| IED ID | IndEnz0007000364 |
| Enzyme Type ID | catalase000364 |
| Protein Name |
L-amino-acid oxidase BatroxLAAO LAO EC 1.4.3.2 |
| Gene Name | |
| Organism | Bothrops atrox (Barba amarilla) (Fer-de-lance) |
| 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 atrox (Barba amarilla) (Fer-de-lance) |
| Enzyme Sequence | MNVFFTFSLLFLAALGSCADDRNPLEECFRETDYEEFLEIAKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIRKFDLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEVGKSAGQLYEESLQKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARVIKIQQDVKEVTVTYQTSEKETLSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAICRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNRASEIKK |
| Enzyme Length | 506 |
| Uniprot Accession Number | P0CC17 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 62; /note=FAD; /evidence=ECO:0007744|PDB:5TS5; BINDING 89; /note=FAD; /evidence=ECO:0007744|PDB:5TS5; BINDING 108; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 241; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 279; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0007744|PDB:5TS5; BINDING 390; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 475; /note=FAD; /evidence=ECO:0007744|PDB:5TS5 |
| 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:18804547}; 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:18804547}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:18804547}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:18804547}; CATALYTIC ACTIVITY: Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:18804547}; CATALYTIC ACTIVITY: Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:18804547}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:18804547}; |
| 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 (PubMed:18804547). Shows high catalytic activity against L-Met, L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile (PubMed:18804547). Shows no or weak activity on L-Cys, L-Val, L-Gln, L-Thr, L-Ser, L-Lys, L-Arg, L-Asn, L-Glu, L-Gly, L-Pro, L-Asp and L-His (PubMed:18804547). Induces platelet aggregation in platelet-rich plasma, probably due to hydrogen peroxide production, since catalase inhibits aggregation effect (PubMed:18804547). Induces moderate mouse paw edema (PubMed:18804547). Induces apoptosis and shows cytotoxicity against several cancer cell lines, which is inhibited by catalase (PubMed:18804547, PubMed:21300133). Shows hemolytic activity and antibacterial activities against both Gram-positive and Gram-negative bacteria (PubMed:21300133). Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (PubMed:21300133). Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage (with 50 ug of enzyme) (PubMed:18804547). {ECO:0000269|PubMed:18804547, ECO:0000269|PubMed:21300133}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 61..62; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 81..82; /note=FAD; /evidence=ECO:0007744|PDB:5TS5; NP_BIND 105..108; /note=FAD; /evidence=ECO:0007744|PDB:5TS5; NP_BIND 482..487; /note=FAD; /evidence=ECO:0007744|PDB:5TS5 |
| Features | Beta strand (21); Binding site (7); Chain (1); Disulfide bond (2); Glycosylation (1); Helix (26); Metal binding (9); Nucleotide binding (4); Region (1); Sequence conflict (8); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Apoptosis;Cytolysis;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemolysis;Hemostasis impairing toxin;Metal-binding;Oxidoreductase;Platelet aggregation activating toxin;Secreted;Signal;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18804547}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:18804547 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5TS5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,408 |
| Kinetics | |
| Metal Binding | METAL 36; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:28137621, ECO:0007744|PDB:5TS5"; METAL 111; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:28137621, ECO:0007744|PDB:5TS5"; METAL 118; /note="Zinc 3"; /evidence="ECO:0000269|PubMed:28137621, ECO:0007744|PDB:5TS5"; METAL 150; /note="Zinc 4"; /evidence="ECO:0007744|PDB:5TS5"; METAL 219; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:28137621, ECO:0007744|PDB:5TS5"; METAL 248; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:28137621, ECO:0007744|PDB:5TS5"; METAL 299; /note="Zinc 4"; /evidence="ECO:0000269|PubMed:28137621, ECO:0007744|PDB:5TS5"; METAL 332; /note="Zinc"; /evidence="ECO:0000269|PubMed:28137621"; METAL 458; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:28137621, ECO:0007744|PDB:5TS5" |
| Rhea ID | RHEA:13781; RHEA:60996; RHEA:61240; RHEA:61244; RHEA:61236; RHEA:61232; RHEA:61248 |
| Cross Reference Brenda | 1.4.3.2; |