• • DRAMP ID

  • DRAMP02522

• • Peptide Name

  • L-amino-acid oxidase (LAAO, LAO, Oh-LAAO; Snakes, reptiles, animals)

• • Source

  • Ophiophagus hannah (King cobra) (Naja hannah)

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • HVINLEESFQEPEYENHLA

• • Sequence Length

  • 19

• • UniProt Entry

  • P81383,A8QL50

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-

• • Target Organism

  • • Gram-negative bacteria: Klebsiella pneumonia (MIC=0.4 µM), Pseudomonas aeruginosa (MIC=0.2 µM), Escherichia coli (MIC=0.4 µM), Escherichia coli ATCC 25922 (MIC=0.8 µM);
    • Gram-positive bacteria: Staphylococcus aureus (MIC=0.006 µM), S. epidermidis (MIC=0.012 µM).

• • Hemolytic Activity

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

• • Cytotoxicity

  • • Not included yet

• • Binding Target

  • Bacterial cell

• • 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

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP02522.

DRAMP02522

• • Function

  • It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis.

• • Tissue specificity

  • Expressed by the venom gland.

• • Toxic dose

  • LD50 is 5 mg/kg by intravenous injection into mice.

• • Temperature dependence

  • Exhibits unusual thermal stability. At pH 7.4, the enzyme retains full activity after incubation at 25 degrees Celsius for 30 days. Is stable at alkaline condition and is not inactivated by freezing.

• ·Literature 1

• • Title

  • Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).

• • Pubmed ID

  • 9304806

• • Reference

  • Int J Biochem Cell Biol. 1997 Jun;29(6):911-919.

• • Author

  • Ahn MY, Lee BM, Kim YS.

• ·Literature 2

• • Title

  • Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom.

• • Pubmed ID

  • 2619759

• • Reference

  • Biochem Int. 1989 Oct;19(4):937-944.

• • Author

  • Tan NH, Saifuddin MN.

• ·Literature 3

• • Title

  • Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase.

• • Pubmed ID

  • 2044840

• • Reference

  • Int J Biochem. 1991;23(3):323-327.

• • Author

  • Tan NH, Saifuddin MN.

• ·Literature 4

• • Title

  • Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation.

• • Pubmed ID

  • 7886693

• • Reference

  • Toxicon. 1994 Nov;32(11):1349-1358.

• • Author

  • Li ZY, Yu TF, Lian EC.

• ·Literature 5

• • Title

  • Antibacterial action of a heat-stabl

• • Pubmed ID

  • 21059402

• • Reference

  • Comp Biochem Physiol C Toxicol Pharmacol. 2011 M

• • Author

  • Lee ML, Tan NH, Fung SY, Sekaran SD.