Snake venom zinc metalloprotease that has fibrino(geno)lytic activities. Hydrolyzes the alpha-chain (FGA) and more slowly the beta-chain of fibrinogen (FGB), without affecting the gamma-chain. Preferentially hydrolyzes the beta-chain (FGB) of fibrin. In vivo, shows a low edema-inducing effect. This action may be attributed to degradation of proteins in the cell membrane and consequent release of inflammatory mediators and leukocyte infiltrate. Binds 1 zinc ion per subunit. Inhibited by EDTA and 1,10-phenanthroline. Not inhibited by beta-mercaptoethanol, benzamidine and aprotinin. Monomer. Expressed by the venom gland. Contains 7 disulfide bonds. Is devoid of coagulant activities on bovine plasma. In vivo, does not induce hemorrhage on mice back skin when 50 ug of enzyme are intradermally injected (PubMed:21130897). Belongs to the venom metalloproteinase (M12B) family. P-I subfamily. If fragments identified by mass spectrometry (and not included in this entry) are taken into account for comparison, this protein is 71% identical to the metalloproteinase from the same venom leucurolysin-A (AC P84907).