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L-amino-acid oxidase L2

Daboia russelii (Russel's viper) (Vipera russelii)
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli


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).By similarity

Catalytic activityi

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


FAD1 Publication


  1. KM=1.89 mM for L-Ile1 Publication
  2. KM=599.7 µM for L-Leu1 Publication
  3. KM=222.8 µM for L-Met1 Publication
  4. KM=49.3 µM for L-Phe1 Publication
  5. KM=235.1 µM for L-Trp1 Publication
  6. KM=538.2 µM for L-Tyr1 Publication
  1. Vmax=6.94 µmol/min/mg enzyme toward L-Phe1 Publication

GO - Molecular functioni

GO - Biological processi


Molecular functionAntibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Toxin
Biological processApoptosis, Cytolysis, Hemolysis
LigandFAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase L2 (EC:
Short name:
Short name:
Short name:
OrganismiDaboia russelii (Russel's viper) (Vipera russelii)
Taxonomic identifieri31159 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004126011 – ›20L-amino-acid oxidase L2Add BLAST›20

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi10 ↔ ?By similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein


Tissue specificityi

Expressed by the venom gland.1 Publication


Subunit structurei

Monomer (Probable). This is in contrast with most of its orthologs, that are non-covalently linked homodimers.Curated1 Publication

Family & Domainsi

Sequence similaritiesi


Sequence statusi: Fragment.

P0DI90-1 [UniParc]FASTAAdd to basket

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        10         20
Mass (Da):2,310
Last modified:September 21, 2011 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei201

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiOXLA2_DABRR
AccessioniPrimary (citable) accession number: P0DI90
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: January 7, 2015
This is version 13 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program


Keywords - Technical termi

Direct protein sequencing


  1. SIMILARITY comments
    Index of protein domains and families