Phospholipases: Generation of Lipid-Derived Second Messengers

  • Mary F. Roberts
Part of the Hormones in Health and Disease book series (HHD)

Absrtact

Phospholipases are lipolytic enzymes that play key roles in signal transduction by generating both lipid and in some cases soluble second messengers. Their catalytic properties are often exquisitely controlled by phosphorylation, interaction with other proteins (e.g., GTP-binding proteins), as well as interaction with other lipids. Most of these proteins fall into the category of peripheral membrane proteins. An important aspect of these enzymes is that while they are in general water-soluble, the carry out their catalysis at an interface. This complicates kinetics because the dimensionality of the reaction has changed from a single phase (bulk solution) to two phases (the phospholipid aggregate interface as well as the bulk solution). Often there is a separate binding domain /site for the interface as well as for the active site. Such multiple functional sites can be modular or incorporated into a single area of the protein. A recurring theme is that there are mechanisms that enhance protein association with the inteface. This in turn increases the local concentration of substrate (and in some cases chemically modifies the protein) such that catalytic efficiency is increased. These secondary sites can serve to regulate enzyme activity by controlling access to substrate. However, there are often other modes of regulation that interwine phospholipases with other signal transduction proteins.

Keywords

Serine Thiol Cytosol Quercetin Lecithin 

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© Springer Science+Business Media New York 1999

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  • Mary F. Roberts

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