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P86535 (OXLA1_DABRR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 15. 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 L1

Short name=LAAO
Short name=LAAO-L1
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. UniProtKB P81375

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. UniProtKB P81375

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 Ref.2.

Tissue specificity

Expressed by the venom gland. Ref.1 Ref.2

Post-translational modification

N-glycosylated Probable. Ref.1

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.297 mM for L-Met Ref.1

KM=1.44 mM for L-Ile

KM=0.750 mM for L-Leu

KM=0.066 mM for L-Phe

KM=0.210 mM for L-Trp

KM=0.052 mM for L-Tyr

Vmax=8.96 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 L1
PRO_0000394725

Amino acid modifications

Disulfide bond10 ↔ ? By similarity UniProtKB Q90W54

Experimental info

Sequence conflict41I → K AA sequence Ref.2
Sequence conflict71K → L AA sequence Ref.2
Sequence conflict121F → R AA sequence Ref.2
Sequence conflict171Y → E AA sequence Ref.2
Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P86535 [UniParc].

Last modified September 21, 2011. Version 2.
Checksum: 999C77D7C86348E7

FASTA202,519
        10         20 
ADDINPKEEC FFEDDYYEFE 

« Hide

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.
[2]"Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka."
Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G., Athauda S.B., Moriyama A.
Biomed. Res. 31:71-81(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-19, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA1_DABRR
AccessionPrimary (citable) accession number: P86535
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: September 21, 2011
Last modified: February 19, 2014
This is version 15 of the entry and version 2 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