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P81375 (OXLA_MACLB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismMacrovipera lebetina (Levantine viper) (Vipera lebetina)
Taxonomic identifier8709 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeMacrovipera

Protein attributes

Sequence length107 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highest specificity towards L-Met, L-Trp, L-Leu followed by L-His, L-Phe, L-Arg and L-Ile, wherease L-Gly, L-Ser, L-Thr, L-Pro, L-Cys, L-Asp are not oxidized), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as antibacterial activities against both Gram-negative (E.coli) and Gram-positive (B.subtilis) bacteria, and inhibition of agonist-induced 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, edema, apoptosis, and have antiparasitic activities. Ref.2

Catalytic activity

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

Cofactor

FAD.

Subunit structure

Homodimer; non-covalently linked. Ref.2

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=0.40 mM for L-Leu Ref.2

KM=0.65 mM for L-Met

KM=0.17 mM for L-Trp

Temperature dependence:

Thermostable between 4 and 25 degrees Celsius. At -20 degrees Celsius, the remaining activity is 20%. Heating at 70 degrees Celsius inactivates the enzyme in 15 minutes.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›107›107L-amino-acid oxidase
PRO_0000099872

Regions

Nucleotide binding35 – 384FAD By similarity

Sites

Binding site381Substrate By similarity
Binding site491Substrate By similarity

Amino acid modifications

Disulfide bond10 ↔ ? By similarity

Experimental info

Non-adjacent residues27 – 282
Non-adjacent residues38 – 392
Non-adjacent residues48 – 492
Non-adjacent residues57 – 582
Non-adjacent residues67 – 682
Non-adjacent residues79 – 802
Non-adjacent residues90 – 912
Non-terminal residue1071

Sequences

Sequence LengthMass (Da)Tools
P81375 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 576D2F829779B412

FASTA10712,435
        10         20         30         40         50         60 
ADDKNPLEEC FREDDYEEFL EIAKNGLEGW YANLGPMRYP VKPSEEGKHD DIFAYEKFDE 

        70         80         90        100 
IVGGMDKKFW EDDGIHGGKE TFCYSPMIQK PYQFQHFSEA LTAPVGR 

« Hide

References

[1]Tan C.H., Ang W.C.
Submitted (MAY-1998) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-27.
Tissue: Venom.
[2]"L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteria."
Tonismagi K., Samel M., Trummal K., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.
Toxicon 48:227-237(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-107, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_MACLB
AccessionPrimary (citable) accession number: P81375
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 51 of the entry and version 2 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