Detail Information for IndEnz0002002142
IED ID IndEnz0002002142
Enzyme Type ID protease002142
Protein Name Leukotriene A-4 hydrolase homolog
LTA-4 hydrolase
EC 3.3.2.6
Leukotriene A
4
hydrolase
Gene Name BC1G_09514
Organism Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Enzyme Sequence MATVSTINMPRDPNTLSNYNNWRTKHTIADLAIDFTKQRVHGTVTLQLESITDKESEEIILDTSFVDVQSVAVDGNKTGEWTLEKRIEPFGTPLSVKIPGGAAKGTVIALAITLSTTDKCTALQWLTPAQTSNKKFPYMFSQCQAIHNRSIFPCQDTPDVKSTYDFRIRSPLPVLASGLPRGAGSFVHGENGESGTLLYSFYQEIPMPSYLFALASGDIATASIGPRSLVSTGPEELIGAKWELERDTEKFIETIEKIVYPYEWTQYNVLVLPPSFPYGGMENPVFTFATPTIISGDRENVDVVAHELAHSWSGNLVSNASWEHFWLNEGWTVYLERRIIAAVHGEAYRDFSSIIGWKALEDSVKLYGEDHEFTKLIVDLKGKDPDDAFSSVPYEKGFHFLYYLERLVGKPSWDKFIPHYFTTWKKKSLDSYDFKATLLDFFASDSAASKALESVDWDSWFYKPGLPSKPEFDTSLVDKCYALAKKWESKDYTPSPSDIEGWAANQVVVFLQQVQLFTTPLTPVQSQAMGKAYNLVNTKNVELSSRYFGVGLAAKDETVYQPTAELLGKVGRMKFVRTLYRKLVVVDRKLAVETFEKNKDFYHPICRDQVEKDLKE
Enzyme Length 616
Uniprot Accession Number A6SAG8
Absorption
Active Site ACT_SITE 307; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 394; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O + leukotriene A4 = leukotriene B4; Xref=Rhea:RHEA:22324, ChEBI:CHEBI:15377, ChEBI:CHEBI:57461, ChEBI:CHEBI:57463; EC=3.3.2.6;
DNA Binding
EC Number 3.3.2.6
Enzyme Function FUNCTION: Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA(4) to form LTB(4) (in vitro) (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
nucleotide Binding
Features Active site (2); Chain (1); Erroneous initiation (1); Metal binding (3); Region (2)
Keywords Cytoplasm;Hydrolase;Leukotriene biosynthesis;Metal-binding;Metalloprotease;Nucleus;Protease;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 69,504
Kinetics
Metal Binding METAL 306; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 310; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 329; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID RHEA:22324
Cross Reference Brenda