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Phospholipases A 2 : structure and function
Author(s) -
Wilton David C.
Publication year - 2005
Publication title -
european journal of lipid science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 94
eISSN - 1438-9312
pISSN - 1438-7697
DOI - 10.1002/ejlt.200401089
Subject(s) - phospholipid , membrane , phospholipase a2 , phospholipase , enzyme , function (biology) , chemistry , biochemistry , cytosol , membrane protein , biophysics , biology , microbiology and biotechnology
Phospholipases A 2 (PLA 2 ) are an example of peripheral membrane proteins that must first bind to the phospholipid interface to allow phospholipid hydrolysis to occur. The interfacial (membrane) binding step plays a crucial role in the biological function of the enzyme and membrane affinity may be determined both by the phospholipid composition of the membrane and the properties of the interfacial binding surface of the protein. There are now three major categories of these enzymes, secreted PLA 2 (sPLA 2 ), cytosolic PLA 2 (cPLA 2 ) and Ca 2+ ‐independent PLA 2 (iPLA 2 ). The structure and function of each category is discussed highlighting how both membrane binding and phospholipid substrate specificity may contribute to the overall functions of these enzymes.