Detail Information for IndEnz0018000451
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;