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A distant evolutionary relationship between GPI‐specific phospholipase D and bacterial phosphatidylcholine‐preferring phospholipase C
Author(s) -
Rigden Daniel J
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.071
Subject(s) - phospholipase d , dictyostelium discoideum , phospholipase , phosphatidylcholine , yeast , microbiology and biotechnology , chemistry , cell , organelle , biochemistry , cell membrane , biology , signal transduction , membrane , enzyme , gene , phospholipid
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 Dictyostelium discoideum .