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Overview
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Background
Secretory phopholipase A2 (PLA2) enzymes cleave an acyl ester bond in the sn-2 position of glycerophospholipids. These extracellular proteins have a high disulfide bond content, low molecular mass (14 kDa), and require mM levels of Ca2+ for catalysis. They play a crucial role in the generation of arachidonates and eicosanoids, and have a number of biological actions including immunological responses, inflammation, cellular proliferation, vasoconstriction, and bronchioconstriction. Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.
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