Enzymology of mammalian phospholipases D: in vitro studies

Mordechai Liscovitch, Vered Chalifa-Caspi

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


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.

Original languageEnglish
Pages (from-to)37-44
Number of pages8
JournalChemistry and Physics of Lipids
Issue number1-2
StatePublished - 24 May 1996
Externally publishedYes


  • Enzymology
  • In vitro studies
  • Isoenzymes
  • Phospholipase D

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Cell Biology


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