Number of the records: 1  

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

  1. 1.
    SYSNO ASEP0380581
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleMolecular 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 TitleBiochemistry-Moscow - ISSN 0006-2979
    Roč. 77, č. 1 (2012), s. 1-14
    Number of pages14 s.
    Languageeng - English
    CountryUS - United States
    Keywordsphospholipase D ; domains ; calcium
    Subject RIVCE - Biochemistry
    R&D ProjectsGAP501/11/1654 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z50380511 - UEB-Q (2005-2011)
    UT WOS000299897200001
    DOI10.1134/S0006297912010014
    AnnotationPhospholipase 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.
    WorkplaceInstitute of Experimental Botany
    ContactDavid Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
    Year of Publishing2013
Number of the records: 1  

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