Dihydrouracil dehydrogenase (NAD+)

In enzymology, a dihydrouracil dehydrogenase (NAD+) (EC 1.3.1.1) is an enzyme that catalyzes the chemical reaction

dihydrouracil dehydrogenase (NAD+)
Identifiers
EC no.1.3.1.1
CAS no.9026-89-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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5,6-dihydrouracil + NAD+ uracil + NADH + H+

Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NAD+, whereas its 3 products are uracil, NADH, 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:NAD+ oxidoreductase. Other names in common use include dehydrogenase, dihydrouracil, dihydropyrimidine dehydrogenase, dihydrothymine dehydrogenase, pyrimidine reductase, thymine reductase, uracil reductase, and dihydrouracil dehydrogenase (NAD+). This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis.

References

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  • Campbell LL (August 1957). "Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase". The Journal of Biological Chemistry. 227 (2): 693–700. PMID 13462991.