• DRAMP ID

    • DRAMP02461
    • Peptide Name

    • L-amino-acid oxidase (BmarLAAO; LAAO; LAO; snakes, reptils, animals)
    • Source

    • Bothrops marajoensis (Marajo lancehead)
    • Family

    • Belongs to the flavin monoamine oxidase family (FIG1 subfamily)
    • Gene

    • Unknown
    • Sequence

    • AHDGNPLEECFREDDEEFFLEIAKNGLTATSNPKRVVIV
    • Sequence Length

    • 39
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial, Antifungal, Antiparasitic, Antimicrobial
    • Target Organism

      • No MICs found on DRAMP database
    • Hemolytic activity

    • Unknown
    • Binding Target

    • Unknown
    • Structure

    • Unknown
    • Structure Description

    • Unknown
    • DRAMP02461 helical wheel diagram
    • Formula

    • C193H300N52O64S
    • Absent Amino Acids

    • MQWY
    • Common Amino Acids

    • E
    • Mass

    • 5082.86
    • PI

    • 4.17
    • Basic Residues

    • 5
    • Acidic Residues

    • 9
    • Hydrophobic Residues

    • 14
    • Boman Index

    • -86.83
    • Hydrophobicity

    • -48.46
    • Aliphatic Index

    • 80
    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 9

DRAMP02461

DRAMP02461 chydropathy plot
    • Function

    • Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antiparasitic activities, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. In addition, this protein inhibits dose-dependently the growth of Gram-positive, Gram-negative bacteria and yeast, probably by the generation of hydrogen peroxide.
    • Tissue specificity

    • Expressed by the venom gland.
    • Miscellaneous

    • Has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.
  • Literature 1
    • Reference

    • Toxicon. 2010 Apr 1;55(4):795-804.
    • Author

    • Costa Torres AF, Dantas RT, Toyama MH, Diz Filho E, Zara FJ, Rodrigues de Queiroz MG, Pinto Nogueira NA, Rosa de Oliveira M, de Oliveira Toyama D, Monteiro HS, Martins AM.
    • Title

    • Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: phospholipase A2 and L-amino acid oxidase.