Dihydrouracil dehydrogenase (NAD+)

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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PMCarticles
PubMedarticles
NCBIproteins

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

+ NAD+
 
 
 
H+
 
H+
 
 

The two substrates of this enzyme are dihydrouracil and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are the nucleotide base uracil, reduced NADH, and a proton. This enzyme can also utilise the alternative nucleotide base thymine to give dihydrothymine.[1][2] The enzyme is most often associated with the catabolism of these bases.[3]

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

  1. ^ Enzyme 1.3.1.1 at KEGG Pathway Database.
  2. ^ Campbell LL (August 1957). "Reductive degradation of pyrimidines. III. Purification and properties of dihydrouracil dehydrogenase". The Journal of Biological Chemistry. 227 (2): 693–700. doi:10.1016/S0021-9258(18)70749-7. PMID 13462991.
  3. ^ West, Thomas P. (2001). "Pyrimidine base catabolism in Pseudomonas putida biotype B". Antonie van Leeuwenhoek. 80 (2): 163–167. doi:10.1023/A:1012275512136. PMID 11759049.