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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


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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003947251 – ›20L-amino-acid oxidase L1Add 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.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)DescriptionActionsGraphical viewLength
Sequence conflicti4I → K AA sequence (PubMed:20203422).Curated1
Sequence conflicti7K → L AA sequence (PubMed:20203422).Curated1
Sequence conflicti12F → R AA sequence (PubMed:20203422).Curated1
Sequence conflicti17Y → E AA sequence (PubMed:20203422).Curated1
Non-terminal residuei201

Similar proteinsi

Entry informationi

Entry nameiOXLA1_DABRR
AccessioniPrimary (citable) accession number: P86535
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: September 21, 2011
Last modified: November 22, 2017
This is version 20 of the entry and version 2 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