P0DI89 · OXLA_BOTLC
- ProteinL-amino-acid oxidase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
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
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.
Catalytic activity
- an L-alpha-amino acid + O2 + H2O = a 2-oxocarboxylate + H2O2 + NH4+
- L-leucine + O2 + H2O = 4-methyl-2-oxopentanoate + H2O2 + NH4+
- L-phenylalanine + O2 + H2O = 3-phenylpyruvate + H2O2 + NH4+
- L-tryptophan + O2 + H2O = indole-3-pyruvate + H2O2 + NH4+
- L-methionine + O2 + H2O = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4+
- L-2-aminohexanoate + O2 + H2O = 2-oxohexanoate + H2O2 + NH4+
- L-tyrosine + O2 + H2O = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4+
Cofactor
pH Dependence
Optimum pH is 7.5-8.8 for L-Leu.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | L-phenylalaine oxidase activity | |
Molecular Function | toxin activity | |
Biological Process | apoptotic process | |
Biological Process | defense response to bacterium | |
Biological Process | killing of cells of another organism |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-amino-acid oxidase
- EC number
- Short namesBl-LAAO ; LAO
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Bothrops
Accessions
- Primary accessionP0DI89
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000412596 | 1-30 | L-amino-acid oxidase | |||
Sequence: ADDRNPLEECFRETDYEEFLEIAKNGLSTT | ||||||
Disulfide bond | 10↔? | |||||
Sequence: ADDRNPLEE |
Post-translational modification
N-glycosylated.
Keywords
- PTM
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
Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Family and domain databases
Sequence
- Sequence statusFragment
- Length30
- Mass (Da)3,507
- Last updated2011-09-21 v1
- Checksum37BCDB4946D486E0
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 30 | |||||
Sequence: T |
Mass Spectrometry
Keywords
- Technical term