Detail Information for IndEnz0018000493
IED ID IndEnz0018000493
Enzyme Type ID peroxidase000493
Protein Name Microsomal glutathione S-transferase 1
Microsomal GST-1
EC 2.5.1.18
Microsomal GST-I
Gene Name MGST1 GST12 MGST
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAKKYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIAYLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL
Enzyme Length 155
Uniprot Accession Number P10620
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Can be activated by reagents that attack Cys-50 sulfhydryl, such as N-ethylmaleimide. Activation also occurs via nitration of Tyr-93 by peroxynitrite (By similarity). {ECO:0000250}.
Binding Site BINDING 38; /note=Glutathione; /evidence=ECO:0000250; BINDING 73; /note=Glutathione; /evidence=ECO:0000250; BINDING 74; /note=Glutathione; /evidence=ECO:0000250; BINDING 76; /note=Glutathione; /evidence=ECO:0000250; BINDING 81; /note=Glutathione; /evidence=ECO:0000250; BINDING 121; /note=Glutathione; /evidence=ECO:0000250
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;
DNA Binding
EC Number 2.5.1.18
Enzyme Function FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Binding site (6); Chain (1); Modified residue (3); Site (1); Topological domain (5); Transmembrane (4)
Keywords Acetylation;Alternative splicing;Endoplasmic reticulum;Membrane;Microsome;Mitochondrion;Mitochondrion outer membrane;Nitration;Reference proteome;Transferase;Transmembrane;Transmembrane helix
Interact With P01133; Q14802-3; O75084; Q8WX92; Q96PQ1; O14798; P01282-2
Induction
Subcellular Location SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Modified Residue MOD_RES 42; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q91VS7; MOD_RES 55; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q91VS7; MOD_RES 60; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q91VS7
Post Translational Modification PTM: Peroxynitrite induces nitration at Tyr-93 which activates the enzyme. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11587073; 11904223; 12818425; 15338373; 16384981; 17483957; 17714764; 19343046; 20195357; 20727966; 23314968; 23805041; 24189400; 24486338; 26638075; 27486097; 28558199; 29695404; 29713984; 31707341; 33539732; 34171541; 8692836; 8703034; 9278457;
Motif
Gene Encoded By
Mass 17,599
Kinetics
Metal Binding
Rhea ID RHEA:16437
Cross Reference Brenda