Dihydropyrimidine dehydrogenase (NADP+)

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In enzymology, a dihydropyrimidine dehydrogenase (NADP+) (EC 1.3.1.2) is an enzyme that catalyzes the chemical reaction

5,6-dihydrouracil + NADP+ \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+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor.

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)
  • dihydrouracil dehydrogenase (NADP+)
  • DHU dehydrogenase
  • hydropyrimidine dehydrogenase
  • dihydropyrimidine dehydrogenase (NADP+)

This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis.

Contents

[edit] Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GT8, 1GTE, 1GTH, 1H7W, and 1H7X.

[edit] References

[edit] External links

The CAS registry number for this enzyme class is 9029-01-0.

[edit] Gene Ontology (GO) codes