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P86163

- OXLA_APLDA

UniProt

P86163 - OXLA_APLDA

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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Aplysia dactylomela (Spotted sea hare)
Status
Reviewed - 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

FAD.1 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

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

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB
  2. modulation of blood coagulation in other organism Source: UniProtKB
  3. 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

Secreted 3 Publications

GO - Cellular componenti

  1. 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

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        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

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

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: October 1, 2014
This is version 5 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