title: Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil.
abstract: The reductive pyrimidine catabolic pathway is absent in Escherichia coli. However, the bacterium contains an enzyme homologous to mammalian dihydropyrimidine dehydrogenase. Here, we show that E. coli dihydropyrimidine dehydrogenase is the first member of a novel NADH-dependent subclass of iron-sulfur flavoenzymes catalyzing the conversion of uracil to 5,6-dihydrouracil in vivo.
authors.affiliation: Institute for Chemical Research, Kyoto University, Kyoto 611-0011, Japan.
authors.forename: Ryota
authors.initials: R
authors.lastname: Hidese
authors.forename: Hisaaki
authors.initials: H
authors.lastname: Mihara
authors.forename: Tatsuo
authors.initials: T
authors.lastname: Kurihara
authors.forename: Nobuyoshi
authors.initials: N
authors.lastname: Esaki
mesh_terms: D042943:Dihydrouracil Dehydrogenase (NADP) / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry / Q000145:classification / Q000201:enzymology / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism*; D010802:Phylogeny; D014498:Uracil / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; C007419:dihydrouracil; D009243:NAD; D014498:Uracil; D042943:Dihydrouracil Dehydrogenase (NADP)