Detail Information for IndEnz0002002160
IED ID IndEnz0002002160
Enzyme Type ID protease002160
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 CIMG_05732
Organism Coccidioides immitis (strain RS) (Valley fever fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Onygenales incertae sedis Coccidioides Coccidioides immitis (Valley fever fungus) Coccidioides immitis (strain RS) (Valley fever fungus)
Enzyme Sequence MKMATPANPLRDPNTLSNYNKFRTVHTSVNFEIRFDQKRLVGNVIHRLKSLTNAESKEVILDSSYLEVKSVKVNGEAAEWQLLPRFEPYGSPLKISLEQAIPLDELIEVDISVNTTEKCTALQWLNPEQTSNGKHPYMFSQCQAIHARAIFPCQDTPDVKATFDFNLSSPLPVIASGVPVKQDASPPQSSGSIYYRFEQKVPIPSYLFAIASGDIAQAQIGPRSHVAVSPDRLDECKWELEGDTERFLQTIGNIIFPYVWGEYNVLILPPSFPYGGMENPVYTFATPSIISKDRQNVDVIAHEISHSWSGNLVTNCSWEHFWLNEGWTTYLERRIQAAIHGEPYRHFSAIIGWKHLVDSVERHGDTHEFTKLVVDLKGKDPDDAFSSVPYEKGFTFIFHLENLIGKDKFDKFIPHYFTRFRGKSLDSYEFKSCILDFFASDEESHVLLNKLDWDSWFYKPGLPPKPSFDTSLVDVVYELANKWKYISQSSFSPKASDMDGLVANQIVVFLEQVLLFDNPLTPEQSRFMGQVYNFAQSQNIEVSYLYLQVGLKAGDDSIVEPTIKLLGEIGRMKFVRPLYRTLEKFNRDIAVDTFEKHKNFYHPICRGLLEKDLFGDKGA
Enzyme Length 619
Uniprot Accession Number Q1DVD1
Absorption
Active Site ACT_SITE 303; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 390; /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 70,678
Kinetics
Metal Binding METAL 302; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 306; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 325; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID RHEA:19037
Cross Reference Brenda