Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells

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DOI	Resolve DOI: https://doi.org/10.1134/S0006297912010014
Author	Search for: Kolesnikov, Y. S.; Search for: Nokhrina, K. P.¹; Search for: Kretynin, S. V.; Search for: Volotovski, I. D.; Search for: Martinec, J.; Search for: Romanov, G. A.; Search for: Kravets, V. S.
Affiliation	National Research Council of Canada. NRC Plant Biotechnology Institute
Format	Text, Article
Subject	phospholipase D; domains; calcium; lipids; G-proteins; protein kinases; protein–protein interactions
Abstract	Phospholipase D (PLD) catalyzes hydrolysis of phospholipids with production of phosphatidic acids, which often act as secondary messengers on transmission of intracellular signals. This review summarizes data of various leading laboratories on specific features of organization and regulation of PLD activity in plant and animal cells. The main structural domains of PLD (C2, PX, PH), the active site, and other functionally important parts of the enzyme are considered. Regulatory mechanisms of PLD activity are characterized in detail. Studies associated with molecular design, analysis, and synthesis of new nontoxic substances capable of inhibiting different PLD isoenzymes in vivo are shown to be promising for biotechnology and medicine.
Publication date	2012-01-27
In	Biochemistry (Moscow) 77, no. 1 (27 January 2012): 1–14.
Language	English
Peer reviewed	Yes
NRC number	NRCC 54644
NPARC number	19631494
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Record identifier	740b4fe5-17f1-4ef7-a4bf-ad2d609c57c2
Record created	2012-04-02
Record modified	2020-04-21

Date modified:: 2024-11-03