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L-amino-acid oxidase L1

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.By similarity


FAD1 Publication


  1. KM=0.297 mM for L-Met1 Publication
  2. KM=1.44 mM for L-Ile1 Publication
  3. KM=0.750 mM for L-Leu1 Publication
  4. KM=0.066 mM for L-Phe1 Publication
  5. KM=0.210 mM for L-Trp1 Publication
  6. KM=0.052 mM for L-Tyr1 Publication
  1. Vmax=8.96 µmol/min/mg enzyme toward L-Phe1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase L1 (EC:
Short name:
LAAOBy similarity
Short name:
Short name:
LAO1 Publication
OrganismiDaboia russelii (Russel's viper) (Vipera russelii)
Taxonomic identifieri31159 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›20›20L-amino-acid oxidase L1PRO_0000394725Add

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi10 ↔ ?By similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein


Tissue specificityi

Expressed by the venom gland.2 Publications


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

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.Sequence analysis


Sequence statusi: Fragment.

P86535-1 [UniParc]FASTAAdd to basket

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        10         20
Mass (Da):2,519
Last modified:September 21, 2011 - v2

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41I → K AA sequence (PubMed:20203422).Curated
Sequence conflicti7 – 71K → L AA sequence (PubMed:20203422).Curated
Sequence conflicti12 – 121F → R AA sequence (PubMed:20203422).Curated
Sequence conflicti17 – 171Y → E AA sequence (PubMed:20203422).Curated
Non-terminal residuei20 – 201


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases


Entry informationi

Entry nameiOXLA1_DABRR
AccessioniPrimary (citable) accession number: P86535
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: September 21, 2011
Last modified: January 7, 2015
This is version 19 of the entry and version 2 of the sequence. [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

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.