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• W1997435698 abstract "Lactobacillus casei cells grown on excess thymine or on folic acid contained low levels of thymidine phosphorylase. On the other hand, thymine starved cells and also cells of a thymidine-monophosphate-kinase-defective mutant grown on excess thymine, possessed derepressed levels. These results suggest that the synthesis of thymidine phosphorylase is regulated by the end product of the thymidine-triphosphate-biosynthetic pathway. L. casei cells lacked 2-deoxyribose-1-phosphate-mutase activity and did not grow on 2-deoxyribose or thymidine as the sole-carbon source. Growth in the presence of thymidine did not result in induction of thymidine-phosphorylase synthesis, probably due to the inability of the cell to convert it to 2-deoxyribose-5-phosphate, which is known to act as an inducer in E. coli cells. Thymidine triphosphate inhibited non-competitively the activity of thymidine phosphorylase. It was also inhibited by dihydrofolic acid." @default.
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• W1997435698 date "1991-08-01" @default.
• W1997435698 modified "2023-09-28" @default.
• W1997435698 title "Regulation of the synthesis and activity of thymidine phosphorylase inLactobacillus casei" @default.
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• W1997435698 doi "https://doi.org/10.1111/j.1574-6968.1991.tb04896.x" @default.
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