| IED ID | IndEnz0007000319 |
| Enzyme Type ID | catalase000319 |
| Protein Name |
L-amino acid oxidase Bs29 BsLAAO LAO EC 1.4.3.2 Fragment |
| Gene Name | |
| Organism | Bothriechis schlegelii (Eyelash palm pitviper) |
| 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) Bothriechis Bothriechis schlegelii (Eyelash palm pitviper) |
| Enzyme Sequence | SCADDRNPLEECFQETDYEEFLEIARNGLKATSNPKHVVIVGAGMSGLSAAYVLAGAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYITKFGLQLNEFSQENENAWYFIKNIRKRVGEVKKDPGLLQYPVKPSEEGKSAGQLYEESLGKVVEELKRTNCSYILDKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDNIFGYEKRFNEIVDGMDKLPTSMYQAIEEKVRFNARVIKIQQNDNEVTVTYQTSENEMSPVTADYVIVCTTSRAARRITFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFVYYPNHDFSSGSAVIMAYGIGDDANFFQALDHKDCGDTVINDLSLIHQLTKEEIQSFCYLSKIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDN |
| Enzyme Length | 498 |
| Uniprot Accession Number | A0A024BTN9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 73; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6STF1; BINDING 92; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q6STF1; BINDING 225; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q6STF1; BINDING 263; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q6STF1; BINDING 374; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q6STF1; BINDING 459; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6STF1 |
| 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:24875315}; 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:24875315}; |
| 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:24875315). Shows activity on L-Leu (PubMed:24875315). Damage cell membranes of the Gram-positive bacteria S.aureus (MIC=4 ug/ml and MBC=8 ug/ml) and the Gram-negative bacteria A.baumanni (MIC=2 ug/ml and MBC=4 ug/ml) (PubMed:24875315). This antibacterial activity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger (PubMed:24875315). {ECO:0000269|PubMed:24875315}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 45..46; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6STF1; NP_BIND 65..66; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6STF1; NP_BIND 89..92; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6STF1; NP_BIND 466..471; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q6STF1 |
| Features | Binding site (6); Chain (1); Disulfide bond (2); Glycosylation (1); Non-terminal residue (2); Nucleotide binding (4); Region (1); Signal peptide (1) |
| Keywords | Antibiotic;Antimicrobial;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24875315}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..3; /evidence=ECO:0000269|PubMed:18444672 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,376 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.37 uM for L-Leu {ECO:0000269|PubMed:24875315}; Vmax=0.39 umol/min/mg enzyme {ECO:0000269|PubMed:24875315}; |
| Metal Binding | |
| Rhea ID | RHEA:13781; RHEA:60996 |
| Cross Reference Brenda |