Poster 150 - Anti-bacteria, anti-parasite and anti-tumor activity of L-amino acid oxidase from

Poster 150. Congresso da Sociedade Brasileira de Toxinologia, 8., Symposium of the Pan American Section of the International Society on Toxinology, 8., 2004, Angra dos Reis, Brasil. Abstracts... J. Venom. Anim. Toxins incl.Trop. Dis., 2004, 10, 3, p.509

Anti-bacteria, Anti-Parasite and Anti-Tumor Activity of L-Amino Acid Oxidase from Bothrops moojeni Snake Venom.

Malta-Neto, N.R.¹; Stábeli, R.G.⁵; Marcussi, S.¹; Monteiro M.C.²; Romão P.R.T.^2,3; Nomizo, A.⁴;Albuquerque, S.⁴;Di Marco, N.⁴; Sant’Ana, C.D.⁴; Sampaio, S. V.⁴; Oliveira, E.B.²; Soares, A.M.¹

1 Unidade de Biotecnologia UNAERP, Ribeirão Preto-SP; 2 Departamento de Bioquímica e Imunologia and Departamento de Farmacologia, FMRP/USP, Ribeir~ao Preto-SP; 3 Departamento de Imunologia, UNISUL, Tubarão-SC, 4 FCFRP/USP, Ribeirão Preto-SP; 5- Laboratório de Bioquímica do Instituto de Pesquisas em Patologias Tropicais (IPEPATRO), Porto Velho-RO.

L-Amino acid oxidases (LAAO, EC 1.4.3.2) are flavoenzymes which catalyze the stereospecific oxidative deamination of an L-amino acid substrate to a corresponding -ketoacid with the production of hydrogen peroxide and ammonia, via an imino acid intermediate. These enzymes are widely distributed in many different organism such as bacteria, fungi, green algae and venomous snakes and

are involved in the utilization of nitrogen sources. The present investigation reports isolation and biochemical characterization of L-amino acid oxidase (BmooLAAO-I) from Bothropsmoojeni venom, that shows bactericidal activity against Escherichia coli and Staphylococcus aureus, with anti-Leishmania activity (L. amazonensis, L. brasiliensis, L. donovani and L. major) and anti-Tumor effect upon human breast adenocarcinoma as well as upon human leukemia T. Bmoo-LAAO-I is an acidic glycoprotein with about 130kDa arranged in two 66kDa monomers. It displays a high specificity toward hydrophobic and basic amino acids, while deglycosylation does not alter its enzymatic activity. Bmoo-LAAO-I also displays dose dependent anti-Leishmania and anti-Tumor activities. The mechanism by its acts seems to be oxidative effects of hydrogen peroxide. SV-LAAOs are therefore interesting multifunctional enzymes, not only for a better understanding of the ophidian envenomation mechanism, but also due to their biotechnological potencial as model for therapeutic agents.