Uridine kinase

From Wikipedia, the free encyclopedia

In enzymology, an uridine kinase (EC 2.7.1.48) is an enzyme that catalyzes the chemical reaction

ATP + uridine $\rightleftharpoons$ ADP + UMP

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 2.7.1.48
BRENDA references for 2.7.1.48 (Recommended.)
PubMed references for 2.7.1.48
PubMed Central references for 2.7.1.48
Google Scholar references for 2.7.1.48
Orengo A (1969). "Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor". J. Biol. Chem. 244: 2204–9. PMID 5782006.
Skold O (1960). "Uridine kinase from Erlich ascites tumor: purification and properties". J. Biol. Chem. 235: 3273–3279.