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:19523971). Is highly active on L-Leu followed by L-Phe and L-Ile, moderately active on L-Asp, L-Glu, and L-Lys, and not active on L-Pro, L-Asn, L-Gly, L-Ser and L-Cys (PubMed:19523971). Exhibits diverse biological activities such as antibacterial activity (Minimal inhibitory concentrations (MIC) are 9.0 ug/ml against S.aureus, 144.0 ug/ml against P.aeruginosa and 288.0 ug/ml against E.coli) and inhibition of ADP- and TMVA-induced 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. This protein may also induce hemolysis, edema, apoptosis and have antiparasitic activities. 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-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+) H2O + L-aspartate + O2 = H2O2 + NH4(+) + oxaloacetate H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+) H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+) Optimum pH is 8.8. Homodimer; non-covalently linked. Expressed by the venom gland. Belongs to the flavin monoamine oxidase family. FIG1 subfamily.