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 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.
Liscovitch
M
M
Department of Biological Regulation, Weizmann Institute of Science, Rehovot, Israel. lhliscov@weizmann.weizmann.ac.il
Chalifa-Caspi
V
V
D000818:Animals; D002474:Cell-Free System; D006801:Humans; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism*; D010739:Phospholipase D / Q000378:metabolism*
D007527:Isoenzymes; D010739:Phospholipase D