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

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DOIResolve DOI: http://doi.org/10.1134/S0006297912010014
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TypeArticle
Journal titleBiochemistry (Moscow)
Volume77
Issue1
Pages114; # of pages: 14
Subjectphospholipase D; domains; calcium; lipids; G-proteins; protein kinases; protein–protein interactions
AbstractPhospholipase 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
LanguageEnglish
AffiliationNRC Plant Biotechnology Institute; National Research Council Canada
Peer reviewedYes
NRC number54644
NPARC number19631494
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Record identifier740b4fe5-17f1-4ef7-a4bf-ad2d609c57c2
Record created2012-04-02
Record modified2016-05-09
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