Cytidylate kinase
cytidylate kinase | |||||||||
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Identifiers | |||||||||
EC number | 2.7.4.14 | ||||||||
CAS number | 37278-21-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a cytidylate kinase (EC 2.7.4.14) is an enzyme that catalyzes the chemical reaction
- ATP + (d)CMP ADP + (d)CDP
Thus, the two substrates of this enzyme are ATP and dCMP, whereas its two products are ADP and dCDP.
This enzyme belongs to the family of transferases, specifically those 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. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 17 structures have been solved for this class of enzymes, with PDB accession codes 1CKE, 1KDO, 1KDP, 1KDR, 1KDT, 1Q3T, 1QF9, 1TEV, 1UKE, 2CMK, 2FEM, 2FEO, 2H92, 2UKD, 3UKD, 4UKD, and 5UKD.
References
- Hurwitz J (1959). "The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material". J. Biol. Chem. 234: 2351–2358.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, p. 139-149.
- Ruffner BW Jr; Anderson EP (1969). "Adenosine triphosphate: uridine monophosphate-cytidine monophosphate phosphotransferase from Tetrahymena pyriformis". J. Biol. Chem. 244 (21): 5994–6002. PMID 5350952.