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Literature summary extracted from

  • Ofiteru, A.; Bucurenci, N.; Alexov, E.; Bertrand, T.; Briozzo, P.; Munier-Lehmann, H.; Gilles, A.M.
    Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase (2007), FEBS J., 274, 3363-3373.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.25 expressed in Escherichia coli BL21(DE3) cells Escherichia coli K-12
2.7.4.25 expression of wild-type and mutant enzymes Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.25 mutant enzyme R188M is crystallized either alone or in complex with dCMP, hanging drop vapor diffusion method, using ammonium sulfate as a precipitant (1.3 M in the case of enzyme alone, and 1.7 M for the R188M-dCMP complex) Escherichia coli K-12
2.7.4.25 purified recombinant mutant R188M free or in complex with CMP, X-ray diffraction structure determination and analysis at 1.9 A and 2.8 A resolution, respectively Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.4.25 D132A the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP Escherichia coli
2.7.4.25 D132A the mutant shows reduced activity compared to the wild type enzyme, the mutation has the most dramatic consequences on the protein stability as Tm decreases by 9°C in comparison with the wild type protein, an increase in the specificity of the D132A variant for UMP over CMP and dCMP is observed Escherichia coli K-12
2.7.4.25 D132H the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP, the D132H variant does not introduce charge reversal, because His is calculated to be deprotonated Escherichia coli
2.7.4.25 D132H the mutant shows reduced activity compared to the wild type enzyme Escherichia coli K-12
2.7.4.25 D132N the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP Escherichia coli
2.7.4.25 D132N the mutant shows reduced activity compared to the wild type enzyme Escherichia coli K-12
2.7.4.25 D132S the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP Escherichia coli
2.7.4.25 D132S the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP Escherichia coli K-12
2.7.4.25 R110M the side chains of Arg110 cannot establish hydrogen bonds with UMP, and its substitution by hydrophobic amino acids simultaneously affects the Km of CMP/dCMP and the kcat value Escherichia coli
2.7.4.25 R110M the mutant shows reduced activity compared to the wild type enzyme Escherichia coli K-12
2.7.4.25 R188M replacement of Arg188 with Met does not affect enzyme stability but dramatically decreases the kcat/Km ratio compared to the wild-type enzyme Escherichia coli
2.7.4.25 R188M the mutation does not affect enzyme stability but dramatically decreases the kcat_Km ratio compared with wild type enzyme, the mutant has no activity towards UMP Escherichia coli K-12
2.7.4.25 S36A the side chains of Arg110 cannot establish hydrogen bonds with UMP, and its substitution by hydrophobic amino acids simultaneously affects the Km of CMP/dCMP and the kcat value Escherichia coli
2.7.4.25 S36A the S36A substitution mainly changes the Km value for the two natural substrates, which increases by a factor of 70 (CMP) and 37 (dCMP) compared with the parent molecule and decreases kcat of 1.6fold (CMP) and 7.4fold (dCMP) with respect to the wild type enzyme Escherichia coli K-12

General Stability

EC Number General Stability Organism
2.7.4.25 four key amino acids interacting with the pyrimidine ring of CMP, Ser36, Asp132, Arg110 and Arg188, contribute to the stability, catalysis and substrate specificity of Escherichia coli CMP kinase Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.25 additional information
-
additional information kinetics and substrate specificities of wild-type and mutant enzymes, overview Escherichia coli
2.7.4.25 0.035
-
CMP wild-type enzyme Escherichia coli
2.7.4.25 0.035
-
CMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.038
-
CMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.0394
-
dCMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.055
-
dCMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.08
-
dCMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.09
-
dCMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.094
-
dCMP wild-type enzyme Escherichia coli
2.7.4.25 0.77
-
dCMP mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.93
-
UMP wild-type enzyme Escherichia coli
2.7.4.25 0.93
-
UMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1
-
CMP mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.3
-
CMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.8
-
dCMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.9
-
UMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 2.5
-
CMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 2.6
-
CMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 2.9
-
CMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 3.5
-
dCMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 3.9
-
UMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 5.4
-
UMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 7.3
-
dCMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 7.9
-
UMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 8
-
UMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 11.3
-
UMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 20.2
-
CMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.25 Mg2+ required Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.4.25 24700
-
calculated from amino acid sequence Escherichia coli K-12

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.25 ATP + CMP Escherichia coli
-
ADP + CDP
-
r
2.7.4.25 ATP + dCMP Escherichia coli
-
ADP + dCDP
-
r
2.7.4.25 additional information Escherichia coli bacterial CMP kinases are specific for CMP and dCMP, whereas the related eukaryotic NMP kinase phosphorylates CMP and UMP with similar efficiency. Bacterial CMP kinase has a narrower NMP-binding pocket and a hydrogen-bonding network involving the pyrimidine moiety specific for the cytosine nucleobase compared to eukaryotic UMP?CMP kinases ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.25 Escherichia coli P0A6I0
-
-
2.7.4.25 Escherichia coli K-12 P0A6I0 strain CJ236
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.25
-
Escherichia coli K-12

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.4.25 additional information
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.25 ATP + CMP
-
Escherichia coli ADP + CDP
-
r
2.7.4.25 ATP + CMP the enzyme is specific for CMP Escherichia coli K-12 ADP + CDP
-
?
2.7.4.25 ATP + dCMP
-
Escherichia coli ADP + dCDP
-
r
2.7.4.25 ATP + dCMP the enzyme is specific for dCMP Escherichia coli K-12 ADP + dCDP
-
?
2.7.4.25 ATP + UMP UMP is a poor substrate Escherichia coli ADP + UDP
-
r
2.7.4.25 ATP + UMP UMP is a weak substrate Escherichia coli K-12 ADP + UDP
-
?
2.7.4.25 additional information bacterial CMP kinases are specific for CMP and dCMP, whereas the related eukaryotic NMP kinase phosphorylates CMP and UMP with similar efficiency. Bacterial CMP kinase has a narrower NMP-binding pocket and a hydrogen-bonding network involving the pyrimidine moiety specific for the cytosine nucleobase compared to eukaryotic UMP?CMP kinases Escherichia coli ?
-
?
2.7.4.25 additional information four key amino acids interacting with the pyrimidine ring of CMP, Ser36, Asp132, Arg110 and Arg188, contribute to the stability, catalysis and substrate specificity of Escherichia coli CMP kinase. D132 is involved in a complicated network of interactions, the strongest being with R110, and also R110 is involved in many interactions, but mainly with D132. Substrate specificities of wild-type and mutant enzymes, overview Escherichia coli ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.25 CMP kinase
-
Escherichia coli
2.7.4.25 CMP kinase
-
Escherichia coli K-12

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.4.25 additional information
-
thermal stability of CMP kinase genetic variants, overview Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.4.25 0.013
-
UMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.04
-
dCMP mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.05
-
dCMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.054
-
UMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.06
-
dCMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.069
-
CMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.12
-
CMP mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.15
-
dCMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.23
-
CMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.45
-
UMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.57
-
UMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.73
-
dCMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.82
-
UMP wild-type enzyme Escherichia coli
2.7.4.25 0.82
-
UMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.4
-
CMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 4.1
-
CMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 8.3
-
UMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 9.9
-
UMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 14.5
-
dCMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 21.1
-
dCMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 22.4
-
CMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 63
-
CMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 103
-
CMP wild-type enzyme Escherichia coli
2.7.4.25 103
-
CMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 108
-
dCMP wild-type enzyme Escherichia coli
2.7.4.25 108
-
dCMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.25 ATP
-
Escherichia coli
2.7.4.25 ATP
-
Escherichia coli K-12

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.4.25 0.0033
-
UMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.0048
-
UMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.0068
-
dCMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.0114
-
CMP mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.052
-
dCMP mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.053
-
CMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.083
-
UMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.12
-
CMP mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.3
-
UMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.4
-
dCMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.54
-
CMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 0.88
-
UMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.04
-
UMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.1
-
dCMP mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.25
-
UMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.41
-
CMP mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1.88
-
dCMP mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 4.1
-
dCMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 25.2
-
CMP mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 230
-
dCMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 589
-
CMP mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 1150
-
dCMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12
2.7.4.25 2940
-
CMP wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C Escherichia coli K-12