Zinc metalloproteinase that causes hemorrhage in mice following intradermal injection and impairs hemostasis in its prey. In skin tissues, it degrades components of the basement membrane surrounding blood vessels and capillaries. In muscle tissue, it degrades the extracellular matrix, thus causing muscle necrosis. However, it lacks direct toxicity on myocytes. Hydrolyzes alpha-2 chain (COL4A2) of type IV collagen more slowly than the alpha-1 chain (COL4A1). Hydrolyzes fibronectin (FN1). It also impairs hemostasis by acting on fibrin(ogen) and platelets. Shows fibrinolytic activity, with a selective degradation of gamma-dimer (FGG). Shows fibrinogenolytic activity by preferentially cleaving the Bbeta chain, and later gamma-chain. Aalpha-chain remains resistant to proteolytic digestion. Weakly inhibits collagen-triggered platelet aggregation of human plasma rich platelet. Binds 3 Zn(2+) ions per subunit. Inhibited by EDTA, 1,10-phenanthroline, cyanide, and serum alpha2-microglobulin. Not inhibited by EGTA, PMSF, leupeptin, pepstatin and aprotinin. Optimum pH is 7.6. Optimum temperature is 37 degrees Celsius. Expressed by the venom gland. Dose that inhibits collagen-triggered platelet aggregation of human plasma rich platelet (IC(50)) is 1.3 mmol/l. Belongs to the venom metalloproteinase (M12B) family.