| IED ID | IndEnz0002002202 |
| Enzyme Type ID | protease002202 |
| Protein Name |
Leucine aminopeptidase EC 3.4.11.- Epoxide hydrolase EC 3.3.2.10 Leukotriene A-4 hydrolase homolog LTA-4 hydrolase |
| Gene Name | LKHA4 Os03g0819100 LOC_Os03g60460 OJ1754_E06.9 OsJ_13129 |
| Organism | Oryza sativa subsp. japonica (Rice) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice) |
| Enzyme Sequence | MPPVDPHSYTDGDHPVTAKAALAFYLDFAASTIHASALLTLSAPHSGDLLLDTRALAVHSASTASGPPSPIPFSLADAADPVLGSALTLTLPPDTTSFLLTFSTSPSASALQWLSPPQTASSLPFVFSQCQSIHARSVFPCHDTPAARITFDLLLNVPTQLSAVAAARHVSRRDPLPSDHRGACDDALWCAPGRIVEEFQMEQSVPPYLFAFAAGGIGFRDLGPRTRVYAEGGDKVLDEAAREFAGVEEMVKVGESLFGPYEWERFDLLVLPPSFPYGGMENPRMVFLTPTVIKGDAAGAQVVAHELAHSWTGNLITNKTNEDFWLNEGFTTYAERRIVEVVQGEERAALNMGIGWRGLNRMMERFKDNMEYTKLKPKMAGIDPDDVYSEVPYEKGFQFLWRIERQIGRPAFDEFLKNYISTFKFKSIDTETFLEFLKTNVPGIENQIDLQLWIEGTGIPPDAMEPESAIYKKICSLAAEFKSGKLPSEDEVADWSGQEWELYLENLPTDVEASQVTALDERYKLSESCDYEVKVAFLQLAIPTGCRCYFNEVEKCLKQVGRMKYLRPLYSSLARCSGEEKMLAHRIFSEAHEFYHPIARSVAESILSKHG |
| Enzyme Length | 611 |
| Uniprot Accession Number | Q84TA3 |
| Absorption | |
| Active Site | ACT_SITE 306; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 393; /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 (3); Sequence conflict (1) |
| Keywords | Cytoplasm;Hydrolase;Leukotriene biosynthesis;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 67,792 |
| Kinetics | |
| Metal Binding | METAL 305; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 309; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 328; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | RHEA:19037 |
| Cross Reference Brenda |