Platelet aggregation and antibacterial effects of an l-amino acid oxidase purified from Bothrops alternatus snake venom
Stábeli, R.G.; Marcussi, S.; Carlos, G.B.; Pietro, R.C.L.R.; Selistre-de-Araújo, H.ís.S.; Giglio, J.é R.; Oliveira, E.B.; Soares, A.M.
Bioorganic and Medicinal Chemistry 12(11): 2881-2886
ISSN/ISBN: 0968-0896 PMID: 15142548 DOI: 10.1016/j.bmc.2004.03.049
The isolation and biochemical/enzymatic characterization of an L-amino acid oxidase, Balt-LAAO-I, from Bothrops alternatus snake venom, is described. Balt-LAAO-I is an acidic glycoprotein, pI approximately 5.37, homodimeric, Mr approximately 123,000, whose N-terminal sequence is ADVRNPLE EFRETDYEVL. It displays a high specificity toward hydrophobic and basic amino acids, while deglycosylation does not alter its enzymatic activity. Balt-LAAO-I induces platelet aggregation and shows bactericidal activity against Escherichia coli and Staphylococcus aureus. In addition, this enzyme is slightly hemorrhagic and induces edema in the mouse paw. Balt-LAAO-I is a multifunctional enzyme with promising relevant biotechnological and medical applications.