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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Crotalus durissus cascavella (Northeastern Brazilian rattlesnake)
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, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as apoptosis, antibacterial activities against both Gram-negative and Gram-positive bacteria and antiparasitic activities, as well as induction 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. This protein may also induce hemorrhage, hemolysis, and edema.1 Publication

Catalytic activityi

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

Cofactori

FAD1 Publication

Kineticsi

  1. KM=46.7 µM for L-Leu1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi43 – 442FADBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation activating 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:
    Casca LAO
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiCrotalus durissus cascavella (Northeastern Brazilian rattlesnake)
    Taxonomic identifieri184540 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›61›61L-amino-acid oxidasePRO_0000273567Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP0C2D2.
    SMRiP0C2D2. Positions 3-61.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Sequencei

    Sequence statusi: Fragment.

    P0C2D2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    ADDRNPLEQC FRETDYEEFL EIARNNLKAT SNPKHVVIVG AGMAGLSAAY
    60
    VLSGGGHQVT V
    Length:61
    Mass (Da):6,561
    Last modified:January 23, 2007 - v1
    Checksum:i9D7F04E64267A122
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei61 – 611

    Cross-referencesi

    3D structure databases

    ProteinModelPortaliP0C2D2.
    SMRiP0C2D2. Positions 3-61.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    ProtoNetiSearch...

    Publicationsi

    1. Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_CRODC
    AccessioniPrimary (citable) accession number: P0C2D2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: January 23, 2007
    Last modified: January 7, 2015
    This is version 40 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 leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.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.