Protein Engineering of α/β-Hydrolase Fold Enzymes

被引：88
作者：
Jochens, Helge [1 ]
Hesseler, Martin [1 ]
Stiba, Konstanze [1 ]
Padhi, Santosh Kumar [1 ]
Kazlauskas, Romas J. [2 ]
Bornscheuer, Uwe T. [1 ]
机构：
[1] Ernst Moritz Arndt Univ Greifswald, Inst Biochem, Dept Biotechnol & Enzyme Catalysis, D-17487 Greifswald, Germany
[2] Univ Minnesota, Dept Biochem Mol Biol & Biophys, St Paul, MN 55108 USA
来源：
CHEMBIOCHEM | 2011年 / 12卷 / 10期
基金：
美国国家科学基金会;
关键词：
3DM; alpha/beta hydrolase fold; directed evolution; divergent evolution; protein engineering; ITERATIVE SATURATION MUTAGENESIS; DIRECTED EVOLUTION; KINETIC RESOLUTION; TERTIARY ALCOHOLS; IMPROVED ENANTIOSELECTIVITY; CATALYTIC-ACTIVITY; EPOXIDE HYDROLASE; ESTERASE; LIPASE; MECHANISM;
D O I：
10.1002/cbic.201000771
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The superfamily of alpha/beta-hydrolase fold enzymes is one of the largest known protein families, including a broad range of synthetically useful enzymes such as lipases, esterases, amidases, hydroxynitrile lyases, epoxide hydrolases and dehalogenases. This minireview covers methods developed for efficient protein engineering of these enzymes. Special emphasis is placed on the alteration of enzyme properties such as substrate range, thermostability and enantioselectivity for their application in biocatalysis. In addition, concepts for the investigation of the evolutionary relationship between the different members of this protein superfamily are covered, together with successful examples.
引用
收藏
页码：1508 / 1517
页数：10
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