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Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells
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SYSNO ASEP 0380581 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells Author(s) Kolesnikov, Y. S. (RU)
Nokhrina, K. P. (CA)
Kretynin, S. V. (RU)
Volotovski, I. D. (BY)
Martinec, Jan (UEB-Q) RID, ORCID
Romanov, G. A. (RU)
Kravets, V. S. (UA)Source Title Biochemistry-Moscow - ISSN 0006-2979
Roč. 77, č. 1 (2012), s. 1-14Number of pages 14 s. Language eng - English Country US - United States Keywords phospholipase D ; domains ; calcium Subject RIV CE - Biochemistry R&D Projects GAP501/11/1654 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50380511 - UEB-Q (2005-2011) UT WOS 000299897200001 DOI 10.1134/S0006297912010014 Annotation 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. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2013
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