Snake venom phospholipase A2 (PLA2) that induces myotoxicity and local edema in mice (PubMed:25365526). In addition, it causes neuromuscular blockade in avian neuromuscular preparations with a significant direct action on skeletal muscle function (PubMed:25365526). Myotoxic action is exerted by both enzymatic and non-enzymatic mechanisms (PubMed:25365526). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:25365526). a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) Binds 1 Ca(2+) ion. P-bromophenacyl bromide (BPB) completely inhibits the catalytic and edematogenic activities (PubMed:25365526). Enzymatic activity is also diminished by EDTA, heparin and crotapotins F2 and F3 from C.d.collilineatus (PubMed:25365526). Inhibited by divalent cations different from calcium ions (cadmium, magnesium, manganese, zinc), since they act as competitive antagonists of this cofactor (PubMed:25365526). Optimum pH is 8. Optimum temperature is 40-45 degrees Celsius. Monomer. Expressed by the venom gland. Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.