来自马其顿假丝酵母的老黄色酶催化酮异佛尔酮C=C键的立体特异性还原反应。
Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=C bond of ketoisophorone.
作者信息
Kataoka Michihiko, Kotaka Atsushi, Hasegawa Akiko, Wada Masaru, Yoshizumi Ayumi, Nakamori Shigeru, Shimizu Sakayu
机构信息
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
出版信息
Biosci Biotechnol Biochem. 2002 Dec;66(12):2651-7. doi: 10.1271/bbb.66.2651.
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.
筛选能够还原3,5,5-三甲基-2-环己烯-1,4-二酮（氧代异佛尔酮；KIP）的微生物，发现了几株能产生(6R)-2,2,6-三甲基环己烷-1,4-二酮（左型异佛尔酮）的菌株。从马其顿假丝酵母AKU4588中分离出催化KIP的C=C键还原生成(6R)-左型异佛尔酮的酶。一级结构分析结果及其酶学性质表明，该酶可能是一种老黄酶家族蛋白。
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