Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0C2D7

- OXLA_VIPBB

UniProt

P0C2D7 - OXLA_VIPBB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Vipera berus berus (Common viper)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (the most specific substrate is L-Phe, followed by L-Met, L-Leu, L-Phe, L-Ile, L-Arg and L-His), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities (By similarity). In addition, this protein has an ability to induce apoptosis in cultured HeLa and K562 cells, and inhibits ADP-induced platelet aggregation dose-dependently. 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 similarity1 Publication

Catalytic activityi

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

Cofactori

FADBy similarity

Kineticsi

  1. KM=0.361 mM for L-Leu1 Publication
  2. KM=0.286 mM for L-Met1 Publication
  3. KM=0.058 mM for L-Phe1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi81 – 866FADBy similarity
Nucleotide bindingi81 – 822SubstrateBy similarity

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
Complete GO annotation...

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
OrganismiVipera berus berus (Common viper)
Taxonomic identifieri31156 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›88›88L-amino-acid oxidasePRO_0000273573Add
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

ProteinModelPortaliP0C2D7.
SMRiP0C2D7. Positions 3-37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Fragments.

P0C2D7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
ADDKNPLEEC FREDDYEEFL EIAKNGLKKT SNPKHIVYPV KPSEQLYEES
60 70 80
LRDQLPTSMH RYPSMIQKIF FAGEYTANAH GWIDSTIK
Length:88
Mass (Da):10,295
Last modified:January 23, 2007 - v1
Checksum:iD2A63168391A7965
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi37 – 382Curated
Non-adjacent residuesi44 – 452Curated
Non-adjacent residuesi52 – 532Curated
Non-adjacent residuesi61 – 622Curated
Non-adjacent residuesi68 – 692Curated
Non-terminal residuei88 – 881

Cross-referencesi

3D structure databases

ProteinModelPortali P0C2D7.
SMRi P0C2D7. Positions 3-37.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom."
    Samel M., Vija H., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.
    Biochim. Biophys. Acta 1764:707-714(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_VIPBB
AccessioniPrimary (citable) accession number: P0C2D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 32 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

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3