P0DI89 (OXLA_BOTLC) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 9. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Bothrops leucurus (White-tailed jararaca) (White-tailed lancehead)|
|Taxonomic identifier||157295 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops|
|Sequence length||30 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (high activity against L-Met, L-Leu, L-Nle, L-Trp, L-Phe and moderate activity against L-Tyr), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities By similarity. In addition, this protein induces apoptosis. It also interacts with endothelial cells, and inhibits collagen- and ADP-induced platelet aggregation. L-LAAO family effects on platelets are controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions. Ref.1
An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
FAD By similarity.
Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers. Ref.1
Expressed by the venom gland.
Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.1).
The existence of several isoforms has been reported that may be due to either different composition or different glycosylation or by the synthesis from different genes (Ref.1).
Optimum pH is 7.5-8.8 for L-Leu. Ref.1
Hemostasis impairing toxin
Platelet aggregation inhibiting toxin
|Technical term||Direct protein sequencing|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: UniProtKB-KWdefense response to bacterium
Inferred from electronic annotation. Source: UniProtKB-KWhemolysis in other organism
Inferred from electronic annotation. Source: UniProtKB-KW
Inferred from electronic annotation. Source: UniProtKB-SubCell
|Molecular_function||L-amino-acid oxidase activity|
Inferred from electronic annotation. Source: UniProtKB-EC
|Complete GO annotation...|
Sequence annotation (Features)
|||"Cytotoxicity and inhibition of platelet aggregation caused by an l-amino acid oxidase from Bothrops leucurus venom."|
Naumann G.B., Silva L.F., Silva L., Faria G., Richardson M., Evangelista K., Kohlhoff M., Gontijo C.M., Navdaev A., de Rezende F.F., Eble J.A., Sanchez E.F.
Biochim. Biophys. Acta 1810:683-694(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY.
|Accession||Primary (citable) accession number: P0DI89|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
|Annotation program||Animal Toxin Annotation Program|
Index of protein domains and families