• DRAMP ID

    • DRAMP02902
    • Peptide Name

    • L-amino-acid oxidase (LAAO, LAO; BpirLAAO-I; reptilia, animals)
    • Source

    • Bothrops pirajai (Piraja's lance head)
    • Family

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

    • Not found
    • Sequence

    • ADDKNPLEEFRETNYEVFLEIAKNGLKATSNPKRVVIVGAGMAGLSAAY
    • Sequence Length

    • 49
    • Protein Existence

    • Protein level
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli, Pseudomonas aeruginosa. Leishmania sp..
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP02902 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP02902.
    • Formula

    • C235H375N63O74S
    • Absent Amino Acids

    • CHQW
    • Common Amino Acids

    • A
    • Mass

    • 5299
    • PI

    • 5.15
    • Basic Residues

    • 6
    • Acidic Residues

    • 7
    • Hydrophobic Residues

    • 19
    • Net Charge

    • -1
    • Boman Index

    • -71.89
    • Hydrophobicity

    • -0.253
    • Aliphatic Index

    • 85.71
    • Half Life

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

    • 2980
    • Absorbance 280nm

    • 62.08
    • Polar Residues

    • 14

DRAMP02902

DRAMP02902 chydropathy plot
    • FunctionCatalyzes 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. This protein may also have activities in hemorrhage, hemolysis, and apoptosis.

    • Tissue specificity

    • Expressed by the venom gland.
    • Miscellaneous

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

    • Biochemical and functional characterization of an L-amino acid oxidase isolated from Bothrops pirajai snake venom.
    • Reference

    • Bioorg Med Chem. 2006 Oct 15;14(20):7034-7043.
    • Author

    • Izidoro LF, Ribeiro MC, Souza GR, Sant'Ana CD, Hamaguchi A, Homsi-Brandeburgo MI, Goulart LR, Beleboni RO, Nomizo A, Sampaio SV, Soares AM, Rodrigues VM.