Strategy and success for the directed evolution of enzymes

被引：144

作者：

Dalby, Paul A. ^{[1
]}

机构：

[1] UCL, Dept Biochem Engn, London WC1E 7JE, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2011年 / 21卷 / 04期

基金：

英国工程与自然科学研究理事会;

关键词：

IN-VITRO; SATURATION MUTAGENESIS; SUBSTRATE SPECIFICITIES; COMPUTATIONAL DESIGN; PROTEIN; STABILITY; MUTATIONS; DIVERSITY; ESTERASE; THERMOSTABILIZATION;

D O I：

10.1016/j.sbi.2011.05.003

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：

Directed evolution is widely used to improve enzymes, particularly for industrial biocatalytic processes. Molecular biology advances present many new strategies for directed evolution. Commonly used techniques have led to many successful examples of enzyme improvement, yet there is still a need to improve both the efficiency and capability of directed evolution. Recent strategies aimed at making directed evolution faster and more efficient take better advantage of available structural and sequence information. The underlying principles that lead to early dead-ends for directed evolution experiments are also discussed along with recent strategies designed to by-pass them. Several emerging methods for creating novel enzymes are also discussed including examples of catalytic activity for which there is no precedent in nature. Finally, the combined use of several strategies is likely to be required in practice to improve multiple target properties of an enzyme, as successfully shown by a recent industrial example.

引用

页码：473 / 480

页数：8

共 65 条

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