Detail Information for IndEnz0002002215
IED ID IndEnz0002002215
Enzyme Type ID protease002215
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 SS1G_05513
Organism Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Sclerotinia Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum) Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Enzyme Sequence MPRDPNTLSNYNNWRTKHTIADLAIDFKKQRVHGTVTLQLESITDKESEEIILDTSFVDVQKIAVDGSKTEEWVLKERNEPYGSPLSVKIPGGAAKGTIIALDITISTTDKCTALQWLTPAQTSNKKFPYMFSQCQAIHNRSIFPCQDTPDVKSTYDFRIRSPLPVLASGLPRGAASFVHGENGESGTLLYSFYQEIPMPSYLFALSSGDIATASIGSRSLVSTGPEELLGAKWELERDTEKFIETIEKIVYPYEWTQYNVLVLPPSFPYGGMENPVFTFATPTIISGDRENVDVIAHELAHSWSGNLVSNASWEHFWLNEGWTVYLERRIIAAVHGEAYRDFSSIIGWKALEDSVKLFGEDHEFTKLVVDLKGKDPDDAFSSVPYEKGFHFLYYLERLVGKPTWDKFIPHYFTTWKKKSLDSYEFKATLLDFFASDEAASKALESVDWDSWFYKPGLPPKPEFDTSLVDKCYALAKKWESKDFVPSPSDIEGWSANQVVVFLQQVQLFTTPLTPSQSQAMGKAYSLVDTQNVELSSRYFGVGLAAKDESVYLPTAELLGKVGRMKFVRTLYRKLLVVDRKLAEETFEKNKDFYHPICREQVEKDLKE
Enzyme Length 608
Uniprot Accession Number A7EJL9
Absorption
Active Site ACT_SITE 299; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 386; /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 (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 68,945
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