P0DI89 · OXLA_BOTLC

Function

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 (PubMed:21539897).
Is highly active against L-Met, L-Leu, L-norleucine (L-2-aminohexanoate), L-Trp, L-Phe, moderately active against L-Tyr, and no active on L-Gly, L-Ala, L-Val, L-Pro, L-His, L-Lys, L-Arg, L-Asp, L-Asn, L-Gln, L-Glu, L-Ser, and L-Thr (PubMed:21539897).
Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities (By similarity).
In addition, this protein induces apoptosis. It also interacts with endothelial cells, and inhibits collagen- and ADP-induced platelet aggregation. L-LAAO family effects on platelets are controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions

Miscellaneous

Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.

Caution

The existence of several isoforms has been reported that may be due to either different composition or different glycosylation or by the synthesis from different genes.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

pH Dependence

Optimum pH is 7.5-8.8 for L-Leu.

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular FunctionL-phenylalaine oxidase activity
Molecular Functiontoxin activity
Biological Processapoptotic process
Biological Processdefense response to bacterium
Biological Processkilling of cells of another organism

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-amino-acid oxidase
  • EC number
  • Short names
    Bl-LAAO
    ; LAO

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Bothrops

Accessions

  • Primary accession
    P0DI89

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00004125961-30L-amino-acid oxidase
Disulfide bond10↔?

Post-translational modification

N-glycosylated.

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

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

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    30
  • Mass (Da)
    3,507
  • Last updated
    2011-09-21 v1
  • Checksum
    37BCDB4946D486E0
ADDRNPLEECFRETDYEEFLEIAKNGLSTT

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue30

Mass Spectrometry

Molecular mass is 57,000 Da. Determined by MALDI.

Keywords

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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