| IED ID | IndEnz0007000119 |
| Enzyme Type ID | catalase000119 |
| Protein Name |
L-amino acid oxidase Cdc18 CdcLAAO LAO EC 1.4.3.2 Fragment |
| Gene Name | |
| Organism | Crotalus durissus cumanensis (South American rattlesnake) |
| 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) Crotalus Crotalus durissus (tropical rattlesnake) Crotalus durissus cumanensis (South American rattlesnake) |
| Enzyme Sequence | SCADDRNPLEECFRETDYEEFLEIARNGLTVTSNPKHVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIRKFGLQLNEFFQENENAWYFIKNIRKRVREVKNNPGILEYPVKPSEEGKSAAQLYVESLRKVVKELKRTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDRETKVTYQTSANEMPSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCKRKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQLPKEDIQTFCRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDN |
| Enzyme Length | 498 |
| Uniprot Accession Number | K9N7B7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 73; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 90; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 223; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 263; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 374; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 459; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382 |
| 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:23287728}; 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:23287728}; |
| 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:23287728). Shows activity on L-Leu (PubMed:23287728). Damages cell membranes of the Gram-positive bacteria S.aureus (MIC=8 ug/ml and MBC=16 ug/ml) and the Gram-negative bacteria A.baumannii (MIC=16 ug/ml and MBC=32 ug/ml). This antimicrobial activity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger. {ECO:0000269|PubMed:23287728}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 45..46; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 65..66; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 87..90; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 466..471; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382 |
| Features | Binding site (6); Chain (1); Disulfide bond (2); Glycosylation (1); Non-terminal residue (1); 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:19863078}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..2; /evidence=ECO:0000269|PubMed:19863078 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,827 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.23 uM for L-Leu {ECO:0000269|PubMed:23287728}; Vmax=0.46 uM/min/mg enzyme for L-Leu {ECO:0000269|PubMed:23287728}; |
| Metal Binding | |
| Rhea ID | RHEA:13781; RHEA:60996 |
| Cross Reference Brenda |