Biology:(d)CMP kinase
From HandWiki
Short description: Class of enzymes
| (d)CMP kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.4.25 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| 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][2] This enzyme catalyses the following chemical reaction
- ATP + (d)CMP ADP + (d)CDP
The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP).
References
- ↑ "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. February 2002. doi:10.1006/jmbi.2001.5286. PMID 11827479.
- ↑ "The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP". Journal of Bacteriology 191 (8): 2884–7. April 2009. doi:10.1128/jb.01337-08. PMID 19181797.
External links
- (d)CMP+kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
 |  |
