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  • Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone.

Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone.

Bioscience, biotechnology, and biochemistry (2003-02-25)
Michihiko Kataoka, Atsushi Kotaka, Akiko Hasegawa, Masaru Wada, Ayumi Yoshizumi, Shigeru Nakamori, Sakayu Shimizu
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
2,6,6-Trimethyl-2-cyclohexene-1,4-dione, 98%
Sigma-Aldrich
4-Oxoisophorone, ≥98%, FG
Sigma-Aldrich
Isophorone, ≥97%, FG
Sigma-Aldrich
Isophorone, 97%