Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=Cbond of ketoisophorone
Old Yellow Enzyme from Candida macedoniensis catalyzes the stereospecific reduction of the C=Cbond of ketoisophorone
复制标题
来自马其顿念珠菌的老黄酶催化酮异佛尔酮 C=C 键的立体特异性还原
DOI：
10.1271/bbb.66.2651
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发表时间：
2002-12-01
影响因子：
1.6
通讯作者：
Shimizu, S
中科院分区：
文献类型：
--
作者：
Kataoka, M;Kotaka, A;Shimizu, S
对微生物进行了筛选，寻找还原 3,5,5-三甲基-2-环己烯-1,4-二酮（酮异佛尔酮；KIP）的微生物，并发现一些菌株可产生 (6R)-2,2,6-三甲基环己烷-1,4-二酮（左旋二酮）。从马其顿假丝酵母 AKU4588 中分离出催化 KIP C = C 键还原生成 (6R)-左旋二酮的酶。一级结构分析及其酶学性质的结果表明该酶可能是一种老黄酶家族蛋白。
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.