Akashi T, Aoki T, Ayabe S
Department of Applied Biological Science, Nihon University, Kanagawa, Fujisawa, 252-8510, Japan.
Biochem Biophys Res Commun. 1998 Oct 9;251(1):67-70. doi: 10.1006/bbrc.1998.9414.
The microsome of yeast cells overexpressing CYP81E1, a cytochrome P450 cDNA recently cloned from licorice (Glycyrrhiza echinata L., Fabaceae), catalyzed the hydroxylation of isoflavones, daidzein and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. The chemical structures of the reaction products were confirmed by mass spectrometric analysis. Genistein also yielded a putative 2'-hydroxylated product, but flavanones and cinnamic acid derivatives were not used as substrates for the reaction with the recombinant yeast microsome. CYP81E1 protein was thus demonstrated for the first time to be isoflavone 2'-hydroxylase involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes.
最近从豆科植物甘草（Glycyrrhiza echinata L.）中克隆得到的细胞色素P450 cDNA CYP81E1在酵母细胞中过表达，其微粒体催化了异黄酮、大豆苷元和芒柄花黄素的羟基化反应，分别生成2'-羟基异黄酮、2'-羟基大豆苷元和2'-羟基芒柄花黄素。通过质谱分析确定了反应产物的化学结构。染料木黄酮也生成了一种假定的2'-羟基化产物，但黄烷酮和肉桂酸衍生物未被用作与重组酵母微粒体反应的底物。因此，首次证明CYP81E1蛋白是参与豆科植物异黄酮衍生抗菌化合物生物合成的异黄酮2'-羟化酶。
