| IED ID | IndEnz0002002185 |
| Enzyme Type ID | protease002185 |
| 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 | LELG_00410 |
| Organism | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Lodderomyces Lodderomyces elongisporus Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Enzyme Sequence | MEELKAYRPKTSPELDPSTLSNYTCFTVKLTTLHFDIDFEKKIVSGKVKYDLLNKSETDHVDLDTSYLDITKVSIQNESCDNQYKLHSRKEPLGSKLHILIPASTPKNFQLEIEFSTTSKCTALQFLDKEATDGKNHPYLFCQCQAIHARSLFPSFDTPGIKSPYKFSAKSPLKTLLSGLLIKEDNENNTVYFEQPVPIPSYLVSIALGDIARTSIGPRSDVMTEPVNLAKCKWEFERDMENFIQVAEKLIFEYEWQKFDSLVLPASFPYGGMEIPNLCQLTPTLICGDRSLVNVVAHELAHSWSGNLVTNCSWEHFWLNEGWTVYLERRILEALAVIEAKQQGKGDKEAHYYGEQVRQFNAIIGWTDLENDLKSMGDNVDKYSILVQDLKGKKNPDDPDDAFSTVPYEKGFNLLYLIEKIVGKEKFDLFIPAYFREFRFKSLDTFQFIDYLFDFFKEDAVKLDQIEWKKWLYEPGMPPIDPKFDTTLAQACYDLAKKCYQYALSEDDENEFTQFKLVANEINDFSPSQNIVFLDTLIAYEKVAGFSWKQHKKTLNRMATLYHDQYTETLNAEIKFRWFYLQATGEVLDFEVAMGEFLGTIGRMKFVRPGYALLNKVNRELAVRYFQRFENRYHPICKAMVRKDLQLD |
| Enzyme Length | 648 |
| Uniprot Accession Number | A5DSS4 |
| Absorption | |
| Active Site | ACT_SITE 299; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 408; /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); Erroneous gene model prediction (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 | 75,111 |
| Kinetics | |
| Metal Binding | METAL 298; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 302; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 321; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | RHEA:19037 |
| Cross Reference Brenda |