Uridine kinase (EC 2.7.1.48) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from an ascites tumor and Escherichia coli converts uridine to uridine monophosphate and cytidine to cytidine monophosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The enzyme occurs widely, including in yeasts, humans and plants. This enzyme is a transferase, specifically one 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.
Structural studies As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1UDW, PDB: 1UEI, PDB: 1UEJ, PDB: 1UFQ, PDB: 1UJ2, PDB: 1XRJ, PDB: 2JEO, and PDB: 2UVQ.
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