Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone.
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.
Kataoka
Michihiko
M
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan. kataoka@kais.kyoto-u.ac.jp
Kotaka
Atsushi
A
Hasegawa
Akiko
A
Wada
Masaru
M
Yoshizumi
Ayumi
A
Nakamori
Shigeru
S
Shimizu
Sakayu
S
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
D003512:Cyclohexanones; D021122:Protein Subunits; C476259:ketoisophorone; C005940:isophorone; D009252:NADPH Dehydrogenase