Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18346051). Is highly active on L-Leu, L-Met, moderately active on L-Arg, L-Trp, L-Phe, L-Val, L-His, and L-Ile, and is weakly or not active on L-Cys, L-Lys, L-Ala, L-Thr, L-Asp, L-Ser, and L-Pro (PubMed:18346051, PubMed:19101583). Exhibits diverse biological activities, such as hemorrhage, edema, apoptosis of vascular endothelial cells or tumor cell lines, as well as regulation 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 (By similarity). This protein induce hemolysis and has antibacterial and antiparasitic activities (against the Gram-positive S.aureus). Tested in vivo, this protein significantly inhibits Ehrlich ascite tumors growth and induces an influx of polymorphonuclear cells, as well as spontaneous liberation of hydrogen peroxide from peritoneal macrophages. an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+) H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+) H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+) H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+) H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+) H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+) H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+) H2O + L-histidine + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 + NH4(+) H2O + L-valine + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+) Homodimer; non-covalently linked. Expressed by the venom gland. N-Glycosylated. Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (PubMed:19101583, PubMed:20615423). Belongs to the flavin monoamine oxidase family. FIG1 subfamily. Bothrops jararaca venom seems to contain 2 isoforms with different hydrophobic properties (PubMed:18346051). These isoforms may reflect different glycosylation of the protein or they may have been synthesized from different genes.