title: Ketopantoyl lactone reductase is a conjugated polyketone reductase.
abstract: Ketopantoyl lactone reductase (EC 1.1.1.168) of Saccharomyces cerevisiae was found to catalyze the reduction of a variety of natural and unnatural conjugated polyketone compounds and quinones, such as isatin, ninhydrin, camphorquinone and beta-naphthoquinone in the presence of NADPH. 5-Bromoisatin is the best substrate for the enzyme (Km = 3.1 mM; Vmax = 650 mumol/min/mg). The enzyme is inhibited by quercetin, and several polyketones. These results suggest that ketopantoyl lactone reductase is a carbonyl reductase which specifically catalyzes the reduction of conjugated polyketones.
authors.affiliation: Department of Agricultural Chemistry, Kyoto University, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Hata
authors.forename: S
authors.initials: S
authors.lastname: Shimizu
authors.forename: S
authors.initials: S
authors.lastname: Hattori
authors.forename: H
authors.initials: H
authors.lastname: Yamada
mesh_terms: D000429:Alcohol Oxidoreductases / Q000145:classification*; D007659:Ketones / Q000378:metabolism*; D009089:Mucor / Q000201:enzymology; D010084:Oxidation-Reduction; D013379:Substrate Specificity
chemical_list: D007659:Ketones; D000429:Alcohol Oxidoreductases; C021935:2-oxopantoyl lactone reductase