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酶的多效性:进化与机制方面

Enzyme promiscuity: evolutionary and mechanistic aspects.

作者信息

Khersonsky Olga, Roodveldt Cintia, Tawfik Dan S

机构信息

Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.

出版信息

Curr Opin Chem Biol. 2006 Oct;10(5):498-508. doi: 10.1016/j.cbpa.2006.08.011. Epub 2006 Aug 30.

DOI:10.1016/j.cbpa.2006.08.011
PMID:16939713
Abstract

The past few years have seen significant advances in research related to the 'latent skills' of enzymes - namely, their capacity to promiscuously catalyze reactions other than the ones they evolved for. These advances regard (i) the mechanism of catalytic promiscuity - how enzymes, that generally exert exquisite specificity, promiscuously catalyze other, and sometimes barely related, reactions; (ii) the evolvability of promiscuous functions - namely, how latent activities evolve further, and in particular, how promiscuous activities can firstly evolve without severely compromising the original activity. These findings have interesting implications on our understanding of how new enzymes evolve. They support the key role of catalytic promiscuity in the natural history of enzymes, and suggest that today's enzymes diverged from ancestral proteins catalyzing a whole range of activities at low levels, to create families and superfamilies of potent and highly specialized enzymes.

摘要

在过去几年里,与酶的“潜在技能”相关的研究取得了重大进展,即酶能够杂乱地催化除其进化而来的反应之外的其他反应。这些进展涉及:(i)催化杂乱性的机制——通常具有高度特异性的酶如何杂乱地催化其他反应,有时甚至是几乎不相关的反应;(ii)杂乱功能的可进化性——即潜在活性如何进一步进化,特别是杂乱活性如何在不严重损害原始活性的情况下首先进化。这些发现对我们理解新酶如何进化具有有趣的启示。它们支持催化杂乱性在酶的自然历史中的关键作用,并表明当今的酶是从祖先蛋白质分化而来的,这些祖先蛋白质在低水平上催化一系列活动,从而形成了强大且高度专业化的酶家族和超家族。

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