| IED ID | IndEnz0002002168 |
| Enzyme Type ID | protease002168 |
| 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 | AN5812 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MATLMNPVRDPNTLSNYNNWLCTHTTANFEIFFEEKKLVGNVVHKLRSITNAETDEIILDSHHVDIRNVQVAGLPVKAWELLPPLGPYGTALKIKLENPVGLNEIIDVDIAVQTTKECTALQWLTPAQTSNKKHPYMFSQCQAIHARSIFPCQDTPDVKCTFDFNITSPLPVIASGLPVRSTSTVPQSGVKTLHRFHQKVPIPSYLFALASGDIAEAAIGPRSVVATSPDKLEECKWELEADTERFIKTIEEIIYPYAWGEYNVLILPPSFPYGGMENPVFTFATPSIISKDRENVDVIAHELAHSWSGNLVTSASWEHFWLNEGWTVYLERRILASLHGEKYRHFSAIIGWKALRDSVEHYSHDHEFTKLVPNLKGEDPDDAFSTIPYEKGFNFLFHLENLVGKEKFDRFIPHYFTTFKGKSLDSYDFKATLLDFFKSDAEASRLLQELDWDSWFYKPGLPPKPEFDTSLADVVYELAGKWRSLPESPFQPQPSDIQGLTANQIVVFLEQILLFERPLTAELSKLMGEVYGLTGSENIEVANLYLQVGLKAADKSVIGPTTDLLGRIGRMKFVRPLYRALQKVDRQVAIDTFEKHKDFYHPICRGMVEKDLFGKKDA |
| Enzyme Length | 618 |
| Uniprot Accession Number | Q5B0W8 |
| Absorption | |
| Active Site | ACT_SITE 302; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 389; /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 initiation (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 | 70,100 |
| Kinetics | |
| Metal Binding | METAL 301; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 305; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 324; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | RHEA:19037 |
| Cross Reference Brenda |