Cytidylate kinase
| Cytidylate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.14 | ||||||||
| CAS no. | 37278-21-0 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Cytidylate kinase (EC 2.7.4.14) is an enzyme that catalyzes three related chemical reactions. In the first, cytidine monophosphate (CMP) is converted to cytidine diphosphate when a phosphate group is transferred from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP):[1][2]
The enzyme can also convert the deoxynucleotide, deoxycytidine monophosphate (dCMP) to the corresponding dCDP and it also acts on uridine monophosphate:[3]
The enzyme has been found in Tetrahymena pyriformis,[3] Escherichia coli,[4] Arabidopsis thaliana,[4] Dictyostelium discoideum,[5] and humans.[6]
Nomenclature
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:CMP phosphotransferase. Other names in common use include: deoxycytidylate kinase, deoxycytidylate kinase, CMP kinase, CTP:CMP phosphotransferase, dCMP kinase, deoxycytidine monophosphokinase, UMP-CMP kinase, ATP:UMP-CMP phosphotransferase, and pyrimidine nucleoside monophosphate kinase.[7]
References
- ↑ Hurwitz, Jerard (1959). "The Enzymatic Incorporation of Ribonucleotides into Polydeoxynucleotide Material". Journal of Biological Chemistry. 234 (9): 2351–2358. doi:10.1016/S0021-9258(18)69813-8.
- ↑ Boyer PD, Lardy H, Myrback K, eds. (1962). The Enzymes. Vol. 6 (2nd ed.). New York: Academic Press. pp. 139–149.
- 1 2 Ruffner, B.W.; Anderson, E.P. (1969). "Adenosine Triphosphate: Uridine Monophosphate-Cytidine Monophosphate Phosphotransferase from Tetrahymena pyriformis". Journal of Biological Chemistry. 244 (21): 5994–6002. doi:10.1016/S0021-9258(18)63571-9. PMID 5350952.
- 1 2 Zhou, Lan; Lacroute, François; Thornburg, Robert (1998). "Cloning, Expression in Escherichia coli , and Characterization of Arabidopsis thaliana UMP/CMP Kinase1". Plant Physiology. 117 (1): 245–254. doi:10.1104/pp.117.1.245. PMC 35009. PMID 9576794.
- ↑ Scheffzek, Klaus; Kliche, Werner; Wiesmüller, Lisa; Reinstein, Jochen (1996). "Crystal Structure of the Complex of UMP/CMP Kinase from Dictyostelium discoideum and the Bisubstrate Inhibitor P 1-(5'-Adenosyl) P 5-(5'-Uridyl) Pentaphosphate (UP5A) and Mg2+ at 2.2 Å: Implications for Water-Mediated Specificity". Biochemistry. 35 (30): 9716–9727. doi:10.1021/bi960642s. PMID 8703943.
- ↑ Van Rompay, An R.; Johansson, Magnus; Karlsson, Anna (1999). "Phosphorylation of Deoxycytidine Analog Monophosphates by UMP-CMP Kinase: Molecular Characterization of the Human Enzyme". Molecular Pharmacology. 56 (3): 562–569. doi:10.1124/mol.56.3.562. PMID 10462544.
- ↑ Enzyme 2.7.4.14 at KEGG Pathway Database.