Dihydrouracil dehydrogenase (NAD+)
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In enzymology, a dihydrouracil dehydrogenase (NAD+) (EC 1.3.1.1) is an enzyme that catalyzes the chemical reaction
- 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.
[edit] References
- IUBMB entry for 1.3.1.1
- BRENDA references for 1.3.1.1 (Recommended.)
- PubMed references for 1.3.1.1
- PubMed Central references for 1.3.1.1
- Google Scholar references for 1.3.1.1
- CAMPBELL LL Jr (1957). "Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase". J. Biol. Chem. 227: 693–700. PMID 13462991.
[edit] External links
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- The CAS registry number for this enzyme class is 9026-89-5.