Detail Information for IndEnz0002002134
IED ID IndEnz0002002134
Enzyme Type ID protease002134
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 An05g00070
Organism Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 niger Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Enzyme Sequence MAISIHPPRDPNTLSNYNNWICTHITANFDILFDQKKLVGNVIHKLKSTTNGESQEIILDSNHVAIGDVKIDGRPSEWELLPPLEPYGSALKIKLDQGVNLNETIDVEISVQTTEKCTALQWLTPAQTSNKKHPYMFSQCQAIHARSIFPCQDTPDVKSTIDFNISSPLPVIASGLPVRDALGASKSEGKSLYQFHQRVPIPSYLFALASGDISEAAIGPRSVVATSPDKVQECQWELEADTEKFIGAIEKIVYPYAWGEYNVLILPPSFPYGGMENPIFTFATPSIISKDRENIDVIAHELAHSWSGNLVTNASWEHFWLNEGWTTYLERRILAAVHGEAYRHFSAIIGWKALTDSVEHFGHDHEFTKLITDLKGKDPDDAFSSIPYEKGFNFLFHLETLVGKQKFDRFIPHYFTVFKGKSLDSYEFKATLLDFFGTDAEASKLLNDLDWDTWFYAPGLPPKPQFDTSLVDVVYELAQKWKSLSETSSFKPQLSDIESLSANQIVVFLEQMLLLERPLTPELSKLMGEVYGLSKSENIEVANLYFQLGLKAGDENVVDPATELLGRIGRMKFVRPLFRSLQRVNREVAVATFEKYKDFYHPICRAMVEKDLFGKRDV
Enzyme Length 618
Uniprot Accession Number A2QKF8
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 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 69,842
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