• DRAMP ID

    • DRAMP02463
    • Peptide Name

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

    • Eristocophis macmahoni (Leaf-nosed viper)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • ADDKNPLEEAFREADYEVFLEIAKNGL
    • Sequence Length

    • 27
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • 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

    • FAD and Flavoprotein
    • 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

    • DRAMP02463 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP02463.
    • Formula

    • C138H210N34O47
    • Absent Amino Acids

    • CHMQSTW
    • Common Amino Acids

    • E
    • Mass

    • 3097.39
    • PI

    • 4.12
    • Basic Residues

    • 3
    • Acidic Residues

    • 8
    • Hydrophobic Residues

    • 11
    • Net Charge

    • -5
    • Boman Index

    • -61.79
    • Hydrophobicity

    • -0.656
    • Aliphatic Index

    • 83.33
    • Half Life

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

    • 1490
    • Absorbance 280nm

    • 57.31
    • Polar Residues

    • 4

DRAMP02463

DRAMP02463 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 hemolysis, edema, apoptosis, as well as induction 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. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. This protein may also have antibacterial and antiparasitic activities.
    • Catalytic activity

    • An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
    • Subunit structure

    • Homodimer; non-covalently linked.
    • Tissue specificity

    • Expressed by the venom gland.
  • ·Literature 1
    • Title

    • Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom.
    • Reference

    • Arch Biochem Biophys. 2000 Dec 15;384(2):216-226.
    • Author

    • Ali SA, Stoeva S, Abbasi A, Alam JM, Kayed R, Faigle M, Neumeister B, Voelter W.