Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C2D7 (OXLA_VIPBB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismVipera berus berus (Common viper)
Taxonomic identifier31156 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

Protein attributes

Sequence length88 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.361 mM for L-Leu Ref.1

KM=0.286 mM for L-Met

KM=0.058 mM for L-Phe

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›88›88L-amino-acid oxidase
PRO_0000273573

Regions

Nucleotide binding81 – 866FAD By similarity
Nucleotide binding81 – 822Substrate By similarity

Sites

Binding site741FAD By similarity

Amino acid modifications

Disulfide bond10 ↔ ? By similarity

Experimental info

Non-adjacent residues37 – 382
Non-adjacent residues44 – 452
Non-adjacent residues52 – 532
Non-adjacent residues61 – 622
Non-adjacent residues68 – 692
Non-terminal residue881

Sequences

Sequence LengthMass (Da)Tools
P0C2D7 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: D2A63168391A7965

FASTA8810,295
        10         20         30         40         50         60 
ADDKNPLEEC FREDDYEEFL EIAKNGLKKT SNPKHIVYPV KPSEQLYEES LRDQLPTSMH 

        70         80 
RYPSMIQKIF FAGEYTANAH GWIDSTIK 

« Hide

References

[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, MASS SPECTROMETRY, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Venom.

Cross-references

3D structure databases

ProteinModelPortalP0C2D7.
SMRP0C2D7. Positions 3-37.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_VIPBB
AccessionPrimary (citable) accession number: P0C2D7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families