酶催化中的模糊性。
Fuzziness in enzymatic catalysis.
作者信息
Katti Sachin S, Parikh Tvesha, Godek Rachel J, Page Rebecca, Peti Wolfgang
机构信息
Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030, USA.
Department of Cell Biology, University of Connecticut Health Center, Farmington, CT 06030, USA.
出版信息
Curr Opin Struct Biol. 2025 Jun 27;93:103106. doi: 10.1016/j.sbi.2025.103106.
Intrinsically disordered proteins/regions (IDPs/IDRs) frequently engage in dynamic charge:charge interactions, commonly referred to as 'fuzzy' interactions. These fuzzy interactions play critical roles in enzymatic regulation and substrate recruitment, especially for protein kinases and protein phosphatases. Here, we review recent advances that demonstrate how inter- and intramolecular fuzzy interactions among kinases and phosphatases and their cognate regulators and substrates allow for enzyme assembly, activation and substrate recruitment. We also highlight a unique mechanism of protein inhibition, where a protein phosphatase is inhibited by dynamic fuzzy interactions with its active site metals.
内在无序蛋白质/区域（IDPs/IDRs）经常参与动态电荷：电荷相互作用，通常被称为“模糊”相互作用。这些模糊相互作用在酶调节和底物招募中起着关键作用，特别是对于蛋白激酶和蛋白磷酸酶而言。在这里，我们综述了最近的进展，这些进展展示了激酶和磷酸酶与其同源调节因子和底物之间的分子间和分子内模糊相互作用如何实现酶的组装、激活和底物招募。我们还强调了一种独特的蛋白质抑制机制，即一种蛋白磷酸酶通过与其活性位点金属的动态模糊相互作用而受到抑制。
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