Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective

被引:1012
作者
Khersonsky, Olga [1 ]
Tawfik, Dan S. [1 ]
机构
[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
来源
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 79 | 2010年 / 79卷
关键词
enzyme mechanism; protein evolution; superfamilies; COLI ALKALINE-PHOSPHATASE; IN-VITRO EVOLUTION; MALONATE SEMIALDEHYDE DECARBOXYLASE; O-SUCCINYLBENZOATE SYNTHASE; ALLERGIC CROSS-REACTIONS; TRANSFER-RNA SYNTHETASE; DNP IGE ANTIBODY; DIRECTED EVOLUTION; CATALYTIC PROMISCUITY; ACTIVE-SITE;
D O I
10.1146/annurev-biochem-030409-143718
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
Many, if not most, enzymes can promiscuously catalyze reactions, or act on substrates, other than those for which they evolved. Here, we discuss the structural, mechanistic, and evolutionary implications of this manifestation of infidelity of molecular recognition. We define promiscuity and related phenomena and also address their generality and physiological implications. We discuss the mechanistic enzymology of promiscuity-how enzymes, which generally exert exquisite specificity, catalyze other, and sometimes barely related, reactions. Finally, we address the hypothesis that promiscuous enzymatic activities serve as evolutionary starting points and highlight the unique evolutionary features of promiscuous enzyme functions.
引用
收藏
页码:471 / 505
页数:35
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