Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the toxicity of the venom. Shows high activity on L-Phe, L-Tyr, L-Trp, L-Leu, and L-Met, moderate activity on L-Ile, L-Val, L-Ala, and L-His, and slight activity on L-Arg, L-Pro, L-Thr, L-Ser, L-Glu, L-Gly, and L-Lys. Exhibits diverse biological activities, such as edema, apoptosis of tumor cell lines, antibacterial activities against both Gram-positive and Gram-negative bacteria, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. It may also induce hemolysis. Has parasiticidal activities against and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.