| IED ID | IndEnz0007000358 |
| Enzyme Type ID | catalase000358 |
| Protein Name |
L-amino acid oxidase Lm29 LmLAAO LAO EC 1.4.3.2 |
| Gene Name | |
| Organism | Lachesis muta (South American bushmaster) |
| 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) Lachesis Lachesis muta (South American bushmaster) |
| Enzyme Sequence | MNVFFMFSLLFLAALGSCADDRNPLGECFRETDYEEFLEIAKNGLRATSNPKHVVIVGAGMSGLSAAYVLAEAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFHQENDNAWHFIKNIRKRVGEVKEDPGLLQYPVKPSEEGKSAGQLYEESLGKVAEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVDGMDKLPTSMYQAIKEKVRFNARVIKIQQNDREVTVTYQTSANEMSPVTADYVIVCTTSRATRRITFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCGDIVINDLSLIHQLPKKDIQTFCYPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEL |
| Enzyme Length | 516 |
| Uniprot Accession Number | J7H670 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 89; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; 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:0000250|UniProtKB:P81382; BINDING 390; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P81382; BINDING 475; /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:22963728}; 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:22963728}; 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:22963728}; 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:22963728}; 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:22963728}; 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:22963728}; 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:22963728}; |
| 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:22963728). Is highly active on L-Met=L-Leu>>L-Phe>L-Trp>L-Tyr>L-Ile, and weakly or not active on L-His, L-Arg, L-Val, L-Gln, L-Thr, L-Lys, and L-Ser (PubMed:22963728). Exhibits a low myotoxicity (a mild myonecrosis is observed after injection in mice quadriceps muscle) (PubMed:22963728). In vitro, is cytotoxic to a lot of human cell lines, including AGS (IC(50)=22.7 ug/ml), MCF-7 (IC(50)=1.4 ug/ml), HL-60, HeLa and Jurkat cells, as well as to the parasite Leishmania brasiliensis (IC(50)=2.22 ug/ml) (PubMed:22963728). This cytotoxicity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger (PubMed:22963728). {ECO:0000269|PubMed:22963728}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4 degrees Celsius. {ECO:0000269|PubMed:22963728}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for L-Leu. {ECO:0000269|PubMed:22963728}; |
| Pathway | |
| nucleotide Binding | NP_BIND 61..62; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 81..82; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 105..108; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382; NP_BIND 482..487; /note=FAD; /evidence=ECO:0000250|UniProtKB:P81382 |
| Features | Binding site (6); Chain (1); Disulfide bond (2); Glycosylation (2); Nucleotide binding (4); Region (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Myotoxin;Oxidoreductase;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22963728}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:22963728 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,532 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.97 mM for L-Leu {ECO:0000269|PubMed:22963728}; Vmax=0.063 umol/min/mg enzyme for L-Leu {ECO:0000269|PubMed:22963728}; |
| Metal Binding | |
| Rhea ID | RHEA:13781; RHEA:60996; RHEA:61240; RHEA:61244; RHEA:61236; RHEA:61232; RHEA:61248 |
| Cross Reference Brenda |