Department of Chemistry and Biochemistry and Department of Pharmacology, University of California, San Diego, La Jolla, California 92093-0601, USA.
J Biol Chem. 2013 Jan 18;288(3):1806-13. doi: 10.1074/jbc.R112.421909. Epub 2012 Dec 3.
The phospholipase A(2) (PLA(2)) superfamily consists of 16 groups and many subgroups and constitutes a diverse set of enzymes that have a common catalytic activity due to convergent evolution. However, different PLA(2) types have unique three-dimensional structures and catalytic residues as well as specific tissue localization and distinct biological functions. Understanding how the different PLA(2) enzymes associate with phospholipid membranes, specific phospholipid substrate molecules, and inhibitors on a molecular basis has advanced in recent years due to the introduction of hydrogen/deuterium exchange mass spectrometry. Its theory, practical considerations, and application to understanding PLA(2)/membrane interactions are addressed.
磷脂酶 A(2)（PLA(2)）超家族由 16 个组和许多亚组组成，构成了一组多样化的酶，由于趋同进化，这些酶具有共同的催化活性。然而，不同的 PLA(2)类型具有独特的三维结构和催化残基以及特定的组织定位和独特的生物学功能。近年来，由于引入了氢/氘交换质谱，不同的 PLA(2)酶如何在分子基础上与磷脂膜、特定的磷脂底物分子和抑制剂结合的机制得到了进一步的了解。本文介绍了氢/氘交换质谱的原理、实际考虑因素及其在理解 PLA(2)/膜相互作用方面的应用。
