Snake venom zinc metalloprotease that acts at several levels. It has direct fibrino(geno)lytic activity (Aalpha chain of fibrinogen is cleaved quickly, Bbeta chain slowly, and gamma chain even more slowly) and degradation of TNF-alpha. These activities permit to protect against sepsis and disseminated intravascular coagulation (PubMed:18634754, PubMed:17964518, PubMed:19013210, PubMed:19070354). It inhibits ADP-induced platelet aggregation in human platelet-rich plasma (IC(50)=65.4 ug/ml) (PubMed:19013210). It decreases the activity of complement by degrading human C5, C6 and C9 in vitro, decreasing serum levels of C1q, C3 and C4 in rat, and inhibiting the MAC deposition on HUVECs membrane. This inhibition of complement protects against hyperacute rejection that is the main barrier in xenotransplantation (PubMed:23178656). Has preference for Lys at the P1 position. Cleaves insulin B chain at '36-Val-|-Glu-37', '39-Leu-|-Tyr-40', and '48-Phe-|-Phe-49' bonds. Also cleaves fibronectin and type IV collagen (PubMed:19013210). Binds 1 zinc ion per subunit. Inhibited by PMSF and EDTA. Slightly inhibited by Cu(2+) and Zn(2+). Not inhibited by aprotinin, SBTI, Ca(2+), Mg(2+), Na(+) and K(+). Optimum pH is 7.0-10.5. Optimum temperature is 30-50 degrees Celsius. Expressed by the venom gland. LD(50) is 53.5 mg/kg by intravenous injection into mice. This recombinant protein is 95% identical to the peptidase M12B domain of the zinc metalloproteinase-disintegrin-like acurhagin (AC Q9W6M5). Does not activate plasminogen. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily.