1
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