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P0DI90 (OXLA2_DABRR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 9. 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 L2

Short name=LAAO
Short name=LAAO-L2
Short name=LAO
EC=1.4.3.2
OrganismDaboia russelii (Russel's viper) (Vipera russelii)
Taxonomic identifier31159 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, 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, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity.

Catalytic activity

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

Cofactor

FAD. Ref.1

Subunit structure

Monomer Probable. This is in contrast with most of its orthologs, that are non-covalently linked homodimers. Ref.1

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

N-glycosylated Probable. Ref.1

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=1.89 mM for L-Ile Ref.1

KM=599.7 µM for L-Leu

KM=222.8 µM for L-Met

KM=49.3 µM for L-Phe

KM=235.1 µM for L-Trp

KM=538.2 µM for L-Tyr

Vmax=6.94 µmol/min/mg enzyme toward L-Phe

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20L-amino-acid oxidase L2
PRO_0000412601

Amino acid modifications

Disulfide bond10 ↔ ? By similarity

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P0DI90 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 9D194277D99593E7

FASTA202,310
        10         20 
ADDKNPLEEC FCEDDDYCEG 

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References

[1]"Two L-amino acid oxidase isoenzymes from Russell's viper (Daboia russelli russelli) venom with different mechanisms of inhibition by substrate analogs."
Mandal S., Bhattacharyya D.
FEBS J. 275:2078-2095(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INHIBITION BY SUBSTRATE ANALOGS.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA2_DABRR
AccessionPrimary (citable) accession number: P0DI90
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: February 19, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families