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- W12918740 abstract "Over the past decade, there has been increasing evidence of the importance of the pyrimidine catabolic pathway in regulating the metabolism of 5-fluorouracil (5-FU) and thus critically influencing the pharmacology of 5-FU and other fluoropyrimidine drugs (1). Dihydropyrimidine dehydrogenase or DPD (also known as, dihydrouracil dehydrogenase, dihydrothymine dehydrogenase, uracil reductase, E.C. 1.3.1.2) is the initial rate-limiting enzymatic step in the catabolism of not only the widely used antimetabolite cancer chemotherapy drug 5-FU but also the naturally occurring pyrimidines uracil and thymine (2–3). As shown in Fig. 1, DPD occupies an important position in the regulation of the metabolism of 5-FU, converting over 85% of a standard intravenous dose of administered 5-FU to dihydrofluorouracil (5-FUH2), an inactive metabolite, in an enzymatic step that physiologically is essentially irreversible (4,5). Although DPD is critical in regulating 5-FU metabolism, 5-FU cytotoxic action is dependent on the anabolism of 5-FU to the “active” nucleotides 5-fluorodeoxyuridine monophosphate (FdUMP), 5-fluorouridine triphosphate (FUTP), and 5-fluorodeoxyuridine triphosphate (FdUTP). These important “active” metabolites are, in turn, responsible for inhibition of cell replication through primarily inhibition of thymidylate synthase and secondarily through incorporation into RNA or DNA." @default.
- W12918740 created "2016-06-24" @default.
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- W12918740 date "2002-01-01" @default.
- W12918740 modified "2023-09-23" @default.
- W12918740 title "Clinical Implications of Dihydropyrimidine Dehydrogenase on 5-Fluorouracil Pharmacology" @default.
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- W12918740 doi "https://doi.org/10.1007/978-1-59259-160-2_26" @default.
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