• DRAMP ID

    • DRAMP02467
    • Peptide Name

    • L-amino-acid oxidase (LAAO; LAO; Reptiles, animals)
    • Source

    • Vipera berus berus (Common viper)
    • Family

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

    • Not found
    • Sequence

    • ADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVYPVKPSEQLYEESLRDQLPTSMHRYPSMIQKIFFAGEYTANAHGWIDSTIK
    • Sequence Length

    • 88
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Antitumor, Antiparasitic
    • Target Organism

    • No MICs found in DRAMP database
    • 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

    • DRAMP02467 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP02467.
    • Formula

    • C461H701N119O143S3
    • Absent Amino Acids

    • ?
    • Common Amino Acids

    • E
    • Mass

    • 10294.53
    • PI

    • 5.1
    • Basic Residues

    • 14
    • Acidic Residues

    • 16
    • Hydrophobic Residues

    • 24
    • Net Charge

    • -2
    • Boman Index

    • -198.9
    • Hydrophobicity

    • -0.863
    • Aliphatic Index

    • 65.45
    • Half Life

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

    • 12950
    • Absorbance 280nm

    • 148.85
    • Polar Residues

    • 23

DRAMP02467

DRAMP02467 chydropathy plot
    • Function

    • Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (the most specific substrate is L-Phe, followed by L-Met, L-Leu, L-Phe, L-Ile, L-Arg and L-His), 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, antibacterial and antiparasitic activities By similarity. In addition, this protein has an ability to induce apoptosis in cultured HeLa and K562 cells, and inhibits ADP-induced platelet aggregation dose-dependently. 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.
    • Tissue specificity

    • Expressed by the venom gland.
    • Biophysicochemical properties

    • Kinetic parameters (KM=0.361 mM for L-Leu; KM=0.286 mM for L-Met; KM=0.058 mM for L-Phe).
  • ·Literature 1
    • Title

    • Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom.
    • Reference

    • Biochim Biophys Acta. 2006 Apr;1764(4):707-714.
    • Author

    • Samel M, Vija H, Rönnholm G, Siigur J, Kalkkinen N, Siigur E.