Enzymology of mammalian phospholipases D: in vitro studies

The existence of multiple forms of phopholipase D was clearly established in a large number of biochemical studies that described and characterized the enzymological properties of the different PLD activities. This review summarizes the in vitro evidence showing differential subcellular localization...

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Bibliographic Details
Published in:Chemistry and physics of lipids 1996-05, Vol.80 (1), p.37-44
Main Authors: Liscovitch, Mordechai, Chalifa-Caspi, Vered
Format: Article
Language:English
Subjects:
Animals
Cell-Free System
Enzymology
Humans
In vitro studies
In Vitro Techniques
Isoenzymes
Isoenzymes - metabolism
Phospholipase D
Phospholipase D - metabolism
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Summary:The existence of multiple forms of phopholipase D was clearly established in a large number of biochemical studies that described and characterized the enzymological properties of the different PLD activities. This review summarizes the in vitro evidence showing differential subcellular localization and chromatographic properties of putative PLD isozymes, their phospholipid and alcohol substrate specificities, their modulation by various divalent cations, small G proteins and protein kinase c isozymes, and the role of phosphatidylinositol 4,5-bisphosphate as a cofactor of phospholipase D.
ISSN:0009-3084
1873-2941
DOI:10.1016/0009-3084(96)02544-3