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

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

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...

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Bibliographic Details
Published in:Biochemistry (Moscow) Vol. 77; no. 1; pp. 1 - 14
Main Authors: Kolesnikov, Y. S., Nokhrina, K. P., Kretynin, S. V., Volotovski, I. D., Martinec, J., Romanov, G. A., Kravets, V. S.
Format: Journal Article
Language:English
Published: Dordrecht SP MAIK Nauka/Interperiodica 01-01-2012
Springer
Springer Nature B.V
Subjects:
Amino acids
Analysis
Animals
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Biotechnology
Calcium - metabolism
Catalytic Domain
Cells
Flowers & plants
GTP-Binding Proteins - metabolism
Hydrolysis
Isoenzymes
Life Sciences
Lipids
Lipids - chemistry
Microbiology
Molecular structure
Phospholipase D - chemistry
Phospholipase D - metabolism
Phospholipases
Plants - enzymology
Protein Interaction Mapping
Review
Signal Transduction
phospholipase D
lipids
calcium
protein kinases
domains
G-proteins
protein-protein interactions
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Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297912010014