X2JCV5 · OXLAA_CERCE
- ProteinL-amino acid oxidase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids516 (go to sequence)
- 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: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
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.
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-isoleucine + O2 + H2O = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4+
Cofactor
Activity regulation
Inhibited by the substrate analog N-acetyl tryptophan.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.1 mM | L-Met | |||||
0.25 mM | L-Leu | |||||
0.08 mM | L-Phe |
pH Dependence
Optimum pH is 7.8.
Temperature Dependence
Optimum temperature is 50 degrees Celsius.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 61-62 | FAD (UniProtKB | ChEBI) | ||||
Sequence: MS | ||||||
Binding site | 81-82 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EA | ||||||
Binding site | 89 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 105-108 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GPMR | ||||||
Binding site | 108 | substrate | ||||
Sequence: R | ||||||
Binding site | 279 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 475 | FAD (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 482-483 | substrate | ||||
Sequence: GW | ||||||
Binding site | 482-487 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GWIDST |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | L-phenylalaine oxidase activity | |
Molecular Function | toxin activity | |
Biological Process | amino acid catabolic process | |
Biological Process | defense response to bacterium |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-amino acid oxidase
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Viperinae > Cerastes
Accessions
- Primary accessionX2JCV5
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MNVFFMFSLLFLAALESC | ||||||
Chain | PRO_0000430749 | 19-516 | L-amino acid oxidase | |||
Sequence: ADDKNPLEEEFFEADYEEFLLIAKNGLQQTSNPKRVVIVGAGMSGLSAAYVLAKTGHEVILLEASERVGGRVSTYRNDQEGWYANLGPMRLPERHRIVREYIRKFGLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEKGKSAPQLYRDSLQKIIEEYGRSNCSYILNKYDTYSTKDYLIKEGNLSPGAVDMVGDLLNEDSGYYVSFIESLKPDDIFAYENRFDEIVGGFDKLPTSMYQAIQEKVRLNVRVIKIQQDVKEVTVTYQTPAKNLSYVTADYVIVCTTSGAARRIKFEPPLPLKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSITDRPSRLIHYPNHNFPNGIGVLVIFTIADDADFFLALDNKTIADIVIHDLSLIHQLPKEKIRDLCYVSMIQKWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEL | ||||||
Glycosylation | 190 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 299 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 349↔430 | |||||
Sequence: CTKKFWEDDGIHGGKSITDRPSRLIHYPNHNFPNGIGVLVIFTIADDADFFLALDNKTIADIVIHDLSLIHQLPKEKIRDLC | ||||||
Glycosylation | 404 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated (14%). The enzymatic activity remains unchanged after deglycosylation.
Keywords
- PTM
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
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length516
- Mass (Da)58,557
- Last updated2014-06-11 v1
- Checksum41A6F22D886D0235
Keywords
- Technical term