血小板活化因子乙酰水解酶的结构与功能
The structure and function of platelet-activating factor acetylhydrolases.
作者信息
Derewenda Z S, Derewenda U
机构信息
Department of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville 22906-0011, USA.
出版信息
Cell Mol Life Sci. 1998 May;54(5):446-55. doi: 10.1007/s000180050172.
Platelet-activating factor acetylhydrolases (PAF-AHs, EC 3.1.1.47) constitute a unique and biologically important family of phospholipase A2s. They are related to neither the well-characterized secretory nor cytosolic PLA2s, and unlike them do not require Ca2+ for catalytic activity. The distinguishing property of PAF-AHs is their unique substrate specificity: they act on the phospholipid platelet-activating factor (PAF), and in some cases on proinflammatory polar phospholipids, from which they remove a short acyl moiety--acetyl in the case of PAF--located at the sn-2 position. Because PAF is found both in the plasma and in the cytosol of many tissues, PAF-acetylhydrolases are equally widely distributed in an animal organism. Recent crystallographic studies shed new light on the complex structure-function relationships in PAF-AHs.
血小板活化因子乙酰水解酶（PAF-AHs，EC 3.1.1.47）构成了一个独特且具有重要生物学意义的磷脂酶A2家族。它们既与特征明确的分泌型磷脂酶A2无关，也与胞质型磷脂酶A2无关，并且与它们不同的是，催化活性不需要Ca2+。PAF-AHs的显著特性是其独特的底物特异性：它们作用于磷脂血小板活化因子（PAF），在某些情况下还作用于促炎极性磷脂，从中去除位于sn-2位的短酰基部分——PAF的情况下是乙酰基。由于PAF存在于许多组织的血浆和胞质溶胶中，PAF-乙酰水解酶在动物机体中同样广泛分布。最近的晶体学研究为PAF-AHs复杂的结构-功能关系提供了新的线索。
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