(d)CMP kinase
| (d)CMP kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.25 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
(d)CMP kinase (EC 2.7.4.25, prokaryotic cytidylate kinase, deoxycytidylate kinase, dCMP kinase, deoxycytidine monophosphokinase) is an enzyme with systematic name ATP:(d)CMP phosphotransferase.[1] It catalyses two related chemical reactions. The first converts the nucleotide, cytidine monophosphate (CMP), to cytidine diphosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP):[2]
Alternatively, the enzyme can act on deoxycytidine monophosphate (dCMP):[3]
This prokaryotic enzyme is specific for CMP or dCMP.[2]
References
[edit]- ↑ Enzyme 2.7.4.25 at KEGG Pathway Database.
- 1 2 Bertrand T, Briozzo P, Assairi L, Ofiteru A, Bucurenci N, Munier-Lehmann H, Golinelli-Pimpaneau B, Bârzu O, Gilles AM (February 2002). "Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme". Journal of Molecular Biology. 315 (5): 1099–110. doi:10.1006/jmbi.2001.5286. PMID 11827479.
- ↑ Thum C, Schneider CZ, Palma MS, Santos DS, Basso LA (April 2009). "The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP". Journal of Bacteriology. 191 (8): 2884–7. doi:10.1128/jb.01337-08. PMC 2668428. PMID 19181797.
External links
[edit]- (d)CMP+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
