Enzyme (re)design: lessons from natural evolution and computation

被引：98

作者：

Gerlt, John A. ^{[1
,2
]}

Babbitt, Patricia C. ^{[3
]}

机构：

[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

[3] Univ Calif San Francisco, Dept Biopharmaceut Sci, San Francisco, CA 94158 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2009年 / 13卷 / 01期

关键词：

OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE; SINGLE RESIDUE SWITCH; CATALYTIC PROMISCUITY; ACTIVE-SITE; DIVERGENT EVOLUTION; DIRECTED EVOLUTION; 5-MONOPHOSPHATE DECARBOXYLASE; ARYLMALONATE DECARBOXYLASE; ENOLASE SUPERFAMILY; SYNTHASE REACTION;

D O I：

10.1016/j.cbpa.2009.01.014

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 (re)design of enzymes to catalyze 'new' reactions is a topic of considerable practical and intellectual interest. Directed evolution (random mutagenesis followed by screening/selection) has been used widely to identify novel biocatalysts. However, 'rational' approaches using either natural divergent evolution or computational predictions based on chemical principles have been less successful. This review summarizes recent progress in evolution-based and computation-based (re)design.

引用

页码：10 / 18

页数：9

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