title: Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone.
abstract: Microorganisms were screened for ones that reduced 3,5,5-trimethyl-2-cyclohexene-1,4-dione (ketoisophorone; KIP), and several strains were found to produce (6R)-2,2,6-trimethylcyclohexane-1,4-dione (levodione). The enzyme catalyzing the reduction of the C=C bond of KIP to yield (6R)-levodione was isolated from Candida macedoniensis AKU4588. The results of primary structural analysis and its enzymatic properties suggested that the enzyme might be an Old Yellow Enzyme family protein.
authors.affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan. kataoka@kais.kyoto-u.ac.jp
authors.forename: Michihiko
authors.initials: M
authors.lastname: Kataoka
authors.forename: Atsushi
authors.initials: A
authors.lastname: Kotaka
authors.forename: Akiko
authors.initials: A
authors.lastname: Hasegawa
authors.forename: Masaru
authors.initials: M
authors.lastname: Wada
authors.forename: Ayumi
authors.initials: A
authors.lastname: Yoshizumi
authors.forename: Shigeru
authors.initials: S
authors.lastname: Nakamori
authors.forename: Sakayu
authors.initials: S
authors.lastname: Shimizu
mesh_terms: D000595:Amino Acid Sequence; D002175:Candida / Q000201:enzymology*; D003512:Cyclohexanones / Q000737:chemistry* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009252:NADPH Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction; D021122:Protein Subunits; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D003512:Cyclohexanones; D021122:Protein Subunits; C476259:ketoisophorone; C005940:isophorone; D009252:NADPH Dehydrogenase