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Efficient, crosswise catalytic promiscuity among enzymes that catalyze phosphoryl transfer

机译:催化磷酰基转移的酶之间的高效,横向催化混杂

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摘要

The observation that one enzyme can accelerate several chemically distinct reactions was at one time surprising because the enormous efficiency of catalysis was often seen as inextricably linked to specialization for one reaction. Originally underreported, and considered a quirk rather than a fundamental property, enzyme promiscuity is now understood to be important as a springboard for adaptive evolution. Owing to the large number of promiscuous enzymes that have been identified over the last decade, and the increased appreciation for promiscuity's evolutionary importance, the focus of research has shifted to developing a better understanding of the mechanistic basis for promiscuity and the origins of tolerant or restrictive specificity. We review the evidence for widespread crosswise promiscuity amongst enzymes that catalyze phosphoryl transfer, including several members of the alkaline phosphatase superfamily, where large rate accelerations between 106 and 10 17 are observed for both native and multiple promiscuous reactions. This article is part of a Special Issue entitled: Chemistry and mechanism of phosphatases, diesterases and triesterases. ? 2012 Elsevier B.V. All rights reserved.
机译:一种酶可以促进几个化学上不同的反应的观察一次令人惊讶,因为通常认为巨大的催化效率与一种反应的专业化有着千丝万缕的联系。最初,酶含量不高,被认为是古怪而不是基本性质,现在酶的滥交被认为是适应性进化的重要跳板。由于过去十年中已发现大量混杂酶,以及对混杂的进化重要性的日益重视,研究的重点已转移到对混杂的机械基础以及耐受性或限制性起源的更好理解上特异性。我们审查了广泛的交叉混杂的证据之间的催化磷酰基转移的酶,包括碱性磷酸酶超家族的几个成员,其中天然和多重混杂反应观察到106和10 17之间的大速率加速。本文是名为“磷酸酶,二酯酶和三酯酶的化学与机理”的特刊的一部分。 ? 2012 Elsevier B.V.保留所有权利。

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