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Human phospholipase A₂s (PLA₂) constitute a superfamily of enzymes that hydrolyze the sn-2 acyl-chain of glycerophospholipids, producing lysophospholipids and free fatty acids. Each PLA₂ enzyme type contributes to specific biological functions based on its expression, subcellular localization, and substrate specificity. Among the PLA₂ superfamily, the cytosolic cPLA₂ enzymes, calcium-independent iPLA₂ enzymes, and secreted sPLA₂ enzymes are implicated in many diseases, but a central issue is the preference for double-bond positions in polyunsaturated fatty acids (PUFAs) occupying the sn-2 position of membrane phospholipids. We demonstrate that each PLA₂ has a unique preference between the specific omega-3 fatty acids eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) and the omega-6 arachidonic acid (AA), which are the precursors of most proinflammatory and anti-inflammatory …