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Substrate specificity of Escherichia coli thymidine phosphorylase for pyrimidine nucleosides with anti-human
R F Schinazi1, A Peck, J P Sommadossi
1Veterans Affairs Medical Center, Decatur, GA 30033.
Biochemical Pharmacology
|July 22, 1992
Abstract:
Various nucleoside antiviral agents and their metabolites were examined for their ability to be cleaved across the glycosidic bond by Escherichia coli thymidine phosphorylase. The increasing order of susceptibility to cleavage was U greater than T much greater than C derivatives. Nucleosides that were unsaturated in the sugar moiety were more susceptible than saturated ones. 3'-Deoxy-2',3'-didehydrothymidine was a substrate, whereas 3'-azido-, 3'-fluoro-, 3'-oxo- and 3'-thiapyrimidine nucleosides were resistant to this enzyme.