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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops leucurus (White-tailed jararaca) (White-tailed lancehead)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Cofactori

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:1.4.3.2)
Short name:
LAAO
Short name:
LAO
OrganismiBothrops leucurus (White-tailed jararaca) (White-tailed lancehead)
Taxonomic identifieri157295 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

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

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

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

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Fragment.

P0DI89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30
ADDRNPLEEC FRETDYEEFL EIAKNGLSTT
Length:30
Mass (Da):3,507
Last modified:September 21, 2011 - v1
Checksum:i37BCDB4946D486E0
GO

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

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Cytotoxicity and inhibition of platelet aggregation caused by an l-amino acid oxidase from Bothrops leucurus venom."
    Naumann G.B., Silva L.F., Silva L., Faria G., Richardson M., Evangelista K., Kohlhoff M., Gontijo C.M., Navdaev A., de Rezende F.F., Eble J.A., Sanchez E.F.
    Biochim. Biophys. Acta 1810:683-694(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY.
    Tissue: Venom.

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: January 7, 2015
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

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

Caution

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.