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Literature summary extracted from

  • Bertrand, T.; Briozzo, P.; Assairi, L.; Ofiteru, A.; Bucurenci, N.; Munier-Lehmann, H.; Golinelli-Pimpaneau, B.; Barzu, O.; Gilles, A.M.
    Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme (2002), J. Mol. Biol., 315, 1099-1110.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.25 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.4.25 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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.4.25 D185A the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme Escherichia coli
2.7.4.25 R181M the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme Escherichia coli
2.7.4.25 S101A the mutation reduces CMP phosphorylation only moderately, but dramatically reduces dCMP phosphorylation Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.25 0.035
-
 CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.08
-
 CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.094
-
 dCMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.15
-
 2',3'-dideoxy-CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.19
-
 CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.19
-
 dCMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.24
-
 dCMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.24
-
 dCMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.46
-
 2',3'-dideoxy-CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.47
-
 CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.47
-
 ara-CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.53
-
 ara-CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.54
-
 2',3'-dideoxy-CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.65
-
 2',3'-dideoxy-CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.79
-
 ara-CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 1
-
 ara-CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli

Metals/Ions

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

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
-
 ?
2.7.4.25 ATP + dCMP Escherichia coli Escherichia coli CMPK phosphorylates dCMP nearly as well as it does CMP ADP + dCDP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.25 Escherichia coli A0A140N8S7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.25 Ni-NTA column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.25 ATP + 2',3'-dideoxy-CMP 2’,3’-dideoxy-CMP is a poor substrate Escherichia coli ADP + ?
-
 ?
2.7.4.25 ATP + ara-CMP ara-CMP is a poor substrate Escherichia coli ADP + ara-CDP
-
 ?
2.7.4.25 ATP + CMP
-
 Escherichia coli ADP + CDP
-
 ?
2.7.4.25 ATP + dCMP Escherichia coli CMPK phosphorylates dCMP nearly as well as it does CMP Escherichia coli ADP + dCDP
-
 ?
2.7.4.25 ATP + UMP bacterial CMP kinases phosphorylate UMP with very low rates Escherichia coli ADP + UDP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.25 CMP kinase
-
 Escherichia coli
2.7.4.25 CMPK
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.4.25 52
-
 the melting temperature of the wild type enzyme is at 52°C 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 0.0083
-
 2',3'-dideoxy-CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.047
-
 2',3'-dideoxy-CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.071
-
 dCMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.08
-
 CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.085
-
 ara-CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.12
-
 2',3'-dideoxy-CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.19
-
 dCMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.26
-
 CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.45
-
 dCMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.47
-
 ara-CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 0.65
-
 2',3'-dideoxy-CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 1.36
-
 ara-CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 1.38
-
 CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 56
-
 ara-CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 103
-
 CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli
2.7.4.25 109
-
 dCMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.25 ATP
-
 Escherichia coli

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 0.083
-
 ara-CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 0.3
-
 dCMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 0.54
-
 CMP mutant enzyme D185A, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 1.7
-
 ara-CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 1.9
-
 dCMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 6.1
-
 dCMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 7.4
-
 CMP mutant enzyme R181M, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 7.5
-
 ara-CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 105
-
 ara-CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 697
-
 CMP mutant enzyme S101A, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 1160
-
 dCMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli K-12
2.7.4.25 2940
-
 CMP wild type enzyme, at 30°C and pH 7.4 Escherichia coli K-12