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

Bioorg Med Chem. 2004 Jun 1;12(11):2881-6. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Oxidoreductases / chemistry
  • Amino Acid Oxidoreductases / isolation & purification*
  • Amino Acid Oxidoreductases / pharmacology*
  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / isolation & purification*
  • Anti-Bacterial Agents / pharmacology*
  • Bothrops*
  • Crotalid Venoms / enzymology*
  • L-Amino Acid Oxidase
  • Mice
  • Molecular Sequence Data
  • Platelet Aggregation / drug effects*


  • Anti-Bacterial Agents
  • Crotalid Venoms
  • Amino Acid Oxidoreductases
  • L-Amino Acid Oxidase