Detail Information for IndEnz0018000345
IED ID IndEnz0018000345
Enzyme Type ID peroxidase000345
Protein Name Glutathione S-transferase
EC 2.5.1.18
GST class-alpha
Gene Name
Organism Gallus gallus (Chicken)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken)
Enzyme Sequence MSGKPVLHYANTRGRMESVRWLLAAAGVEFEEKFLEKKEDLQKLKSDGSLLFQQVPMVEIDGMKMVQTRAILNYIAGKYNLYGKDLKERALIDMYVEGLADLYELIMMNVVQPADKKEEHLANALDKAANRYFPVFEKVLKDHGHDFLVGNKLSRADVHLLETILAVEESKPDALAKFPLLQSFKARTSNIPNIKKFLQPGSQRKPRLEEKDIPRLMAIFH
Enzyme Length 221
Uniprot Accession Number Q08392
Absorption
Active Site
Activity Regulation
Binding Site BINDING 9; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P13745; BINDING 45; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P13745
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133768; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133771; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione; Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937; Evidence={ECO:0000250|UniProtKB:P08263};
DNA Binding
EC Number 2.5.1.18
Enzyme Function FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid. {ECO:0000250|UniProtKB:P08263}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Domain (2); Region (2)
Keywords Reference proteome;Transferase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 25,299
Kinetics
Metal Binding
Rhea ID RHEA:16437; RHEA:16438; RHEA:50796; RHEA:50797; RHEA:50804; RHEA:50805; RHEA:48888; RHEA:48889; RHEA:43936; RHEA:43937
Cross Reference Brenda