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P0DI89

- OXLA_BOTLC

UniProt

P0DI89 - OXLA_BOTLC

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops leucurus (White-tailed jararaca) (White-tailed lancehead)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    FAD.By similarity

    pH dependencei

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

    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

    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

    1. extracellular region Source: UniProtKB-SubCell

    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

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    ADDRNPLEEC FRETDYEEFL EIAKNGLSTT                         30
    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

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    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: October 1, 2014
    This is version 10 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