Abstract
Phospholipases A2 (PLA2) 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 PLA2 (sPLA 2), cytosolic PLA2 (cPLA2) and Ca 2+-independent PLA2 (iPLA2). 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. © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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CITATION STYLE
Wilton, D. C. (2005). Phospholipases A2: Structure and function. European Journal of Lipid Science and Technology. https://doi.org/10.1002/ejlt.200401089
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