Detail Information for IndEnz0002002157
IED ID IndEnz0002002157
Enzyme Type ID protease002157
Protein Name Leukotriene A-4 hydrolase
LTA-4 hydrolase
EC 3.3.2.6
Leukotriene A
4
hydrolase
Gene Name LTA4H
Organism Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Hystricomorpha Chinchillidae (chinchillas) Chinchilla Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera)
Enzyme Sequence MPEVEDTCFLTSPITVCRTKHLHLRCSVDFSSRALTGIAALTIQSQEDNLRSLVLDTKALTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEVVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAVLPCQDTPSVKLTYTAEVSVPKELVALMSAVRDGETPDPEDPSRKIYKFNQKVPIPCYLIALVVGALESRKIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFHALGGWGELQNTIKTFGETHPFTKLVVDLTDVDPDVAYSSVPYEKGFALLFHLEQLLGGPEVFLGFLKAYVERFSYKSITTDDWKNFLYSHFKDKVDILNQVDWNAWLYSPGLPPVKPNYDMTLTNACIALSQRWITAKEEDLNTFNATDLKDLSTHQVNEFLAQVLQQAPLPLGHVKRMQEVYNFNAVNNSEIRFRWLRLCIQSKWEEAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAIRTYQAHKASMHPVTAMLVGKDLKVD
Enzyme Length 611
Uniprot Accession Number Q6S9C8
Absorption
Active Site ACT_SITE 297; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 384; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation ACTIVITY REGULATION: Inhibited by bestatin. Subject to suicide inhibition by leukotriene A4 (By similarity). {ECO:0000250}.
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: Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (3); Modified residue (4); Region (3); Site (2)
Keywords Acetylation;Cytoplasm;Hydrolase;Leukotriene biosynthesis;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue MOD_RES 73; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P09960; MOD_RES 337; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P09960; MOD_RES 416; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P09960; MOD_RES 573; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P09960
Post Translational Modification PTM: Phosphorylation at Ser-416 inhibits enzymatic activity. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 69,213
Kinetics
Metal Binding METAL 296; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 300; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 319; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID RHEA:22324
Cross Reference Brenda