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Enzyme Nomenclature
Information on EC 2.5.1.18 - glutathione transferase
for references in articles please use BRENDA:EC2.5.1.18
Word Map on EC 2.5.1.18
- 2.5.1.18
- peroxidase
- catalase
- superoxide
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carcinogen
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xenobiotic
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pull-down
- carcinoma
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detoxify
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odds
- carcinogenesis
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smoke
- injury
- malondialdehyde
- fish
- hepatocytes
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smoking
- cyp1a1
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pollution
- placental
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biotransformation
- epoxide
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case-control
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electrophilic
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genotoxic
- wistar
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aquatic
- gill
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hepatotoxicity
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pesticide
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hepatocarcinogenesis
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polycyclic
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benzoapyrene
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tbars
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preneoplastic
- hydroperoxide
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chemopreventive
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co-immunoprecipitation
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thiobarbituric
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insecticide
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drug-metabolizing
- aflatoxin
- phenobarbital
- gssg
- acetylcholinesterase
- ache
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methylation-specific
- gsh-px
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udp-glucuronosyltransferase
- sh2
- cyp2d6
- analysis
- medicine
- drug development
- biotechnology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.5.1.18
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RECOMMENDED NAME
GeneOntology No.
glutathione transferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RX + glutathione = HX + R-S-glutathione
mechanisms for formation of specific mono(glutathionyl) or bis(glutathionyl) conjugates
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RX + glutathione = HX + R-S-glutathione
the enzyme uses a rapid-equilibrium random-order ternary-complex mechanism or a compulsory order ternary-complex mechanism
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RX + glutathione = HX + R-S-glutathione
active site involving residue Trp234, and substrate binding structure, isozyme GST T1-1
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RX + glutathione = HX + R-S-glutathione
the enzyme uses a rapid equilibrium random sequential bi-bi mechanism with intrasubunit modulation between GSH binding site, the G-site, and electrophile binding site, the H-site, Trp12, Phe35 and Ile118 are involved in substrate binding, Phe35 is important for catalytic activity
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RX + glutathione = HX + R-S-glutathione
substrate binding: Tyr9 is responsible for the deprotonation of GSH and Lys15, but also Gln71 are involved, active site and substrate binding structure, overview
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RX + glutathione = HX + R-S-glutathione
active site structure: Tyr111 indirectly stabilizes glutathione binding, Tyr119 modulates hydrophobic substrate binding, and Phe123 indirectly modulates catalysis. An aromatic zipper in the H-site contributing a network of aromatic pi-pi interactions. Several residues of the cluster directly interact with the hydrophobic substrate while others indirectly maintain conformational stability of the dimeric structure through the C-terminal domain II
RX + glutathione = HX + R-S-glutathione
catalytic mechanism of kappa class GST, overview. Substrate binding induces a conformational change of the active site from an open conformation in the apo-form to a closed conformation in the S-hexylglutathione-bound complex, facilitating formations of the G site (GSH-binding site) and the H site (hydrophobic substrate-binding site). The conserved Ser16 at the G site functions as the catalytic residue in the deprotonation of the thiol group and the conserved Asp69, Ser200,Asp201 andArg202 form a network of interactions with gamma -glutamyl carboxylate to stabilize the thiolate anion. The H site is a large hydrophobic pocket with conformational flexibility to allow the binding of different hydrophobic substrates. The kinetic mechanism of hGSTk conforms to a rapid equilibrium random sequential Bi Bi model
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RX + glutathione = HX + R-S-glutathione
active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview
RX + glutathione = HX + R-S-glutathione
the mutant C169A exhibits cooperative behaviour and a ping pong mechanism whereby liberation of a proton from a reduced enzyme-glutathione complex to form an enzyme-unprotonated glutathione complex is essentially irreversible
RX + glutathione = HX + R-S-glutathione
substrate binding structure and reaction mechanism, conformational changes, detailed overview
RX + glutathione = HX + R-S-glutathione
substrate specificity and catalytic mechanism, overview
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RX + glutathione = HX + R-S-glutathione
catalytic mechanism of isozyme GSTH1-1
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RX + glutathione = HX + R-S-glutathione
catalytic mechanism of isozyme GSTH1-1
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RX + glutathione = HX + R-S-glutathione
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aryl group transfer
aryl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
RX:glutathione R-transferase
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
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CAS REGISTRY NUMBER
COMMENTARY
50812-37-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PMD and PMD-R strains, the latter is a highly resistant strain, Isla Mujeres (IM) strain, New Orleans (NO) susceptible strain, isozymes GSTE1-GSTE8
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a cold-adapted marine bivalve Iceandic scallop, mu-class enzyme
SwissProt
sigma class isozyme, gene gst; fall webworm, gene gst, sigma class isozyme
SwissProt
three field populations collected from Nanyang city of Henan Province, and Wuzhou and Hezhou cities of Guangxi Province, China
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cytosolic enzymes, referred to as alpha, mu, pi and theta, and microsomal enzyme
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genes Na-gst-1, Na-gst-2, and Na-gst-3 encoding isozymes GST-1, GST-2, and GST-3
UniProt
the single-site mutation A122C and N124A/V (but not N124S/Y/C) restores the GST activity of Ure2p protein toward 1-chloro-2,4-dinitrobenzene, while causing a substantial reduction in glutathione peroxidase activity
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cultivar Gamay Freaux variant Teinturier
UniProt
ecotype Wassijlieska, phi class isozyme, encoded by inducible gene GSTU26; ecotype Wassijlieska, tau class isozyme, encoded by constitutive gene GSTF9
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isozyme Phi, i.e. GSTF, isozyme Tau, i.e. GSTU, isozyme Theta, i.e. GSTT, isozyme Zeta, i.e. GSTZ, and isozyme Lambda, i.e. GSTL, alll encoded by several genes, overview
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delta class GST; housedust mite, delta class GST isozyme
SwissProt
mu class GST; housedust mite, mu class GST isozyme
SwissProt
isozyme GSTS1; disk abalone, subspecies Haliotis discus discus
UniProt
isozyme GSTS2; disk abalone, subspecies Haliotis discus discus
UniProt
isozyme GSTS3; disk abalone, subspecies Haliotis discus discus
UniProt
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637898, 637899, 637903, 637904, 637905, 637906, 637911, 637916, 637920, 637922, 637925, 637927, 637941, 637942, 637958, 649763, 660644, 660795, 661110, 684236, 684410, 685332, 685432, 702366, 705056, 721532, 722707, 722870, 723016, 737674
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isozyme GSTP1-1, encoded by a single functional GSTP gene termed GSTP1 that maps to chromosome 11q13; isozyme GSTT1-1
UniProt
isozyme GSTD1 or Delta or Theta class isozyme; Sigma and Delta GST isozymes
UniProt
; coho salmon, several isozymes, e.g. pi and rho-class GSTs, as well as alpha and mu class isozymes
SwissProt
subsp. nigeriensis, a rodent malarial parasite, propagated in Swiss albino mice
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637893, 637894, 637895, 637896, 637899, 637903, 637905, 637909, 637915, 637917, 637918, 637921, 637922, 637928, 637930, 637934, 637936, 702461, 721429, 722273
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delta GST isozyme; type hominis, delta GST isozyme
SwissProt
delta GST isozyme; var. vulpes delta, the astigmatid mite, delta GST isozyme; mu GST isozyme; type hominis, mu GST isozyme
SwissProt
gene from GST descended from Schistosoma containing in vector pET42a(+)
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cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GST 19E50; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GST 28e45; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GST Cla47; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GST1; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTA1; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTA2; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTF1; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTF2; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTF3; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTF4; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTF5; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTF6; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTU1A; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTU1B; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTU1C; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTU2; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTU3; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
GSTZ1; cv. MV Emese, drought-tolerant cv. Plainsman, and drought-sensitive cv. GKE
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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the enzyme belongs to the glutathione transferase, GST, superfamily. Phylogenetic analysis shows, among the Delta class, GSTD1 and GSTD10 appear to be recently diverged transcripts with 86% amino acid sequence similarity
evolution
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kappa class GSTs are a distinct class of the GST superfamily or Trx (thioredoxin)-fold superfamily because of their unique cellular localization, function and structure. GSTks do not contain a conserved CXXC motif at the active site
evolution
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structures and properties of YghU and YfcG indicate that they are members of the same distinct subfamily of GSH transferase homologues, proposed to be called the Nu-class GSH transferases. Cytoscape cluster analysis of the GSH transferase superfamily, overvew
evolution
O15217, O43708, O60760, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5
the cytosolic glutathione transferases, GSTs, comprise a super family of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a super family of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a super family of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions; the cytosolic glutathione transferases, GSTs, comprise a superfamily of proteins that can be categorized into multiple classes with a mixture of highly specific and overlapping functions
evolution
GST5118 belongs to a distinct class named GSTFuA, for fungal specific GST class A, as part of the GST superfamily
evolution
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glutathione transferase classes alpha, pi, and mu and their GSH activation mechanism, overview
evolution
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the enzyme belongs to the soluble plant GST superfamily of dimeric enzymes, isozymes classes, overview. Dehydroascorbate reductase and tetrachlorohydroquinone dehalogenase-like proteins also belong to the GST superfamily
evolution
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TDR1 belongs to the glutathione-S-transferase (GST) superfamily
malfunction
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partial silencing of either GSTe7 or GSTe2 by RNA interference results in an increased susceptibility to the pyrethroid, deltamethrin
malfunction
mutation at Phe108, located just below Arg113 in the binding pocket, reduces the affinity and catalytic activity to both GSH and the electrophilic co-substrate, 1-chloro-2,4-dinitrobenzene
malfunction
O15217, O43708, O60760, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5
a single SNP causing an I71L substitution in African subjects causes diminished activity with several substrates including CDNB and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole as a result of an elevation in its Km for GSH, but the specific activity towards DELTA5-androsten-3,17-dione and the Km GSH of the L71 variant are not changed; associations between GSTO1 polymorphisms and vascular dementia and stroke. A236V polymorphism: the V236 variant protein has low specific activity with a range of substrates and shows marked heat instability. It seems highly likely that this substitution leads to GSTO1-1 deficiency in homozygotes. E155 deletion causes a significant folding defectthat may explain the deficiency associated with this deletion. The V236 variant protein has low specific activity with a range of substrates and shows marked heat instability; differences in the catalytic activity of the V105 and I105 variants to carcinogenic diolepoxides may underlie the associations between these alleles and cancer susceptibility; GSTM1-1 deficiency contributes significantly to survival after chemotherapy for childhood leukemia; natural mutations D43N, T65M and T104P, and a frame shift mutation at G412 cause GSTT1-1 deficiency; the GSTT12B allele results from the relatively rare T104P substitution in Scandinavian individuals, and appears to destabilize the protein and result in GSTT1-1 deficiency. The relatively common deletion of the GSTT2b pseudogene is associated with an altered risk of esophageal squamous cell carcinoma; the GSTZ1-A protein has relatively high activity with (±)-2-bromo-3-(4-nitrophenyl)propanoic acid but it has low isomerase activity with its natural substrate maleylacetoacetate; two rare intronic variants (IVS2+11A>C and IVS3+13T>C) are reported, the intron-2 SNP is significantly transmitted to asthma-affected children
malfunction
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isozymes AtGSTs F11, F12, F14 and U14, in which the catalytic serine is replaced by a non-proton abstracting residue, show abolished transferase activity
metabolism
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glutathione S-transferase P1-1 is one of the most important members of phase II detoxification enzyme family which catalyzes the conjugation of glutathione with broad substrates such as chemotherapeutic agents
metabolism
the classical phase II detoxification glutathione transferases are key metabolic enzymes that catalyze the conjugation of glutathione to various electrophilic compounds
metabolism
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GST reaction products as metabolic intermediates, e.g. delivering the sullfur in the compounds, possible role for glutathione and GSTs in sulfur incorporation, detailed overview
metabolism
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the enzyme isoforms play important roles in the detoxification of pesticides
physiological function
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glutathione transferases are a major detoxification system in helminths
physiological function
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the glutathione-S-transferases are a family of multifunctional enzymes involved in the detoxification of electrophilic xenobiotics primarily through conjugation to reduced glutathione
physiological function
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overlapping and specific roles of rice glutathione S-transferase genes during development and stress responses, role of GSTs in mediating crosstalk between various stress and hormone response pathways
physiological function
bmGSTO might be involved in the increase in level of insecticide resistance for lepidopteran insects
physiological function
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HdGSTO1 might play important protective roles against environmental stress. Under thermal stress, HdGSTO2 expression is repressed in a time-dependent pattern, implying different physiological roles of the isozymes under stress
physiological function
the isozymes may be involved in the detoxification and/or transport of heme
physiological function
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glutathione S-transferases are a family of detoxifying enzymes that catalyze the conjugation of glutathione to electrophiles, thereby increasing the solubility of xenobiotics and aiding its excretion from the cell
physiological function
through alternative splicing, two of these GSTTs form fusions with Myb transcription factor-like domains, discrete localization within the nucleus, possibly serving role in reducing nucleic acid hydroperoxides or in signalling
physiological function
O04437, P30110, P30111, Q6U6G6, Q8GRI3, Q8GTB7, Q8GTB8, Q8GTB9, Q8GTC0, Q8GTC1, Q8LGN5, Q8LGN6, Q8LL15, Q8RW00, Q8RW01, Q8RW02, Q8RW03, Q8RW04, Q9SP56
GSTU1B and GSTF6 genes may play important roles in monocarpic senescence of wheat; GSTU1B and GSTF6 genes may play important roles in monocarpic senescence of wheat
physiological function
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GSTs are important phase II drug-metabolizing enzymes that play a major role in protecting cells from the toxic insults of electrophilic compounds
physiological function
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GSTE2 is implicated in conferring resistance to DDT for the dengue vector Aedes aegypti. Epsilon GSTs have DDT dehydrochlorinase activity, GSTe2 and two additional Epsilon GST genes, GSTe5 and GSTe7, are expressed at elevated levels in the resistant population and the recombinant homodimer GSTE5-5 also exhibits low levels of DDT dehydrochlorinase activity
physiological function
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role of mtMGST1 in the oxidant peroxynitrite-induced mitochondrial permeability transition, MPT, pore opening, peroxynitrite induces the swelling of mitoplasts (inner membranes including the matrix) as well as of the mitochondria. mtMGST1, ADP (an adenine nucleotide translocator),and cyclosporin A function as a MPT pore in peroxynitrite-induced swelling, in which the Ca2+ released by peroxynitrite might play an important role in the complex formation
physiological function
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GSTF2 and GSTF3 may have roles in regulating the binding and transport of defence-related compounds in planta
physiological function
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glutathione transferases are a family of enzymes that primarily catalyse nucleophilic addition of the thiol of GSH to a variety of hydrophobic electrophiles in the cellular detoxification of cytotoxic and genotoxic compounds
physiological function
O15217, O43708, O60760, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5
all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. Because of its highly specialized activity the Sigma class GST is generally known as hemopoietic prostaglandin D synthase, HPGDS; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. Because of its highly specialized role catalyzing the penultimate step in the catabolism of tyrosine, GSTZ1-1 is also known as maleylacetoacetate isomerase, MAAI; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. GSTA1-1 is likely to play a significant role in binding hydrophobic ligands such as bilirubin and steroid hormones; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. GSTA3-3 may play an important physiological role as it efficiently catalyzes the isomerization of DELTA5-3-ketosteroids in the synthesis of testosterone and progesterone; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. GSTO1 is a determinant of the age at onset of Alzheimer's and Parkinson's diseases; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. Interaction between GSTM monomers and ASK1 with regulatory function; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. Interaction between GSTM monomers and ASK1 with regulatory function; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. Interaction between GSTM monomers and ASK1 with regulatory function; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. Interaction between GSTM monomers and ASK1 with regulatory function; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. Interaction between GSTM monomers and ASK1 with regulatory function; all the catalytically active GSTs contribute to the glutathione conjugation or glutathione dependant-biotransformation of xenobiotics and many catalyze glutathione peroxidase or thiol transferase reactions. GSTs also catalyze glutathione dependent isomerization reactions required for the synthesis of several prostaglandins and steroid hormones and the catabolism of tyrosine, additional GST physiological functions, overview. The Pi class GST occurs in a monomer-dimer equilibrium and monomers can bind to and regulate other proteins such as JNK and TRAF
physiological function
glutathione S-transferases form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes. GST5118 of Phanerochaete chrysosporium can function as a classical GST through the addition of glutathione mainly to phenethyl isothiocyanate, but alternatively and in a competitive way, it can also act as a ligandin of wood extractive compounds
physiological function
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overexpression of human GSTA1-1 in tumor cells is part of multi drug resistance mechanisms
physiological function
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GSTs functioning in the transport of secondary metabolites, e.g. of the electrophilic oxylipins. Pi class GSTs have assumed such roles in modulating the activity of Jun NH2-terminal kinase through protein-protein interactions. Tau class protein AtGSTU20 is a binding partner of the far-red insensitive 219 protein, such that alterations in its expression give rise to an altered growth phenotype under continuous far-red light. AtGSTF12, in which the catalytic serine is replaced by a non-proton abstracting residue resulting in abolished transferase activity, is necessary for correct anthocyanin pigment formation in developing Arabidopsis seeds, although their function is not related to GSH conjugation. Sometimes, following GST action, S-glutathionylated xenobiotics are imported into the vacuole by ATP-binding cassette (ABC) transporter proteins. In the GST family members where the catalytic serine is replace with a cysteine, the GSTs show the ability to co-ordinately bind hydrophobic ligands in close proximity to the reactive thiol of GSH
physiological function
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AtuGSTH1-1 may play an important regulatory role in stress defence mechanism
physiological function
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posttranslational S-glutathionylation modifications and glutaredoxin-dependent deglutathionylation participate in the regulation of metabolism and redox signalling in most organisms. Thiol-dependent reductase I, TDR1, an enzyme found in parasitic Leishmania species and Trypanosoma cruzi, is implicated in deglutathionylation and activation of antimonial prodrugs used to treat leishmaniasis. The deglutathionylation activity of TDR1 implies that glutathione itself has regulatory intracellular roles in addition to being a precursor for trypanothione, the major low mass thiol present in trypanosomatids
physiological function
-
isoforms GTT1.2, GSTFuA1, and GSTO1 are essential for full aggressiveness of Alternaria brassicicola on host plant
physiological function
-
the enzyme is involved in the detoxification of harmful chemicals
physiological function
-
AtuGSTH1-1 may play an important regulatory role in stress defence mechanism
-
physiological function
-
isoforms GTT1.2, GSTFuA1, and GSTO1 are essential for full aggressiveness of Alternaria brassicicola on host plant
-
physiological function
-
role of mtMGST1 in the oxidant peroxynitrite-induced mitochondrial permeability transition, MPT, pore opening, peroxynitrite induces the swelling of mitoplasts (inner membranes including the matrix) as well as of the mitochondria. mtMGST1, ADP (an adenine nucleotide translocator),and cyclosporin A function as a MPT pore in peroxynitrite-induced swelling, in which the Ca2+ released by peroxynitrite might play an important role in the complex formation
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additional information
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the substrate binding pocket of MdGST6B, involving Arg113 and Phe121 on helix 4, is narrower compared to other delta- and epsilon-class GSTs, structure, overview. The Arg113 hydrogen bond does not play a crucial role in catalysis
additional information
the substrate binding pocket of MdGST6B, involving Arg113 and Phe121 on helix 4, is narrower compared to other delta- and epsilon-class GSTs, structure, overview. The Arg113 hydrogen bond does not play a crucial role in catalysis
additional information
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G-site and H-site structure analysis and modeling, overview
additional information
role of conserved residues Ser13, Asn48 and Pro49 in the catalytic mechanism of the tau class glutathione transferase, overview
additional information
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residues Ser11, Gln51, His52, Ser67, and Arg68 of the N-terminal domain are important for catalytic enzyme function, active site structure, overview
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
GSTT1-1 deficiency as the result of a gene deletion is common and is not deleterious
additional information
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role for mutant Cys in mutant M212C in the transnitrosylation reaction with cyanoDMNG, while the Cys residue is not required in the aromatic substitution with 1-chloro-2,4-dinitrobenzene, for epoxide opening with NPG, and for addition to the ortho-quinone with aminochrome
additional information
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structure of G-site active center amino acids of GSTM1-1, GSTP1-1, and GSTA1-1, mechanism comparison of isozymes, overview. Analysis of the GSH activation mechanism of GSTP1-1 and GSTM1-1 isoenzymes, overview. For the GSTP1-1 enzyme, a water molecule, after an initial conformational rearrangement of GSH, can assist a proton transfer between the GSH cysteine thiol and the GSH glutamate alpha carboxylate groups. The GSTM1-1 enzyme shows a completely different behavior from isoenzyme GSTP1-1, here two water molecules, positioned between the GSH-SH and the zeta N atom of His107, working like a bridge, are able to promote the proton transfer between these two active groups
additional information
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where GSTs are involved in conjugating acceptors with GSH, there is an absolute requirement for the conserved serine residue within the active site, as it promotes the formation of the thiolate anion of GSH. In some family members this serine is replaced with a cysteine, e.g. promoting disulfide exchange reactions in the GSTL
additional information
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AtuGSTH1-1 lacks the classic catalytic essential residues (Tyr, Ser, Cys) and has instead of the classic catalytic residues, an Arg residue (Arg34), an electron-sharing network, and a bridge of a network of water molecules may form the basis of the catalytic mechanism, Phe22, Ser25, and Arg187 are additional important residues for the enzyme's catalytic efficiency and specificity, overview. GSH binding site, G-site, and electrophilic binding site, H-site, structures, overview. In contrast to other GSTs where the H-site involves C-terminal domain residues, interactions in AtuGSTH1-1 are mainly provided by Arg187 and the long turn between strand b1 andhelix H1, residues 25-33
additional information
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contribution of different residues in the GSH-binding site to GSH activation, structure analysis of wild-type and mutant enzymes by circular dichroism and fluorospectroscopic analysis, overview
additional information
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AtuGSTH1-1 lacks the classic catalytic essential residues (Tyr, Ser, Cys) and has instead of the classic catalytic residues, an Arg residue (Arg34), an electron-sharing network, and a bridge of a network of water molecules may form the basis of the catalytic mechanism, Phe22, Ser25, and Arg187 are additional important residues for the enzyme's catalytic efficiency and specificity, overview. GSH binding site, G-site, and electrophilic binding site, H-site, structures, overview. In contrast to other GSTs where the H-site involves C-terminal domain residues, interactions in AtuGSTH1-1 are mainly provided by Arg187 and the long turn between strand b1 andhelix H1, residues 25-33
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-2-bromo-3-(4-nitrophenyl)propanoic acid + glutathione
2-(glutathion-S-yl)-3-(4-nitrophenyl)propanoic acid + HBr
-
-
-
-
?
(2,3-dichloro-4-[2-methylenebutyryl]phenoxy)acetic acid + glutathione
?
-
i.e. ethacrynic acid
-
-
?
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione
1,1-dichloro-2,2-bis-(4-chlorophenyl)ethylene + ?
i.e. DDT, modeling of DDT into the putative DDT-binding pocket, catalytic mechanism of isozyme agGSTe2 that shows high activity through the inclination of the upper part of H4 helix, H4'' helix, which brings residues Arg112, Glu116, and Phe120 closer to the GSH-binding site resulting in a more efficient GS- stabilizing hydrogen-bond-network and higher DDT-binding affinity, overview
product formation through an elimination reaction triggered by the nucleophilic attack of the thiolate group of GS- on the beta-hydrogen of DDT
-
?
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione
?
detoxification of the insecticide DDT, especially by isozyme agGSTe2
-
-
?
1,2-dichloro-4-nitrobenzene + glutathione
S-(2-chloro-4-nitro-phenyl)glutathione + HCl
binding structure with wild-type and mutant Y119E and F123A enzymes, overview
-
-
?
1,3,5-triacryloyl-1,3,5-triazinane + glutathione
L-gamma-glutamyl-S-[3-(3,5-diacryloyl-1,3,5-triazinan-1-yl)-3-oxopropyl]-L-cysteinylglycine
-
-
-
-
?
1,3,5-trinitrobenzene + glutathione
S-(2,4,6-trinitrocyclohexa-2,5-dien-1-yl)glutathione
an anionic sigma-complex is formed between GSH and 1,3,5-trinitrobenzene and is stabilized by Arg15. The trinitrocyclohexadienate moiety of the sigma-complex binds the H-site where the catalytic residue, Tyr9, was identified to hydrogen bond to an o-nitro group of the sigma-complex
-
-
?
1-bromo-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HBr
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
chloride + L-gamma-glutamyl-S-(2,4-dinitrophenyl)-L-cysteinylglycine
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,3-dinitrophenyl)-glutathione + HCl
Tyr119 not only plays a role in hydrophobic substrate binding but also in packing of the active site pocket, which influences chemical interactions involved in enzyme catalysis
-
-
?
1-iodo-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HI
-
-
-
-
?
12-oxo-phytodienoic acid + glutathione
10-S-glutathionyl-12-oxo-phytodienoic acid + H2O
-
-
-
-
?
2,3-hexadienal + GSH
?
-
at 7.5% of the activity with 1-chloro-2,4-dinitrobenzene
-
-
?
2-chloro-5-nitropyridine + glutathione
chloride + L-gamma-glutamyl-S-(5-nitropyridin-2-yl)-L-cysteinylglycine
-
-
-
-
?
4-nitrobenzyl chloride + glutathione
S-(4-nitrobenzyl)glutathione + HCl
-
-
-
?
4-nitrophenethyl bromide + glutathione
S-(4-nitrophenyl)glutathione + HBr
-
-
-
?
4-nitrophenyl butyrate + glutathione
S-(4-nitrophenyl)glutathione + butyrate
-
-
-
?
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid + glutathione
?
-
-
-
-
?
5-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid + glutathione
?
-
-
-
-
?
7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH
7-chloro-4-glutathionylbenzo-2-oxa-1,3-diazole
-
-
-
-
?
7-oxabicyclo[4.1.0]heptan-2-one + glutathione
chloride + L-gamma-glutamyl-S-(6-oxocyclohex-1-en-1-yl)-L-cysteinylglycine
-
-
-
-
?
azathioprine + glutathione
?
-
aromatic substitution. Wild-type hGST M2-2 has modest activity with azathioprine, but mutant C87A/C115A/C174A/M212C displays no detectable activity. The azathioprine activity of wild-type hGST M2-2 can be enhanced 30fold by two point mutations of other residues in the active site
-
-
?
glutathione + (2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
chloride + 5-glutathionyl-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
-
-
?
glutathione + (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
chloride + 3-glutathionyl-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
glutathione + (2Z,4E)-3-chloro-6-(3,5-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
?
-
-
-
-
?
glutathione + 1,2-epoxy-3-(4-nitro-phenoxy)propane
?
-
best substrate for the wild-type GST T1-1 and mutant W234K
-
-
?
glutathione + 1,2-epoxy-3-(p-nitrophenoxy)-propane
?
-
substrate of the theta class isozyme
-
-
?
glutathione + 1-bromo-4-nitrobenzene
bromide + 4-nitrophenyl-glutathione
-
recombinant catalytically active monoclonal antibody fragment ScFv2F3
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione