O93364 · OXLA_CROAD

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:6067195).
Is active on L-Arg, L-Phe, L-Met, and L-Leu and is weakly active on L-Val (PubMed:6067195).
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).

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site61-62FAD (UniProtKB | ChEBI)
Binding site81-82FAD (UniProtKB | ChEBI)
Binding site89FAD (UniProtKB | ChEBI)
Binding site103-106FAD (UniProtKB | ChEBI)
Binding site106substrate
Binding site239substrate
Binding site279FAD (UniProtKB | ChEBI)
Binding site390substrate
Binding site475FAD (UniProtKB | ChEBI)
Binding site482-483substrate
Binding site482-487FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular FunctionL-phenylalaine oxidase activity
Molecular Functiontoxin activity
Biological Processamino acid catabolic process
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
    LAAO
    ; LAO

Organism names

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

Accessions

  • Primary accession
    O93364

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000000170619-516L-amino-acid oxidase
Disulfide bond28↔189
Disulfide bond349↔430
Glycosylation379N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated.

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Homodimer; non-covalently linked.

Structure

Family & Domains

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    516
  • Mass (Da)
    58,662
  • Last updated
    1998-11-01 v1
  • Checksum
    FDFAA77A49FDA05A
MNVFFMFSLLFLAALGSCAHDRNPLEECFRETDYEEFLEIAKNGLTATSNPKRVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIKKFDLKLNEFSQENENAWYFIKNIRKRVREVKNNPGLLEYPVKPSEEGKSAAQLYVESLRKVVEELRSTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDREATVTYQTSANEMSSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHELPKEDIQTFCHPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF071564
EMBL· GenBank· DDBJ
AAC32267.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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