Detail Information for IndEnz0002002139
IED ID IndEnz0002002139
Enzyme Type ID protease002139
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 ATEG_06861
Organism Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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 terreus Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Enzyme Sequence MATTINPPRDPNTLSNYNNWLSTHITANFDILFDQKKLVGNVIHKLKSITNAESTDIVLDTSHVDVTDVKVDGKPSVWELLPPVKPYGTALKIKLDQGVKMDEIVHVDISVKTTEKCTALQWLTPAQTSNKKHPYMFSQCQAIHARSIFPCQDTPDVKSTIDFNITSPLPVIASGLLVRDASGAPQTGGKNLYQFHQKVPIPSYLFALASGDISEAAIGPRSVVATSPDKLRECQWELEADTENFINAIEKIVYPYVWGEYNVLILPPSFPYGGMENPIFTFATPSIISKDRENVDVIAHELAHSWSGNLVTNASWEHFWLNEGWTVYLERRILAAVHGEAYRHFSAIIGWKALSDSVDHFGHDHEFTRLITDLKGKDPDDAFSSIPYEKGFNFLFHLENLVGKQKFDQFIPHYFTKFKGKSLDSYEFKATILDFFKSDAEASKLLNELDWDTWFYAPGLPPKPKFDTSLVDVVYDLAKKWQSIPESSFKPQPSDIKDLTGNQIVVFLEQVLLFERPLAPELSKLMGEVYGLAKSANIEVANLYFRVGLNAGDESVFEPTADLLGKIGRMKFVRPLYRNLQKVNRPLAIETFEKNKDFYHPICRAMVEKDLFGKKDA
Enzyme Length 617
Uniprot Accession Number Q0CFY9
Absorption
Active Site ACT_SITE 301; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 388; /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); 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 69,701
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