| IED ID | IndEnz0002002137 |
| Enzyme Type ID | protease002137 |
| Protein Name |
Leucine aminopeptidase 2 EC 3.4.11.- Epoxide hydrolase EC 3.3.2.10 Leukotriene A-4 hydrolase homolog LTA-4 hydrolase |
| Gene Name | AO090011000940 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MATVIHSPRDPNTLSNYNNWVSTHITATFDILFEQKKLVGNVVHKLKSITDARSTEIILDTNHVDIGDVKVDGQASHWELLPPLEPYGAALKINLDQGVGLNEMVEVEISVKTTEKCTALQWLTPAQTSNRKHPYMFSQCQAIHARSIFPCQDTPDVKSTIDFNITSPLPVVASGLPVRGIIEKAQPGSKTLYQFHQKLPIPSYLFALASGDISEAAIGPRSVVATSPDKLSECQWELKADTENFIHAIEKIVYPYAWGEYNVLILPPSFPYGGMENPIFTFATPSIISKDRENVDVIAHELAHSWSGNLVTNASWEHFWLNEGWTTYLERRVSLHGEAYRHFSAIIGWKSLADSVEHFGHDHPFTKLVTDLKGKDPDDAFSSIPYEKGFNFLFHLENLLAKDKFDRFIPHYFTKFKGKSLDSYEFKATMLEFFQHDLEASNLLKNVDWDAWFYAPGLPPKPQFDTSLVDVVYELSSKWKSLPDSSFQPRTSDIEGLTANQIVVLLEQILLFERPLTPELSRVLGEVYSLAKSENIEVSNLYFQVGLRAGDDTVYKPTAELLGKIGRMKFVRPLYRNLQKVNRPLAIETFEKNKDFYHPICRAMVEKDLFGKREE |
| Enzyme Length | 615 |
| Uniprot Accession Number | Q2TZ99 |
| Absorption | |
| Active Site | ACT_SITE 301; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 386; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence={ECO:0000250|UniProtKB:Q10740}; |
| DNA Binding | |
| EC Number | 3.4.11.-; 3.3.2.10 |
| Enzyme Function | FUNCTION: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro). {ECO:0000250|UniProtKB:Q10740}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (3); Region (2) |
| Keywords | Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10740}. Nucleus {ECO:0000250|UniProtKB:Q10740}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,817 |
| Kinetics | |
| Metal Binding | METAL 300; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 304; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 323; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | RHEA:19037 |
| Cross Reference Brenda |