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 |