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L-amino-acid oxidase

Bothrops leucurus (Whitetail lancehead)
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli


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.By similarity1 Publication

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.


FADBy similarity

pH dependencei

Optimum pH is 7.5-8.8 for L-Leu.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation inhibiting toxin, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:
Short name:
Short name:
OrganismiBothrops leucurus (Whitetail lancehead)
Taxonomic identifieri157295 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›30›30L-amino-acid oxidasePRO_0000412596Add

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi10 ↔ ?By similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein


Tissue specificityi

Expressed by the venom gland.


Subunit structurei

Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers.1 Publication

Family & Domainsi

Sequence similaritiesi


Sequence statusi: Fragment.

P0DI89-1 [UniParc]FASTAAdd to basket

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        10         20         30
Mass (Da):3,507
Last modified:September 21, 2011 - v1

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei30 – 301

Mass spectrometryi

Molecular mass is 57000 Da from positions 1 - ?. Determined by MALDI. 1 Publication


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases


Entry informationi

Entry nameiOXLA_BOTLC
AccessioniPrimary (citable) accession number: P0DI89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: December 9, 2015
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program



Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.1 Publication


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.1 Publication

Keywords - Technical termi

Direct protein sequencing


  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.