Enzymology of mammalian phospholipases D: in vitro studies

Mordechai Liscovitch; Vered Chalifa-Caspi

doi:10.1016/0009-3084(96)02544-3

Enzymology of mammalian phospholipases D: in vitro studies

Mordechai Liscovitch
, Vered Chalifa-Caspi

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

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 language	English
Pages (from-to)	37-44
Number of pages	8
Journal	Chemistry and Physics of Lipids
Volume	80
Issue number	1-2
DOIs	https://doi.org/10.1016/0009-3084(96)02544-3
State	Published - 24 May 1996
Externally published	Yes

Keywords

Enzymology
In vitro studies
Isoenzymes
Phospholipase D

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Organic Chemistry
Cell Biology

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10.1016/0009-3084(96)02544-3

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title = "Enzymology of mammalian phospholipases D: in vitro studies",

abstract = "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.",

keywords = "Enzymology, In vitro studies, Isoenzymes, Phospholipase D",

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AU - Liscovitch, Mordechai

AU - Chalifa-Caspi, Vered

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Y1 - 1996/5/24

N2 - 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.

AB - 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.

KW - Enzymology

KW - In vitro studies

KW - Isoenzymes

KW - Phospholipase D

UR - https://www.scopus.com/pages/publications/0029990785

U2 - 10.1016/0009-3084(96)02544-3

DO - 10.1016/0009-3084(96)02544-3

M3 - Article

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AN - SCOPUS:0029990785

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JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

IS - 1-2

ER -

Enzymology of mammalian phospholipases D: in vitro studies

Abstract

Keywords

ASJC Scopus subject areas

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