P0CJ40 (OXLA_BOTMA) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 12. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Bothrops marajoensis (Marajo lancehead)|
|Taxonomic identifier||157554 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops|
|Sequence length||39 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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, and antiparasitic activities, as well as regulation of 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 By similarity. In addition, this protein inhibits dose-dependently the growth of Gram-positive, Gram-negative bacteria and yeast, probably by the generation of hydrogen peroxide. 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.
N-glycosylated By similarity.
Has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.1).
Hemostasis impairing 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-KWdefense response to fungus
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)
|||"Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: phospholipase A2 and L-amino acid oxidase."|
Costa Torres A.F., Dantas R.T., Toyama M.H., Diz Filho E., Zara F.J., Rodrigues de Queiroz M.G., Pinto Nogueira N.A., Rosa de Oliveira M., de Oliveira Toyama D., Monteiro H.S.A., Martins A.M.C.
Toxicon 55:795-804(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
|Accession||Primary (citable) accession number: P0CJ40|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Animal Toxin Annotation Program|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families