Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops jararaca (Jararaca) (Bothrops jajaraca)
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 (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.By similarity3 Publications

Catalytic activityi

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

Cofactori

FADBy similarity

GO - Molecular functioni

  1. L-amino-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
  3. hemolysis in other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, 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:
BjarLAAO-I
Short name:
LAAO
Short name:
LAO
OrganismiBothrops jararaca (Jararaca) (Bothrops jajaraca)
Taxonomic identifieri8724 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›37›37L-amino-acid oxidasePRO_0000412595Add
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

Homodimer; non-covalently linked.1 Publication

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Fragment.

P0DI88-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30 
ADDKNPLEEC FRETDYEEFL EIARNGLKAT SNPKRVV
Length:37
Mass (Da):4,299
Last modified:September 21, 2011 - v1
Checksum:i9C3BDE3E1E664AE7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei37 – 371

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "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.
    Tissue: Venom.
  2. "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.
    Tissue: Venom.
  3. "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.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_BOTJA
AccessioniPrimary (citable) accession number: P0DI88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: January 7, 2015
This is version 17 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

Miscellaneousi

Miscellaneous

Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (PubMed:20615423 and PubMed:19101583).

Caution

Bothrops jararaca venom seems to contain 2 isoforms with different hydrophobic properties (PubMed:18346051). These isoforms may reflect different glycosylation of the protein or they may have been synthesized 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.