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单价阳离子激活酶的分子机制。

Molecular Mechanisms of Enzyme Activation by Monovalent Cations.

作者信息

Gohara David W, Di Cera Enrico

机构信息

From the Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri 63104.

From the Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri 63104

出版信息

J Biol Chem. 2016 Sep 30;291(40):20840-20848. doi: 10.1074/jbc.R116.737833. Epub 2016 Jul 26.

Abstract

Regulation of enzymes through metal ion complexation is widespread in biology and underscores a physiological need for stability and high catalytic activity that likely predated proteins in the RNA world. In addition to divalent metals such as Ca, Mg, and Zn, monovalent cations often function as efficient and selective promoters of catalysis. Advances in structural biology unravel a rich repertoire of molecular mechanisms for enzyme activation by Na and K Strategies range from short-range effects mediated by direct participation in substrate binding, to more distributed effects that propagate long-range to catalytic residues. This review addresses general considerations and examples.

摘要

通过金属离子络合对酶进行调控在生物学中广泛存在,这突显了对稳定性和高催化活性的生理需求,这种需求在RNA世界中可能早于蛋白质就已存在。除了钙、镁和锌等二价金属外,单价阳离子通常也作为高效且具选择性的催化促进剂发挥作用。结构生物学的进展揭示了钠和钾激活酶的丰富分子机制。其策略涵盖从直接参与底物结合介导的短程效应,到远距离传播至催化残基的更分散效应。本文综述了一些一般性考量及实例。

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