title: Structure of porcine aldehyde reductase holoenzyme.
abstract: Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. The structure of porcine aldehyde reductase-NADPH binary complex has been determined by x-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 A resolution. The tertiary structure of aldehyde reductase is similar to that of aldose reductase and consists of an alpha/beta-barrel with the active site located at the carboxy terminus of the strands of the barrel. Unlike aldose reductase, the N epsilon 2 of the imidazole ring of His 113 in aldehyde reductase interacts, through a hydrogen bond, with the amide group of the nicotinamide ring of NADPH.
authors.affiliation: University of Alabama at Birmingham, Center for Macromolecular Crystallography 35294-0005, USA.
authors.forename: O
authors.initials: O
authors.lastname: el-Kabbani
authors.forename: K
authors.initials: K
authors.lastname: Judge
authors.forename: S L
authors.initials: SL
authors.lastname: Ginell
authors.forename: D A
authors.initials: DA
authors.lastname: Myles
authors.forename: L J
authors.initials: LJ
authors.lastname: DeLucas
authors.forename: T G
authors.initials: TG
authors.lastname: Flynn
mesh_terms: D000449:Aldehyde Reductase / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray / Q000379:methods; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D017354:Point Mutation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013552:Swine
chemical_list: D011994:Recombinant Proteins; D009249:NADP; D000449:Aldehyde Reductase