EC 2.7.4.25 - (d)CMP kinase

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IntEnz Enzyme Nomenclature
EC 2.7.4.25

Names

Accepted name:
(d)CMP kinase
Other names:
prokaryotic cytidylate kinase
deoxycytidylate kinase [misleading]
dCMP kinase [misleading]
deoxycytidine monophosphokinase [misleading]
Systematic name:
ATP:(d)CMP phosphotransferase

Reaction

Comments:

The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP [1].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (567) [show] [UniProt]

References

  1. 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.
    J. Mol. Biol. 315 : 1099-1110 (2002). [PMID: 11827479]
  2. Thum, C., Schneider, C. Z., Palma, M. S., Santos, D. S., Basso, L. A.
    The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP.
    J. Bacteriol. 191 : 2884-2887 (2009). [PMID: 19181797]

[EC 2.7.4.25 created 2010]