Disease relevance of Uck1

• Properties of uridine-cytidine kinase derived from L1210 leukemia cells [1].

High impact information on Uck1

• Uridine-cytidine kinase was less inhibited in the presence of lowered UTP and CTP, which are potent feedback inhibitors of the enzyme, and enabled an enhanced formation of phosphorylated derivatives of 5-fluorouridine (FUrd) [2].
• Other properties of uridine-cytidine kinase were examined, and the apparent Michaelis constants for uridine, cytidine, and adenosine 5'-triphosphate were 23 x 10(-5) M, 15 x 10(-5) M, and 34.9 x 10(-5) M, respectively [1].
• Partially purified uridine-cytidine kinase catalyzes the initial phosphorylation of cyclopentenylcytosine with an apparent Km of 196 +/- 9 microM, and cyclopentenylcytosine is a competitive inhibitor of cytidine phosphorylation by this enzyme with a Ki value of 144 +/- 14 microM [3].
• By growth rate experiments, these uridine-cytidine kinase-deficient cell lines have altered sensitivities to the toxic pyrimidine analogs, 6-azauridine, 5-fluorouracil, and 5-fluorouridine and thus have been useful in elucidating the biochemical determinants involved in the metabolism of these compounds [4].
• Uridine-cytidine kinase. IV. Kinetics of the competition between 5-azacytidine and the two natural substrates [5].

Associations of Uck1 with chemical compounds

• Cyclopentenyluridine and cyclopentenylcytidine analogues as inhibitors of uridine-cytidine kinase [6].
• Uridine-cytidine kinase. III. Competition between uridine and cytidine for a single enzyme [7].

Analytical, diagnostic and therapeutic context of Uck1

• Uridine-cytidine kinase isolated from murine L1210 leukemia cells exist in several isozymic forms, as indicted by isoelectric focusing and by column chromatography on Sepharose 6B [1].

References