Challenges in the directed evolution of stereoselective enzymes for use in organic chemistry

被引：13

作者：

Reetz, M. T. ^{[1
]}

Krebs, G. P. L. ^{[1
]}

机构：

[1] Max Planck Inst Kohlenforsch, D-45470 Mulheim, Germany

来源：

COMPTES RENDUS CHIMIE | 2011年 / 14卷 / 09期

关键词：

Asymmetric; Catalysis; Biocatalysis; Directed evolution; Enantioselectivity; Enzymes; ITERATIVE SATURATION MUTAGENESIS; BAEYER-VILLIGER MONOOXYGENASE; LABORATORY EVOLUTION; EPOXIDE HYDROLASE; THEORETICAL INVESTIGATIONS; ENANTIOSELECTIVE ENZYMES; COOPERATIVE MUTATIONS; SUBSTRATE ACCEPTANCE; KINETIC RESOLUTION; CATALYSIS;

D O I：

10.1016/j.crci.2011.02.002

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Directed evolution constitutes an ideal method for engineering essentially any catalytic parameter of enzymes for application in synthetic organic chemistry and biotechnology, including thermostability, substrate scope and enantioselectivity. Stereoselectivity is especially important when applying biocatalysts to synthetic organic chemistry. This article focuses on recent methodology developments in laboratory evolution of stereoselective enzymes, hydrolases and monooxygenases serving as the enzymes. Iterative saturation mutagenesis (ISM) has been developed as an unusually effective method to evolve enhanced or reversed enantioselectivity, broader substrate scope and/or higher thermostability of enzymes. (C) 2011 Published by Elsevier Masson SAS on behalf of Academie des sciences.

引用

页码：811 / 818

页数：8

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