Phospholipase A2 enzyme (PLA2)

Phospholipase A2 enzymes (PLA2s) are a superfamily of enzymes that hydrolyze the sn-2 fatty acid of membrane phospholipids, releasing free fatty acids and lysophospholipids[1][2][5]. At presynaptic membranes, certain PLA2 isoforms—particularly those derived from snake venoms—act as potent neurotoxins that disrupt synaptic vesicle cycling, inhibit neurotransmitter (e.g., acetylcholine) release, and induce neuroparalysis by damaging the presynaptic membrane or interacting with specific membrane proteins and ion channels[3][4][5][6]. Endogenous PLA2s are also involved in normal physiological regulation of membrane fluidity, calcium mobilization, and inflammatory responses, with abnormal PLA2 activity implicated in neurodegenerative, cardiovascular, and inflammatory diseases[1][2]. The term "Phospholipase A2 enzyme activity at presynaptic membrane" describes a biological function, not a unique molecular entity; it typically refers to the activity of PLA2 isoforms (e.g., secreted PLA2, snake venom PLA2) at the presynaptic terminal, rather than a distinct target molecule—hence, this entry is incomplete or non-canonical from a target nomenclature perspective[4][6].

Other names

Phospholipases A2Phospholipase A2PLA2sSecreted phospholipase A2Snake venom phospholipase A2Presynaptic neurotoxic phospholipase A2

Inhibition of PLA2 enzymatic activity to prevent phospholipid hydrolysis Neutralization of neurotoxic effects via antivenoms