X2JCV5 · OXLAA_CERCE

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:25009089).
Is highly active on L-Met>L-Leu>L-Phe>L-Trp=L-Ile (PubMed:25009089).
Binds to the cell surface and enables the production of highly localized concentration of hydrogen peroxide in or near the binding interfaces (PubMed:26433175).
Does not bind to phospholipids (PubMed:26433175).
Induces platelet-rich plasma aggregation, shows cytotoxic effects on some cancer cell lines (B16-F10 (mouse melanoma), PC12 (rat pheochromocytoma), MCF-7 and MDA-MB-231 (human breast carcinoma)) and shows antibacterial activities against both Gram-positive and Gram-negative bacteria (PubMed:26433175).
Also exhibits hemorrhage and edema (By similarity).
Does not show cytotoxicity on erythrocytes and peripheral blood mononuclear cells (PubMed:26433175).
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

Miscellaneous

Two L-amino-acid oxidase isoforms from C.cerastes venom have been described: Cc-LAAOI and Cc-LAAOII. It is unknown which isoform is presented here.

Caution

Lacks two of the six Cys residues found in other family members, resulting in the loss of one disulfide bond.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Activity regulation

Inhibited by the substrate analog N-acetyl tryptophan.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.1 mML-Met
0.25 mML-Leu
0.08 mML-Phe

pH Dependence

Optimum pH is 7.8.

Temperature Dependence

Optimum temperature is 50 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site61-62FAD (UniProtKB | ChEBI)
Binding site81-82FAD (UniProtKB | ChEBI)
Binding site89FAD (UniProtKB | ChEBI)
Binding site105-108FAD (UniProtKB | ChEBI)
Binding site108substrate
Binding site279FAD (UniProtKB | ChEBI)
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 Processdefense response to bacterium

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-amino acid oxidase
  • Alternative names
    • CC-LAAO
      (LAO) (EC:1.4.3.2
      ) . EC:1.4.3.2 (UniProtKB | ENZYME | Rhea)

Organism names

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

Accessions

  • Primary accession
    X2JCV5

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000043074919-516L-amino acid oxidase
Glycosylation190N-linked (GlcNAc...) asparagine
Glycosylation299N-linked (GlcNAc...) asparagine
Disulfide bond349↔430
Glycosylation404N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated (14%). The enzymatic activity remains unchanged after deglycosylation.

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Homodimer; non-covalently linked.

Structure

Family & Domains

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

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)
    58,557
  • Last updated
    2014-06-11 v1
  • Checksum
    41A6F22D886D0235
MNVFFMFSLLFLAALESCADDKNPLEEEFFEADYEEFLLIAKNGLQQTSNPKRVVIVGAGMSGLSAAYVLAKTGHEVILLEASERVGGRVSTYRNDQEGWYANLGPMRLPERHRIVREYIRKFGLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEKGKSAPQLYRDSLQKIIEEYGRSNCSYILNKYDTYSTKDYLIKEGNLSPGAVDMVGDLLNEDSGYYVSFIESLKPDDIFAYENRFDEIVGGFDKLPTSMYQAIQEKVRLNVRVIKIQQDVKEVTVTYQTPAKNLSYVTADYVIVCTTSGAARRIKFEPPLPLKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSITDRPSRLIHYPNHNFPNGIGVLVIFTIADDADFFLALDNKTIADIVIHDLSLIHQLPKEKIRDLCYVSMIQKWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KJ028110
EMBL· GenBank· DDBJ
AHN53388.1
EMBL· GenBank· DDBJ
mRNA

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