Journal
BIOCHEMISTRY-MOSCOW
Volume 77, Issue 1, Pages 1-14Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S0006297912010014
Keywords
phospholipase D; domains; calcium; lipids; G-proteins; protein kinases; protein-protein interactions
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Funding
- State Foundation for Basic Research of the Ukraine [F40.4/081, F41.4/042]
- National Academy of Sciences of Ukraine [18-10]
- Academy of Sciences of Czech Republic [5/1-2011]
- Czech Science Foundation [501/11/1654]
- State Foundation for Basic Research of Belarus [B09K-061, B07K-058, B05K-108]
- Russian Foundation for Basic Research [11-04-90491-Ukr., 11-04-00614]
- Russian Academy of Sciences Presidium
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Phospholipase D (PLD) catalyzes hydrolysis of phospholipids with production of phosphatidic acid, which often acts as secondary messenger of transduction of intracellular signals. This review summarizes data of 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 discussed. 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.
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