Old Yellow Enzyme from Candida macedoniensis Catalyzes the Stereospecific Reduction of the C=C Bond of Ketoisophorone

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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. © 2002 by Japan Society for Bioscience, Biotechnology, and Agrochemistry.

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Kataoka, M., Kotaka, A., Hasegawa, A., Wada, M., Yoshizumi, A., Nakamori, S., & Shimizu, S. (2002). Old Yellow Enzyme from Candida macedoniensis Catalyzes the Stereospecific Reduction of the C=C Bond of Ketoisophorone. Bioscience, Biotechnology and Biochemistry, 66(12), 2651–2657. https://doi.org/10.1271/bbb.66.2651

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