General Information
-
DRAMP ID
- DRAMP02466
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Peptide Name
- L-amino-acid oxidase L2 (LAAO; LAAO-L2; LAO; Reptiles, animals)
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Source
- Daboia russelii (Russel's viper) (Vipera russelii)
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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
- ADDKNPLEECFCEDDDYCEG
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Sequence Length
- 20
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UniProt Entry
- P0DI90
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Protein Existence
- Protein level
Activity Information
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Biological Activity
- Antimicrobial, Antibacterial, Antitumor, Antiparasitic
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Target Organism
- No MICs found in DRAMP database
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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 DRAMP02466.
Physicochemical Information
-
Formula
- C93H132N22O41S3
Absent Amino Acids
- HIMQRSTVW
Common Amino Acids
- D
Mass
- 2310.37
PI
- 3.51
Basic Residues
- 1
Acidic Residues
- 9
Hydrophobic Residues
- 3
Net Charge
- -8
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Boman Index
- -68.68
Hydrophobicity
- -1.315
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
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 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 Information
- ·Literature 1
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Title
- Two L-amino acid oxidase isoenzymes from Russell's viper (Daboia russelli russelli) venom with different mechanisms of inhibition by substrate analogs.
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Pubmed ID
- 18384385
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Reference
- FEBS J. 2008 May;275(9):2078-2095.
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Author
- Mandal S, Bhattacharyya D.