General Information
-
DRAMP ID
- DRAMP02462
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Peptide Name
- L-amino-acid oxidase (LAAO; LAO; snakes, reptils, animals)
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Source
- Naja oxiana (Central Asian cobra) (Oxus cobra)
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Family
- Belongs to the flavin monoamine oxidase family (FIG1 subfamily)
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Gene
- Not found
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Sequence
- DDRRSPLEECFQQNDYEEFLEIARNSQLYQESLREDSSYHLSFIESLKSDALFSYEKKFWEADGIHGGKVINDLSLIHDLPKREIQALCYPSIKK
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Sequence Length
- 95
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UniProt Entry
- P0DI91
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antiparasitic
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Target Organism
-
- Gram-positive bacterium: Bacillus subtilis;
- Gram-negative bacterium: E. coli.
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
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N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
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Nonterminal Modifications and Unusual Amino Acids
- Not included yet
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Stereochemistry
- Not included yet
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Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP02462.
Physicochemical Information
-
Formula
- C500H764N132O158S2
Absent Amino Acids
- MT
Common Amino Acids
- ELS
Mass
- 11216.48
PI
- 4.86
Basic Residues
- 15
Acidic Residues
- 19
Hydrophobic Residues
- 29
Net Charge
- -4
-
Boman Index
- -235.37
Hydrophobicity
- -0.762
Aliphatic Index
- 81.16
Half Life
-
- Mammalian:1.1 hour
- Yeast:3 min
- E.coli:>10 hour
Extinction Coefficient Cystines
- 13075
Absorbance 280nm
- 139.1
Polar Residues
- 24
DRAMP02462

Comments Information
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 antibacterial activity against both Gram-positive (B.subtilis) and Gram-negative (E.coli) bacteria, and inhibition of ADP- or collagen-induced 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. This protein may also induce hemorrhage, hemolysis, edema, apoptosis, and have antiparasitic activities.
Tissue specificity
- Expressed by the venom gland.
Biophysicochemical properties
- Kinetic parameters (KM=0.885 mM for L-Met; KM=0.051 mM for L-Phe; KM=0.147 mM for L-Trp; KM=0.75 mM for L-Leu)
Literature Information
- ·Literature 1
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Title
- L-Amino acid oxidase from Naja naja oxiana venom.
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Pubmed ID
- 18294891
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Reference
- Comp Biochem Physiol B Biochem Mol Biol. 2008 Apr;149(4):572-580.
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Author
- Samel M, Tõnismägi K, Rönnholm G, Vija H, Siigur J, Kalkkinen N, Siigur E.