Platelet aggregation and antibacterial effects of an l-amino acid oxidase purified from Bothrops alternatus snake venom

• Published in: Bioorganic & medicinal chemistry 2004-06, Vol.12 (11), p.2881-2886
• Main Authors: Stábeli, Rodrigo G., Marcussi, Silvana, Carlos, Guilherme B., Pietro, Rosemeire C.L.R., Selistre-de-Araújo, Heloı́sa S., Giglio, José R., Oliveira, Eduardo B., Soares, Andreimar M.
• Format: Article
• Language: English
• Subjects: Amino Acid Oxidoreductases - chemistry; Amino Acid Oxidoreductases - isolation & purification; Amino Acid Oxidoreductases - pharmacology; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - isolation & purification; Anti-Bacterial Agents - pharmacology; Antibacterial agents; Antibiotics. Antiinfectious agents. Antiparasitic agents; Bactericidal effect; Biological and medical sciences; Biotechnological application; Bothrops; Bothrops alternatus; Crotalid Venoms - enzymology; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; L-Amino Acid Oxidase; Medical sciences; Mice; Miscellaneous; Molecular Sequence Data; Oxidoreductases; Pharmacology. Drug treatments; Platelet aggregation; Platelet Aggregation - drug effects; Snake venom
• ISSN: 0968-0896; 1464-3391
• DOI: 10.1016/j.bmc.2004.03.049

N-terminal sequence is: A D V R N P L E E F R E T D Y E V L The present investigation reports the isolation and biochemical characterization of an l-amino acid oxidase (Balt-LAAO-I) from Bothrops alternatus venom, with special reference to its platelet aggregation effect and bactericidal activity. 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, p I ∼ 5.37, homodimeric, M r∼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.