Dihydropyrimidine dehydrogenase (NADP+)

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Template:Cs1 config Template:Short description Template:Infobox enzyme

In enzymology, a dihydropyrimidine dehydrogenase (NADP+) (Template:EC number) is an enzyme that catalyzes the chemical reaction

5,6-dihydrouracil + NADP+ 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.[1][2] It is the initial and rate-limiting step in pyrimidine catabolism.Template:Citation needed It catalyzes the reduction of uracil and thymine.[3] It is also involved in the degradation of the chemotherapeutic drugs 5-fluorouracil and tegafur.[4] It also participates in beta-alanine metabolism and pantothenate and coa biosynthesis.

Terminology

The systematic name of this enzyme class is 5,6-dihydrouracil:NADP+ 5-oxidoreductase.
Other names in common use include:

  • dihydrothymine dehydrogenase
  • dihydrouracil dehydrogenase (NADP+)
  • 4,5-dihydrothymine: oxidoreductase
  • DPD
  • DHPDH
  • dehydrogenase, dihydrouracil (nicotinamide adenine dinucleotide, phosphate)
  • DHU dehydrogenase
  • hydropyrimidine dehydrogenase
  • dihydropyrimidine dehydrogenase (NADP+)

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, and Template:PDB link.

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.[2]

Interactive pathway map

Template:FluoropyrimidineActivity WP1601

See also

References

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Further reading

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  1. Template:Cite journal
  2. 2.0 2.1 Template:Cite web
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