Enantioselective acylation of primary and secondary alcohols catalyzed by lipase QL from Alcaligenes sp: A predictive active site model for lipase QL to identify which enantiomer of an alcohol reacts faster in this acylation
Enantioselective acylation of primary and secondary alcohols catalyzed by lipase QL from Alcaligenes sp: A predictive active site model for lipase QL to identify which enantiomer of an alcohol reacts faster in this acylation
复制标题
DOI：
10.1016/0957-4166(96)00429-6
复制
发表时间：
1996-11-01
影响因子：
--
通讯作者：
Tobe, Y
中科院分区：
文献类型：
--
作者：
Naemura, K;Murata, M;Tobe, Y
脂肪酶QL（来自产碱菌属）-在二异丙醚中使用乙酸异丙烯酯作为酰化剂的醇的催化酰化优先将具有S构型的伯醇和具有R构型的仲醇转化成相应的纯手性乙酸酯。观察到的对映异构体的选择性的基础上，脂肪酶QL的预测活性位点模型，提出了确定的对映异构体的伯醇或仲醇在此酰化反应更快。版权所有（C）1996 Elsevier Science Ltd
Lipase QL (from Alcaligenes sp.)-catalyzed acylation of alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether converted preferentially primary alcohols with an S configuration and secondary alcohols with an R configuration into the corresponding homochiral acetates. On the basis of observed enantiomer selectivities, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation. Copyright (C) 1996 Published by Elsevier Science Ltd