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

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Abstract
The new phosphonate analogues of CTP and UTP (CTPc and UTPc) inhibit the phosphorylation of uridine catalysed by uridine kinase in the presence of ATP and Mg2+-ions. The inhibition is competitive with respect to phosphate donor, and non-competitive with respect to phosphate acceptor. With respect to uridine the Ki constants for CTPc and UTPc are 7.5 . 10-5 mol l-1 and 1.0 . 10-4 mol l-1, respectively. With respect to ATP the Ki value for CTPc (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.