Collect. Czech. Chem. Commun.
1983, 48, 1783-1787
https://doi.org/10.1135/cccc19831783
Donor activity of 5'-O-phosphonylmethyl analogues of ATP and GTP in the phosphorylation of uridine catalyzed by uridine kinase from mouse leukemic cells
Jiří Veselý, Ivan Rosenberg and Antonín Holý
Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6
Abstract
The phosphonate analogues of ATP and GTP can function as phosphate donors in uridine kinase reaction. The Km constants for ATP and its analogue ATPc (I) are identical, the Vmax value for ATP is five times higher than that for ATPc. Also the Vmax constants with respect to uridine follow the same pattern (250 nmol for ATP, 35.7 nmol for ATPc). The optimum Mg2+ concentration for the phosphonate is 3 times higher compared with ATP.
