Snake venom phospholipase A2 (PLA2) that shows enzymatic activity in the presence of a synthetic substrate. In vitro, blocks the neuromuscular transmission in young chick biventer cervicis preparations. In mice, induces myonecrosis and a systemic interleukin-6 response upon intramuscular injection. Also induces edema and exerts a strong pro-inflammatory effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. 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. Inhibited by magnesium, cadmium and manganese ions. Also inhibited by crotapotin. Optimum pH is 8.0. Optimum temperature is 35-45 degrees Celsius. Expressed by the venom gland. Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.