General Information

    • DRAMP ID

    • DRAMP03168

    • Peptide Name

    • L-amino-acid oxidase (K-LAO; LAAO; LAO; reptilia, animals)

    • Source

    • Naja naja kaouthia (Monocled cobra)

    • Family

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

    • Gene

    • Not found

    • Sequence

    • DDRRSPLEECFQQNDYEEFLEIAKNGLKKTXNPKHVXV

    • Sequence Length

    • 38

    • Protein Existence

    • Protein level

Activity Information

    • 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, Flavoprotein

Structure Information

    • 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

    • DRAMP03168 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP03168.

Physicochemical Information

    • Formula

    • C187H289N53O59S

    • Absent Amino Acids

    • MW

    • Common Amino Acids

    • E

    • Mass

    • 4514.42

    • PI

    • 5.13

    • Basic Residues

    • 7

    • Acidic Residues

    • 8

    • Hydrophobic Residues

    • 9

    • Net Charge

    • -1

    • Boman Index

    • -116.27

    • Hydrophobicity

    • -1.197

    • Aliphatic Index

    • 58.95

    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 1490

    • Absorbance 280nm

    • 40.27

    • Polar Residues

    • 8

DRAMP03168

DRAMP03168 chydropathy plot

Comments Information

    • Function

    • Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highly active against L- Phe and L-Tyr, and moderately active against L-Trp, L-Met, L-Leu, and L-Arg), 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). This protein inhibits both agonist- and shear stress-induced platelet aggregation (SIPA). 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.

Literature Information

  • ·Literature 1

    • Title

    • Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom.

    • Reference

    • Int J Biochem. 1992 Jun;24(6):967-973.

    • Author

    • Tan NH, Swaminathan S.
  • ·Literature 2

    • Title

    • Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom.

    • Reference

    • Toxicon. 2001 Dec;39(12):1827-1833.

    • Author

    • Sakurai Y, Takatsuka H, Yoshioka A, Matsui T, Suzuki M, Titani K, Fujimura Y.