Platelet aggregation and antibacterial effects of an l-amino acid oxidase purified from Bothrops alternatus snake venom.
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.
Stábeli
Rodrigo G
RG
Laboratório de Bioquímica do Instituto de Pesquisas em Patologias Tropicais, Porto Velho-RO, Brazil.
Marcussi
Silvana
S
Carlos
Guilherme B
GB
Pietro
Rosemeire C L R
RC
Selistre-de-Araújo
Heloísa S
HS
Giglio
José R
JR
Oliveira
Eduardo B
EB
Soares
Andreimar M
AM
D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D017837:Bothrops; D003435:Crotalid Venoms / Q000201:enzymology*; D050830:L-Amino Acid Oxidase; D051379:Mice; D008969:Molecular Sequence Data; D010974:Platelet Aggregation / Q000187:drug effects*
D000900:Anti-Bacterial Agents; D003435:Crotalid Venoms; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase