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ⓘ Dihydropyrimidine dehydrogenase, NADP+. In enzymology, a dihydropyrimidine dehydrogenase is an enzyme that catalyzes the chemical reaction 5.6-dihydrouracil + N ..



Dihydropyrimidine dehydrogenase (NADP+)
                                     

ⓘ Dihydropyrimidine dehydrogenase (NADP+)

In enzymology, a dihydropyrimidine dehydrogenase is an enzyme that catalyzes the chemical reaction

5.6-dihydrouracil + NADP + ⇌ {\displaystyle \rightleftharpoons } uracil + NADPH + H +

Thus, the two substrates of this enzyme are 5.6-dihydrouracil and NADP +, whereas its 3 products are uracil, NADPH, and H +.

In humans the enzyme is encoded by the DPYD gene. It is the initial and rate-limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine. It is also involved in the degradation of the chemotherapeutic drugs 5-fluorouracil and tegafur. It also participates in beta-alanine metabolism and pantothenate and coa biosynthesis.

                                     

1. Terminology

The systematic name of this enzyme class is 5.6-dihydrouracil:NADP+ 5-oxidoreductase. Other names in common use include:

  • dehydrogenase, dihydrouracil nicotinamide adenine dinucleotide, phosphate
  • dihydrothymine dehydrogenase
  • dihydrouracil dehydrogenase NADP+
  • hydropyrimidine dehydrogenase
  • 4.5-dihydrothymine: oxidoreductase
  • DHPDH
  • DHU dehydrogenase
  • DPD
  • dihydropyrimidine dehydrogenase NADP+
                                     

2. Function

The protein is a pyrimidine catabolic enzyme and the initial and rate-limiting factor in the pathway of uracil and thymidine catabolism. Genetic deficiency of this enzyme results in an error in pyrimidine metabolism associated with thymine-uraciluria and an increased risk of toxicity in cancer patients receiving 5-fluorouracil chemotherapy.

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