O93364 · OXLA_CROAD
- 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: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).
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
- 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-methionine + O2 + H2O = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4+
- L-arginine + O2 + H2O = 5-guanidino-2-oxopentanoate + H2O2 + NH4+
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 61-62 | FAD (UniProtKB | ChEBI) | ||||
Sequence: MA | ||||||
Binding site | 81-82 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EA | ||||||
Binding site | 89 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 103-106 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GPMR | ||||||
Binding site | 106 | substrate | ||||
Sequence: R | ||||||
Binding site | 239 | substrate | ||||
Sequence: H | ||||||
Binding site | 279 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 390 | substrate | ||||
Sequence: Y | ||||||
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 | 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 namesLAAO ; LAO
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Crotalus
Accessions
- Primary accessionO93364
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MNVFFMFSLLFLAALGSC | ||||||
Chain | PRO_0000001706 | 19-516 | L-amino-acid oxidase | |||
Sequence: AHDRNPLEECFRETDYEEFLEIAKNGLTATSNPKRVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIKKFDLKLNEFSQENENAWYFIKNIRKRVREVKNNPGLLEYPVKPSEEGKSAAQLYVESLRKVVEELRSTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDREATVTYQTSANEMSSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHELPKEDIQTFCHPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEF | ||||||
Disulfide bond | 28↔189 | |||||
Sequence: CFRETDYEEFLEIAKNGLTATSNPKRVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIKKFDLKLNEFSQENENAWYFIKNIRKRVREVKNNPGLLEYPVKPSEEGKSAAQLYVESLRKVVEELRSTNC | ||||||
Disulfide bond | 349↔430 | |||||
Sequence: CTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHELPKEDIQTFC | ||||||
Glycosylation | 379 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
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)58,662
- Last updated1998-11-01 v1
- ChecksumFDFAA77A49FDA05A
Keywords
- Technical term