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P0DI88 (OXLA_BOTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=BjarLAAO-I
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops jararaca (Jararaca) (Bothrops jajaraca)
Taxonomic identifier8724 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length37 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.3

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-Glycosylated. Ref.2

Miscellaneous

Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.3 and Ref.2).

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Caution

Bothrops jararaca venom seems to contain 2 isoforms with different hydrophobic properties (Ref.1). These isoforms may reflect different glycosylation of the protein or they may have been synthesized from different genes.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›37›37L-amino-acid oxidase
PRO_0000412595

Amino acid modifications

Disulfide bond10 ↔ ? By similarity

Experimental info

Non-terminal residue371

Sequences

Sequence LengthMass (Da)Tools
P0DI88 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 9C3BDE3E1E664AE7

FASTA374,299
        10         20         30 
ADDKNPLEEC FRETDYEEFL EIARNGLKAT SNPKRVV 

« Hide

References

[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.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_BOTJA
AccessionPrimary (citable) accession number: P0DI88
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families