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The secretory phospholipase A2 (sPLA2) from Crotalus adamanteus (Eastern Diamondback Rattlesnake) venom is a major toxic component responsible for the local and systemic inflammatory effects of envenomation. While the user refers to it as Group 10, it is formally classified as a Group IIA sPLA2; the Group 10 designation likely stems from its identification as Peak 10 in the species' venom proteome. This enzyme catalyzes the calcium-dependent hydrolysis of the sn-2 ester bond of phospholipids, releasing arachidonic acid and lysophospholipids, which are precursors for potent inflammatory mediators such as prostaglandins and leukotrienes. This activity leads to significant tissue necrosis, edema, and systemic inflammation in snakebite victims. The enzyme is a primary therapeutic target for polyvalent antivenoms and is the focus of development for small-molecule inhibitors like Varespladib, which aim to neutralize its catalytic activity and mitigate the inflammatory cascade.
Competitive inhibition of the sPLA2 active site, preventing substrate binding and hydrolysis.
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