Erxleben Andrea
School of Chemistry, National University of Ireland Galway, Galway, Ireland.
Front Chem. 2019 Feb 21;7:82. doi: 10.3389/fchem.2019.00082. eCollection 2019.
Phosphoesterases hydrolyze the phosphorus oxygen bond of phosphomono-, di- or triesters and are involved in various important biological processes. Carboxylate and/or hydroxido-bridged dizinc(II) sites are a widespread structural motif in this enzyme class. Much effort has been invested to unravel the mechanistic features that provide the enormous rate accelerations observed for enzymatic phosphate ester hydrolysis and much has been learned by using simple low-molecular-weight model systems for the biological dizinc(II) sites. This review summarizes the knowledge and mechanistic understanding of phosphoesterases that has been gained from biomimetic dizinc(II) complexes, showing the power as well as the limitations of model studies.
磷酸酯酶可水解磷酸单酯、二酯或三酯的磷氧键，并参与各种重要的生物过程。羧酸根和/或羟基桥联的二锌（II）位点是这类酶中广泛存在的结构基序。人们投入了大量精力来揭示那些为酶促磷酸酯水解所观察到的巨大速率加速提供支持的机制特征，并且通过使用针对生物二锌（II）位点的简单低分子量模型系统已经了解到了很多信息。本综述总结了从仿生二锌（II）配合物中获得的关于磷酸酯酶的知识和机制理解，展示了模型研究的作用以及局限性。
