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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Aplysia dactylomela (Spotted sea hare)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative deamination of positively charged L-amino acids L-Lys and L-Arg but not of amino acids L-His, L-Asp or L-Glu. Has antibacterial activity against the Gram-positive bacterium S.aureus (MIC=15 µg/ml). This antibacterial activity is bacteriostatic in the absence of amino acids L-Lys or L-Arg but bactericidal in their presence. The antibacterial effect is largely dependent on H2O2 produced in the oxidative deamination of substrates. Has hemagglutinating activity towards rabbit erythrocytes. Hemagglutinating activity is inhibited by the glycoprotein fetuin, but not by glucose, mannose, galactose, N-acetylglucosamine, N-acetylgalactosamine or sialic acid.2 Publications

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

Cofactori

FAD1 Publication

Kineticsi

  1. KM=0.22 mM for L-Lys1 Publication
  2. KM=0.015 mM for L-Arg1 Publication

    pH dependencei

    Optimum pH is 8. More than 50% activity is retained between pH 3 and 12. Inactive at pH 2.1 Publication

    Temperature dependencei

    Activity remains stable after 30 min at 55 degrees Celsius.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • defense response to bacterium Source: UniProtKB
    • modulation of blood coagulation in other organism Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemagglutinin, Oxidoreductase, Toxin

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidaseBy similarity (EC:1.4.3.21 Publication)
    Short name:
    LAAOBy similarity
    Short name:
    LAOBy similarity
    Alternative name(s):
    Dactylomelin-P1 Publication
    OrganismiAplysia dactylomela (Spotted sea hare)
    Taxonomic identifieri144766 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›26›26L-amino-acid oxidasePRO_0000413471Add
    BLAST

    Post-translational modificationi

    Not glycosylated.2 Publications

    Expressioni

    Tissue specificityi

    Expressed by the ink gland.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family.Sequence Analysis

    Sequencei

    Sequence statusi: Fragment.

    P86163-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20 
    DGVCSNRRQC NKEVCGSSYD VAIVGA
    Length:26
    Mass (Da):2,731
    Last modified:October 19, 2011 - v1
    Checksum:i9B38D1C8D14C510E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei26 – 2611 Publication

    Cross-referencesi

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    ProtoNetiSearch...

    Publicationsi

    1. "Further characterization and mode of action of dactylomelin-P, an antibacterial protein isolated from the ink of the sea hare Aplysia dactylomela (Rang, 1828)."
      Tavares T.C.L., Nogueira V.L.R., Vasconcelos I.M., Gomes V.M., da Cunha M., Carvalho A.F.U., Melo V.M.M.
      J. Exp. Mar. Biol. Ecol. 0:0-0(2011)
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
      Tissue: Ink1 Publication.
    2. "Purification of a novel antibacterial and haemagglutinating protein from the purple gland of the sea hare, Aplysia dactylomela rang, 1828."
      Melo V.M.M., Duarte A.B.G., Carvalho A.F.F.U., Siebra E.A., Vasconcelos I.M.
      Toxicon 38:1415-1427(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ABSENCE OF GLYCOSYLATION.
      Tissue: Ink1 Publication.
    3. "Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californica."
      Yang H., Johnson P.M., Ko K.C., Kamio M., Germann M.W., Derby C.D., Tai P.C.
      J. Exp. Biol. 208:3609-3622(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF GLYCOSYLATION.
    4. "Packaging of chemicals in the defensive secretory glands of the sea hare Aplysia californica."
      Johnson P.M., Kicklighter C.E., Schmidt M., Kamio M., Yang H., Elkin D., Michel W.C., Tai P.C., Derby C.D.
      J. Exp. Biol. 209:78-88(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Ink1 Publication.

    Entry informationi

    Entry nameiOXLA_APLDA
    AccessioniPrimary (citable) accession number: P86163
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: October 19, 2011
    Last modified: November 26, 2014
    This is version 6 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    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.