Characterization of pyrimidine nucleoside monophosphokinase in normal and malignant tissues

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-doexyuridine 5'-monop...

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Bibliographic Details
Published in:Cancer research (Chicago, Ill.) Ill.), 1977-06, Vol.37 (6), p.1593-1597
Main Authors: Arima, T, Akiyoshi, H, Fujii, S
Format: Article
Language:English
Subjects:
Animals
Cytidine Monophosphate - metabolism
Deoxycytidine Monophosphate - metabolism
Deoxyribonucleotides - metabolism
In Vitro Techniques
Kinetics
Liver - enzymology
Male
Molecular Weight
Nucleoside-Phosphate Kinase - antagonists & inhibitors
Nucleoside-Phosphate Kinase - isolation & purification
Nucleoside-Phosphate Kinase - metabolism
Phosphotransferases - metabolism
Pyrimidine Nucleotides - metabolism
Rats
Sarcoma, Yoshida - enzymology
Thymidine Monophosphate - metabolism
Uracil Nucleotides
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Summary: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-doexyuridine 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 Km of 3.1 X 10(-5)M and dUMP with a Km of 7.7 X 10(-4) M. dTMP phosphorylation catalyzed by dTMP-dUMP kinase was inhibited competively by dUMP with a Ki of 2.0 X 10(-3) M. Similarly, phosphorylation of dUMP by this enzyme was inhibited competively by dTMP with a Ki of 2.5 X 10 (-5) M. CMP-dCMP-UMP-dUMP kinase of Yoshida sarcoma phosphorylated dUMP with a Km of 3.1 X 10(-3) M and dCMP with a Km 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 Ki's of 6.9 X 10(-4) and 3.0 X 10(-3) M, respectively, and phosphorylation of dCMP was inhibited completely by dUMP a Ki of 2.2 X 10(-3) M. Relative Vmax activity of this enzyme was 345 nmoles/mg protein with dCMP and 127 nmoles/mg protein with dUMP.
ISSN:0008-5472