• DRAMP ID

    • DRAMP02466
    • Peptide Name

    • L-amino-acid oxidase L2 (LAAO; LAAO-L2; LAO; Reptiles, animals)
    • Source

    • Daboia russelii (Russel's viper) (Vipera russelii)
    • Family

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

    • Unknown
    • Sequence

    • ADDKNPLEECFCEDDDYCEG
    • Sequence Length

    • 20
    • Evidence code

    • Protein level
    • Biological Activity

    • Antibacterial, Antiparasitic, Antitumor, Antimicrobial
    • Target Organism

      • No MICs found on DRAMP database
    • Hemolytic activity

    • Unknown
    • Binding Target

    • Unknown
    • Structure

    • Unknown
    • Structure Description

    • Unknown
    • DRAMP02466 helical wheel diagram
    • Formula

    • C93H132N22O41S3
    • Absent Amino Acids

    • HIMQRSTVW
    • Common Amino Acids

    • D
    • Mass

    • 2649.48
    • PI

    • 3.33
    • Basic Residues

    • 1
    • Acidic Residues

    • 9
    • Hydrophobic Residues

    • 3
    • Boman Index

    • -68.68
    • Hydrophobicity

    • -131.5
    • Aliphatic Index

    • 24.5
    • Half Life

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

    • 1615
    • Absorbance 280nm

    • 85
    • Polar Residues

    • 6

DRAMP02466

DRAMP02466 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, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity.
    • Tissue specificity

    • Expressed by the venom gland.
    • Biophysicochemical properties

    • Kinetic parameters (KM=1.89 mM for L-Ile; KM=599.7 µM for L-Leu; KM=222.8 µM for L-Met; KM=49.3 µM for L-Phe; KM=235.1 µM for L-Trp; KM=538.2 µM for L-Tyr; Vmax=6.94 µmol/min/mg enzyme toward L-Phe).
  • Literature 1
    • Reference

    • FEBS J. 2008 May;275(9):2078-2095.
    • Author

    • Mandal S, Bhattacharyya D.
    • Title

    • Two L-amino acid oxidase isoenzymes from Russell's viper (Daboia russelli russelli) venom with different mechanisms of inhibition by substrate analogs.