P0DI88 (OXLA_BOTJA) Reviewed, UniProtKB/Swiss-Prot
Last modified October 31, 2012. Version 7. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Bothrops jararaca (Jararaca)|
|Taxonomic identifier||8724 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops|
|Sequence length||37 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Met, L-Leu, L-Phe, L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, edema, apoptosis of vascular endothelial cells or tumor cell lines, 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. This protein induce hemolysis and has antibacterial and antiparasitic activities (against the Gram-positive S.aureus). Tested in vivo, this protein significantly inhibits Ehrlich ascite tumors growth and induces an influx of polymorphonuclear cells, as well as spontaneous liberation of hydrogen peroxide from peritoneal macrophages. Ref.1 Ref.2 Ref.3
An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
FAD By similarity.
Homodimer; non-covalently linked. Ref.1
Expressed by the venom gland.
Bothrops jararaca venom seems to contain 2 isoforms with different hydrophobic properties (Ref.1). These isoforms may reflect different glycosylation of the protein or they may have been synthesized from different genes.
Hemostasis impairing toxin
|Technical term||Direct protein sequencing|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: UniProtKB-KWcytolysis
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: EC
|Complete GO annotation...|
Sequence annotation (Features)
|||"Antitumoural effect of an L-amino acid oxidase isolated from Bothrops jararaca snake venom."|
de Vieira Santos M.M., Sant'Ana C.D., Giglio J.R., da Silva R.J., Sampaio S.V., Soares A.M., Fecchio D.
Basic Clin. Pharmacol. Toxicol. 102:533-542(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
|||"Antigenic, microbicidal and antiparasitic properties of an L-amino acid oxidase isolated from Bothrops jararaca snake venom."|
Ciscotto P., Machado de Avila R.A., Coelho E.A., Oliveira J., Diniz C.G., Farias L.M., de Carvalho M.A., Maria W.S., Sanchez E.F., Borges A., Chavez-Olortegui C.
Toxicon 53:330-341(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GLYCOSYLATION.
|||"L-amino acid oxidase activity present in fractions of Bothrops jararaca venom is responsible for the induction of programmed cell death in Trypanosoma cruzi."|
Deolindo P., Teixeira-Ferreira A.S., DaMatta R.A., Alves E.W.
Toxicon 56:944-955(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|Accession||Primary (citable) accession number: P0DI88|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Animal Toxin Annotation Program|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families