Prokaryotic Phospholipase A2
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The prokaryotic phospholipase A2 domain is found in bacterial and fungal
phospholipase A phospholipase is an enzyme that hydrolyzes phospholipids into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C, and D, which are distinguished by the type of reaction which they catalyze: *Phospholipase ...
s. It enables the liberation of
fatty acids In chemistry, in particular in biochemistry, a fatty acid is a carboxylic acid with an aliphatic chain, which is either saturated or unsaturated. Most naturally occurring fatty acids have an unbranched chain of an even number of carbon atoms, ...
and
lysophospholipid The lysophospholipid receptor (LPL-R) group are members of the G protein-coupled receptor family of integral membrane proteins that are important for lipid signaling. In humans, there are eleven LPL receptors, each encoded by a separate gene. Th ...
by hydrolyzing the 2-ester bond of 1,2-diacyl-3-''sn''-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments.


References

{{InterPro content, IPR015141 Protein domains Peripheral membrane proteins