Dihydrouracil dehydrogenase (NAD+)

From Wikipedia, the free encyclopedia
Jump to: navigation, search
dihydrouracil dehydrogenase (NAD+)
Identifiers
EC number 1.3.1.1
CAS number 9026-89-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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

5,6-dihydrouracil + NAD+ \rightleftharpoons 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[edit]

  • CAMPBELL LL Jr (1957). "Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase". J. Biol. Chem. 227 (2): 693–700. PMID 13462991.