Dihydropyrimidine dehydrogenase (NADP+)

Dihydropyrimidine dehydrogenase (NADP+)
dihydropyrimidine dehydrogenase (NADP+)
Identifiers
EC number 1.3.1.2
CAS number 9029-01-0
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 dihydropyrimidine dehydrogenase (NADP+) (EC 1.3.1.2) 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)
  • 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 1GT8, 1GTE, 1GTH, 1H7W, and 1H7X.

References

  • FRITZSON P (1960). "Properties and assay of dihydrouracil dehydrogenase of rat liver". J. Biol. Chem. 235: 719–25. PMID 13825299. 
  • Shiotani T, Weber G (1981). "Purification and properties of dihydrothymine dehydrogenase from rat liver". J. Biol. Chem. 256 (1): 219–24. PMID 7451435. 
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