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Merck
CN
  • 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
摘要

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.

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Sigma-Aldrich
异佛尔酮, 97%
Sigma-Aldrich
4-氧代异佛尔酮, ≥98%, FG
Sigma-Aldrich
异佛尔酮, ≥97%, FG
Sigma-Aldrich
2,6,6-三甲基-2-环己烯-1,4-二酮, 98%