• DRAMP ID

    • DRAMP02459
    • Peptide Name

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

    • Bothrops jararaca (Jararaca)
    • Family

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

    • Unknown
    • Sequence

    • ADDKNPLEECFRETDYEEFLEIARNGLKATSNPKRVV
    • Sequence Length

    • 37
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial, Antiparasitic, Antitumor, Anti-Gram+, Antimicrobial
    • Target Organism

      • Gram-positive bacterium: S. aureus.
    • Hemolytic activity

    • Unknown
    • Binding Target

    • Unknown
    • Structure

    • Unknown
    • Structure Description

    • Unknown
    • DRAMP02459 helical wheel diagram
    • Formula

    • C186H294N52O63S
    • Absent Amino Acids

    • HMQW
    • Common Amino Acids

    • E
    • Mass

    • 4941.05
    • PI

    • 4.37
    • Basic Residues

    • 6
    • Acidic Residues

    • 9
    • Hydrophobic Residues

    • 11
    • Boman Index

    • -115.66
    • Hydrophobicity

    • -98.65
    • Aliphatic Index

    • 65.95
    • Half Life

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

    • 1490
    • Absorbance 280nm

    • 41.39
    • Polar Residues

    • 9

DRAMP02459

DRAMP02459 chydropathy plot
    • Function

    • Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Met, L-Leu, L-Phe, L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, edema, apoptosis of vascular endothelial cells or tumor cell lines, 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. This protein induce hemolysis and has antibacterial and antiparasitic activities (against the Gram-positive S.aureus). Tested in vivo, this protein significantly inhibits Ehrlich ascite tumors growth and induces an influx of polymorphonuclear cells, as well as spontaneous liberation of hydrogen peroxide from peritoneal macrophages.
    • Tissue specificity

    • Expressed by the venom gland.
    • Miscellaneous

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

    • Basic Clin Pharmacol Toxicol. 2008 Jun;102(6):533-542.
    • Author

    • de Vieira Santos MM, Sant'Ana CD, Giglio JR, da Silva RJ, Sampaio SV, Soares AM, Fecchio D.
    • Title

    • Antitumoural effect of an L-amino acid oxidase isolated from Bothrops jararaca snake venom.
  • Literature 2
    • Reference

    • Toxicon. 2009 Mar 1;53(3):330-341.
    • Author

    • Ciscotto P, Machado de Avila RA, Coelho EA, Oliveira J, Diniz CG, Farías LM, de Carvalho MA, Maria WS, Sanchez EF, Borges A, Chávez-Olórtegui C.
    • Title

    • Antigenic, microbicidal and antiparasitic properties of an L-amino acid oxidase isolated from Bothrops jararaca snake venom.
  • Literature 3
    • Reference

    • Toxicon. 2010 Nov;56(6):944-955.
    • Author

    • olindo P, Teixeira-Ferreira AS, DaMatta RA, Alves EW.
    • Title

    • L-amino acid oxidase activity present in fractions of Bothrops jararaca venom is responsible for the Induction: of programmed cell death in Trypanosoma cruzi.