Phosphorylation of 5 halogenated deoxycytidine analogues by deoxycytidine kinase

G. M. Cooper, S. Greer

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

The phosphorylation of 5 substituted deoxycytidine analogues by deoxycytidine kinase was studied in extracts of mouse and human lymphoid cells. The apparent Km for the phosphorylation of 5 bromodeoxycytidine in extracts of mouse lymphoma cells was 2.0 mM, in contrast to a Km of 10 μM for deoxycytidine phosphorylation. The apparent Km for the phosphorylation of 5 methyldeoxycytidine by the mouse enzyme was 80 μM. The affinity of mouse deoxycytidine kinase for 5 iododeoxycytidine was lower than for 5 bromodeoxycytidine, whereas its affinity for 5 fluorodeoxycytidine was similar to that for deoxycytidine. With human deoxycytidine kinase the apparent Km was 0.4 mM for 5 bromodeoxycytidine, as compared to 2.0 μM for deoxycytidine. These results suggest that the activity of deoxycytidine kinase is affected by the size of substitutions in position 5 of its substrate. This restricted substrate specificity of deoxycytidine kinase could limit the utilization of 5 bromodeoxycytidine for DNA synthesis.

Original languageEnglish (US)
Pages (from-to)704-710
Number of pages7
JournalMolecular Pharmacology
Volume9
Issue number6
StatePublished - Dec 1 1973

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology

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