IED ID | IndEnz0018000451 |
Enzyme Type ID | peroxidase000451 |
Protein Name |
Leukotriene C4 synthase LTC4 synthase EC 4.4.1.20 Glutathione S-transferase LTC4 EC 2.5.1.- Leukotriene-C 4 synthase |
Gene Name | Ltc4s |
Organism | Rattus norvegicus (Rat) |
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 Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MKEETALLATVTLLGVLLQAYFSLQVISARRTFHVSPPLTSGPPEFERVFRAQVNCSEYFPLFLATLWVAGIFFHEGAAALCGLFYLFARLRYFQGYARSAQHRLDPLYASARALWLLVAMAALGLLVHFLPGTLRAALFRWLQVLLPMA |
Enzyme Length | 150 |
Uniprot Accession Number | Q925U2 |
Absorption | |
Active Site | ACT_SITE 31; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q16873; ACT_SITE 104; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q16873 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by MK886. {ECO:0000250|UniProtKB:Q16873}. |
Binding Site | BINDING 30; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:Q16873 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000269|PubMed:12445492};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17619; Evidence={ECO:0000250|UniProtKB:Q16873}; CATALYTIC ACTIVITY: Reaction=(13S,14S)-epoxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate + glutathione = (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:53508, ChEBI:CHEBI:57925, ChEBI:CHEBI:131958, ChEBI:CHEBI:137407; Evidence={ECO:0000250|UniProtKB:Q16873};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53509; Evidence={ECO:0000250|UniProtKB:Q16873}; |
DNA Binding | |
EC Number | 4.4.1.20; 2.5.1.- |
Enzyme Function | FUNCTION: Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity (PubMed:12445492). Can also catalyzes the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions (By similarity). {ECO:0000250|UniProtKB:Q16873, ECO:0000269|PubMed:12445492}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis. {ECO:0000250|UniProtKB:Q16873}. |
nucleotide Binding | |
Features | Active site (2); Binding site (1); Chain (1); Modified residue (1); Region (3); Sequence conflict (1); Topological domain (5); Transmembrane (4) |
Keywords | Endoplasmic reticulum;Leukotriene biosynthesis;Lyase;Membrane;Nucleus;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | INDUCTION: Up-regulated by all-trans retinoic acid. {ECO:0000269|PubMed:12445492}. |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. Nucleus membrane {ECO:0000250|UniProtKB:Q16873}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16873}. |
Modified Residue | MOD_RES 36; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16873 |
Post Translational Modification | PTM: Phosphorylation at Ser-36 by RPS6KB1 inhibits the leukotriene-C4 synthase activity. {ECO:0000250|UniProtKB:Q16873}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12767051; 14637132; 15084748; 15619010; 17194456; 17496435; 18440824; 18461660; 19908283; 7827126; 9794912; |
Motif | |
Gene Encoded By | |
Mass | 16,850 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:17617; RHEA:17619; RHEA:53508; RHEA:53509 |
Cross Reference Brenda | 4.4.1.20; |