Phospholipases A2: structure and function
Phospholipases A2: structure and function
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 (sPLA2), cytosolic PLA2 (cPLA2) and Ca2+-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.
membrane binding, apoptesis, lipid signalling, antilacteral protein, inflammation
193-205
Wilton, David C.
4b995f66-ad6c-4d96-9179-c64f3b54466a
March 2005
Wilton, David C.
4b995f66-ad6c-4d96-9179-c64f3b54466a
Wilton, David C.
(2005)
Phospholipases A2: structure and function.
European Journal of Lipid Science and Technology, 107 (3), .
(doi:10.1002/ejlt.200401089).
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 (sPLA2), cytosolic PLA2 (cPLA2) and Ca2+-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.
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Published date: March 2005
Keywords:
membrane binding, apoptesis, lipid signalling, antilacteral protein, inflammation
Organisations:
Centre for Biological Sciences
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Local EPrints ID: 372325
URI: http://eprints.soton.ac.uk/id/eprint/372325
ISSN: 1438-7697
PURE UUID: 2b6a9449-1f34-4bf5-9419-2378370b4c74
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Date deposited: 01 Dec 2014 11:26
Last modified: 14 Mar 2024 18:34
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