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Characterization of Pyrimidine Nucleoside Monophosphokinase in Normal and Malignant Tissues¹

Department of Enzyme Physiology, Institute for Enzyme Research, School of Medicine, Tokushima University, Tokushima 770, Japan

It was found that there are two kinds of pyrimidine nucleoside, monophosphokinase deoxythymidine 5'-monophosphate-deoxyuridine 5'-monophosphate (dTMP-dUMP) kinase and cytidine 5'-monophosphate-deoxycytidine 5'-monophosphate-uridine 5'-monophosphate-deoxyuridine 5'-monophosphate (CMP-dCMP-UMP-dUMP) kinase, and their molecular weights were calculated to be 46,000 and 26,000, respectively, by gel filtration.

dTMP-dUMP kinase phosphorylated dTMP with a K_m of 3.1 x 10^-5 M and dUMP with a K_m of 7.7 x 10^-4 M. dTMP phosphorylation catalyzed by dTMP-dUMP kinase was inhibited competitively by dUMP with a K_i of 2.0 x 10^-3 M. Similarly, phosphorylation of dUMP by this enzyme was inhibited competitively by dTMP with a K_i of 2.5 x 10^-5 M. CMP-dCMP-UMP-dUMP kinase of Yoshida sarcoma phosphorylated dUMP with a K_m of 3.1 x 10^-3 M and dCMP with a K_m of 7.1 x 10^-4 M, but it did not phosphorylate dTMP. Phosphorylation of dUMP by CMP-dCMP-UMP-dUMP kinase was inhibited competitively by dCMP and dTMP with K_i's of 6.9 x 10^-4 and 3.0 x 10^-3 M, respectively, and phosphorylation of dCMP was inhibited competitively by dUMP with a K_i of 2.2 x 10^-3 M. Relative V_max activity of this enzyme was 345 nmoles/mg protein with dCMP and 127 nmoles/mg protein with dUMP.

¹ This work was supported in part by grants-in-aid for cancer research from the Ministry of Education, Science and Culture, Japan.

² Present address: Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan.

Received 10/13/75. Accepted 1/18/77.

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