P0DI86 (OXLA_RHIAN) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 11. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Rhinocerophis alternatus (Urutu) (Bothrops alternatus)|
|Taxonomic identifier||64174 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops|
|Sequence length||18 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 slight hemorrhage, induction of platelet aggregation, edema in the mouse paw and bactericidal activity against both Gram-positive (S.aureus) and Gram-negative (E.coli) bacteria. May also induce hemolysis, apoptosis of vascular endothelial cells or tumor cell lines, and may have antiparasitic activities. 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. Ref.1
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. Ref.1
Contains 2 disulfide bonds By similarity.
N-glycosylated Probable. The enzymatic activity is not affected by deglycosylation. Ref.1
The existence of several isoforms has been reported (Ref.1) that may be due to either different composition or different glycosylation or by the synthesis from different genes.
Hemostasis impairing toxin
Platelet aggregation activating 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)
|||"Platelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Bothrops alternatus snake venom."|
Stabeli R.G., Marcussi S., Carlos G.B., Pietro R.C., Selistre-de-Araujo H.S., Giglio J.R., Oliveira E.B., Soares A.M.
Bioorg. Med. Chem. 12:2881-2886(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
|Accession||Primary (citable) accession number: P0DI86|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Animal Toxin Annotation Program|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families