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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.