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

0380581 - ÚEB 2013 RIV US eng J - Článek v odborném periodiku
Kolesnikov, Y. S. - Nokhrina, K. P. - Kretynin, S. V. - Volotovski, I. D. - Martinec, Jan - Romanov, G. A. - Kravets, V. S.
Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells.
Biochemistry-Moscow. Roč. 77, č. 1 (2012), s. 1-14. ISSN 0006-2979. E-ISSN 1608-3040
Grant CEP: GA ČR(CZ) GAP501/11/1654
Výzkumný záměr: CEZ:AV0Z50380511
Klíčová slova: phospholipase D * domains * calcium
Kód oboru RIV: CE - Biochemie
Impakt faktor: 1.149, rok: 2012

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.
Trvalý link: http://hdl.handle.net/11104/0211250