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Inhibition by CTP and UTP analogues of uridine kinase from mouse leukemic cells

1982; Wiley-VCH; Volume: 47; Issue: 12 Linguagem: Inglês

10.1135/cccc19823464

1212-6950

Jiří Veselý, Ivan Rosenberg, Antonı́n Holý,

Pneumocystis jirovecii pneumonia detection and treatment

The new phosphonate analogues of CTP and UTP (CTP c and UTP c ) inhibit the phosphorylation of uridine catalysed by uridine kinase in the presence of ATP and Mg 2+ -ions. The inhibition is competitive with respect to phosphate donor, and non-competitive with respect to phosphate acceptor. With respect to uridine the K i constants for CTP c and UTP c are 7.5 . 10 -5 mol l -1 and 1.0 . 10 -4 mol l -1 , respectively. With respect to ATP the K i value for CTP c (3.6 . 10 -6 mol l -1 ) is 3x lower than that for CTP. The novel analogues could be useful for further study of uridine kinase.