| Identification |
|---|
| HMDB Protein ID
| HMDBP13689 |
| Secondary Accession Numbers
| None |
| Name
| L-amino-acid oxidase |
| Synonyms
|
- K-LAO
- LAAO
|
| Gene Name
| Not Available |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific 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 (PubMed:1612186). Is very active against L-Phe and L-Tyr, moderately active against L-Trp, L-Met, L-Leu, L-norleucine (L-2-aminohexanoate), L-Arg and L-norvaline (L-2-aminopentanoate), and slightly active against L-His, L-cystine, and L-Ile (PubMed:1612186). L-Gln, L-Lys, L-Asn, L-ornithine, L-Ala and L-Val are oxidized very slowly (PubMed:1612186). 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) (PubMed:11600144). 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. |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| apoptotic process |
| defense response to bacterium |
| hemolysis in other organism |
| Cellular Component |
| extracellular region |
| Molecular Function |
| toxin activity |
| L-phenylalaine oxidase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| Not Available |
| Molecular Weight
| Not Available |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
Not Available |
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P0C2D4 |
| UniProtKB/Swiss-Prot Entry Name
| OXLA_NAJKA |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Sakurai Y, Takatsuka H, Yoshioka A, Matsui T, Suzuki M, Titani K, Fujimura Y: Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom. Toxicon. 2001 Dec;39(12):1827-33. doi: 10.1016/s0041-0101(01)00133-7. [PubMed:11600144 ]
- Tan NH, Swaminathan S: Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom. Int J Biochem. 1992 Jun;24(6):967-73. doi: 10.1016/0020-711x(92)90105-a. [PubMed:1612186 ]
|
