P0C2D2 (OXLA_CRODC) Reviewed, UniProtKB/Swiss-Prot
Last modified October 3, 2012. Version 33. History...
Names and origin
|Protein names||Recommended name:|
Short name=Casca LAO
|Organism||Crotalus durissus cascavella (Northeastern Brazilian rattlesnake)|
|Taxonomic identifier||184540 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus ›|
|Sequence length||61 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 apoptosis, antibacterial activities against both Gram-negative and Gram-positive bacteria and antiparasitic activities, as well as induction 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. This protein may also induce hemorrhage, hemolysis, and edema. Ref.1
An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Homodimer; non-covalently linked. 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).
KM=46.7 µM for L-Leu Ref.1
Optimum pH is 6.5.
Hemostasis impairing toxin
Platelet aggregation activating 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)
|||"Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom."|
Toyama M.H., Toyama Dde O., Passero L.F., Laurenti M.D., Corbett C.E., Tomokane T.Y., Fonseca F.V., Antunes E., Joazeiro P.P., Beriam L.O., Martins M.A., Monteiro H.S., Fonteles M.C.
Toxicon 47:47-57(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
|Accession||Primary (citable) accession number: P0C2D2|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Animal Toxin Annotation Program|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families