Dihydropyrimidine dehydrogenase (NADP+)

In enzymology, a dihydropyrimidine dehydrogenase (NADP+) 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.

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