| IED ID | IndEnz0007000130 |
| Enzyme Type ID | catalase000130 |
| Protein Name |
L-amino acid oxidase Bpic-LAAO LAO EC 1.4.3.2 Fragment |
| Gene Name | |
| Organism | Bothrops pictus (Desert lancehead) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Bothrops Bothrops pictus (Desert lancehead) |
| Enzyme Sequence | SLLFLAAVGSCADDRNPLEECFRETDYEEFLEIAKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIKKFDLRLNEFSQENENAWYFLQNIKKRVREVNKDPGVLEYPVKPSEVGKSAGQLYEESLRKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARVIEIQQDVKEVTVTYQTSQKETLSVTADYVIVCTTSRAARRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAICRPSMIQRWSLDNYAMGGITTFTPYHFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLRAATDVNRASENK |
| Enzyme Length | 498 |
| Uniprot Accession Number | X2L4E2 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by glutathione, and moderately inhibited by PMSF, acetate iodine and glutamic acid. Is also inhibited by Zn(2+) ions, but not by Ca(2+), Mg(2+) and Mn(2+). {ECO:0000269|PubMed:29024770}. |
| Binding Site | BINDING 82; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6TGQ9; BINDING 101; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 234; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 272; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q6TGQ9; BINDING 383; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 468; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6TGQ9 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:29024770}; CATALYTIC ACTIVITY: Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:29024770}; |
| DNA Binding | |
| EC Number | 1.4.3.2 |
| Enzyme 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 (By similarity). This enyzme shows activity on L-Leu (PubMed:29024770). This enzyme inhibits platelet aggregation in human platelet rich plasma induced by ADP (IC(50)=3.2 mg/mL), and shows antibacterial activities on both Gram-positive and Gram-negative bacteria (P.aeruginosa, V.cholerae, S.aureus, E.faecalis and E.coli) (PubMed:29024770). These two effects are due to hydrogen peroxide, since they are inhibited by catalase (PubMed:29024770). It also induces edema in mouse paw pads but does not show hemolytic activity (PubMed:29024770). This protein may also have activities in hemorrhage, and apoptosis (By similarity). {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:29024770}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35-45 degrees Celsius. {ECO:0000269|PubMed:29024770}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-10.0. {ECO:0000269|PubMed:29024770}; |
| Pathway | |
| nucleotide Binding | NP_BIND 54..55; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6TGQ9; NP_BIND 74..78; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6TGQ9; NP_BIND 74..75; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 98..101; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6TGQ9; NP_BIND 475..480; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 476..480; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6TGQ9 |
| Features | Binding site (6); Chain (1); Disulfide bond (2); Glycosylation (1); Non-terminal residue (2); Nucleotide binding (6); Region (1); Signal peptide (1) |
| Keywords | Antibiotic;Antimicrobial;Apoptosis;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemostasis impairing toxin;Oxidoreductase;Platelet aggregation inhibiting toxin;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29024770}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. Contains 18.73% carbohydrates. {ECO:0000305|PubMed:29024770}. |
| Signal Peptide | SIGNAL <1..11; /evidence=ECO:0000269|PubMed:29024770 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,349 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:13781; RHEA:60996 |
| Cross Reference Brenda |