| (d)CMP kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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
- ^ 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
- (d)CMP+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| (d)CMP kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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
- ^ 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
- (d)CMP+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)