A distant evolutionary relationship between GPI-specific phospholipase D and bacterial phosphatidylcholine-preferring phospholipase C

被引：5

作者：

Rigden, DJ ^{[1
]}

机构：

[1] Univ Liverpool, Sch Biol Sci, Liverpool L69 7ZB, Merseyside, England

来源：

FEBS LETTERS | 2004年 / 569卷 / 1-3期

关键词：

glycosylphosphatidylinositol anchor; phospholipase D; distant homology; molecular modelling; trimetal catalytic site;

D O I：

10.1016/j.febslet.2004.05.071

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In eukaryotes some surface proteins are attached to the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. A GPI-specific phospholipase D (GPI-PLD) activity has been characterized and implicated in the regulation of anchoring, thereby influencing the dispersal of anchored proteins or their maintenance on the cell surface, and possibly in cell signalling. Despite its biological and medical importance, little is known of the structure of GPI-PLD. Here, a distant relationship between the catalytic domains of GPI-PLD and some bacterial phospholipases C is demonstrated. A model of the GPI-PLD catalytic site sheds light on catalysis and highlights possibilities for design of improved and more specific GPI-PLD inhibitors. The databases contain hitherto unnoticed close homologues of GPI-PLD from yeast and Dictyostefium discoideum. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：229 / 234

页数：6

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