Uridine kinase
In enzymology, an uridine kinase (EC 2.7.1.48) is an enzyme that catalyzes the chemical reaction
- ATP + uridine ADP + UMP
| uridine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Uridine-cytidine kinase 2, tetramer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.48 | ||||||||
| CAS no. | 9026-39-5 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are ATP and uridine, whereas its two products are ADP and UMP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names in common use include pyrimidine ribonucleoside kinase, uridine-cytidine kinase, uridine kinase (phosphorylating), and uridine phosphokinase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1UDW, 1UEI, 1UEJ, 1UFQ, 1UJ2, 1XRJ, 2JEO, and 2UVQ.
References
- Orengo A (April 1969). "Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor". The Journal of Biological Chemistry. 244 (8): 2204–9. PMID 5782006.
- Skold O (1960). "Uridine kinase from Erlich ascites tumor: purification and properties". J. Biol. Chem. 235: 3273–3279.