The Phospholipase A2 (PLA2) superfamily contains hundreds of enzymes that all fulfill the same function of breaking down phospholipids by cleaving off their sn-2 hydrocarbon tails. Inside human cells, PLA2 performs several key cellular functions including the production of signaling molecules and the digestion of dietary fats. However, PLA2 can also enter the human body unexpectedly through animal toxins – such as snake venom – where it causes disruption of the cell membrane and eventually leads to tissue death. Due to PLA2 and other toxins, the World Health Organization classifies snake bites as the “deadliest neglected tropical disease.” (World Health Organization, 2023) PLA2 proteins range in size from 14 to 18 kDa, including three conserved alpha helices, and six to eight disulfide bridges stabilizing the molecule. The enzyme’s catalytic dyad is nestled between the ɑ2 and ɑ3 helices and consists of a histidine (His47) and aspartate (Asp93), where the lipid cleavage takes place. In order for the protein to react, a Ca2+ ion cofactor must be present, stabilized by a glycine (Gly30). In addition, a flexible C terminal loop allows PLA2 to change conformation in order to interact with a number of natural lipids. As one of the main components of highly toxic snake venoms, research on PLA2 aims to develop better antivenoms, with the hope of saving people from death (81,000 annually) or permanent injury (400,000 annually). (World Health Organization, 2023) Other intriguing directions for future studies of the PLA2 superfamily include cancer research, degenerative joint disease, and cardiovascular disease.