This metalloproteinase displays proteolytic activity on fibrin, fibrinogen, collagen, casein and gelatin. It inhibits ADP- and collagen-induced platelet aggregation and displays a very low edema inducing activity. Binds 1 zinc ion per subunit. Completely inhibited by EDTA, EGTA, 1,10-phenanthroline, and partially by beta-mercaptoethanol. Is not inhibited by aprotinin and leupeptin. Conserves its activity upon fibrinogen when incubated with cobalt, magnesium ions up to 40 mM, but loses the proteolytic activity when incubated with manganese, fer, zinc or calcium ions. Optimum pH is 7.0. Monomer. Expressed by the venom gland. Does not induce hemorrhage, myotoxicity and lethality and does not show any clotting or anticoagulant activity on human citrated plasma. Belongs to the venom metalloproteinase (M12B) family. P-I subfamily.