从葡萄酒酒球菌中纯化和表征一种具有 Prelog 醇立体选择性的醇脱氢酶，该酶能将 2-辛酮还原为 (R)-2-辛醇。

Purification and characterization of an anti-Prelog alcohol dehydrogenase from Oenococcus oeni that reduces 2-octanone to (R)-2-octanol.

机构信息

Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, 214122 Wuxi, Jiangsu, China.

出版信息

Biotechnol Lett. 2010 Apr;32(4):533-7. doi: 10.1007/s10529-009-0194-z. Epub 2009 Dec 25.

DOI:10.1007/s10529-009-0194-z

PMID:20035369

Abstract

An anti-Prelog alcohol dehydrogenase from Oenococcus oeni that reduces 2-octanone to (R)-2-octanol was purified by 26-fold to homogeneity. The enzyme had a homodimeric structure consisting of 49 kDa subunits, required NADPH, but not NADH, as a cofactor and was a Zn-independent short-chain dehydrogenase. Aliphatic methyl ketones (chain length > or =6 carbon atoms) and aromatic methyl ketones were the preferred substrates for the enzyme, the best being 2-octanone. Maximum enzyme activity with 2-octanone was at 45 degrees C and at pH 8.0.

摘要

从酒香酵母中纯化出一种反普雷洛格尔醇脱氢酶，它能将 2-辛酮还原为（R）-2-辛醇，酶比活提高了 26 倍，达到均一。该酶具有由 49 kDa 亚基组成的同源二聚体结构，需要 NADPH 作为辅酶，而不是 NADH，是一种 Zn 非依赖性的短链脱氢酶。脂肪族甲基酮（链长≥6 个碳原子）和芳香族甲基酮是该酶的首选底物，其中以 2-辛酮最佳。该酶对 2-辛酮的最大活性在 45°C 和 pH8.0 时。