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
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
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 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
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
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
isozymes AtGSTs F11, F12, F14 and U14, in which the catalytic serine is replaced by a non-proton abstracting residue, show abolished transferase activity
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
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
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
the classical phase II detoxification glutathione transferases are key metabolic enzymes that catalyze the conjugation of glutathione to various electrophilic compounds
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
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
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
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
the glutathione-S-transferases are a family of multifunctional enzymes involved in the detoxification of electrophilic xenobiotics primarily through conjugation to reduced glutathione
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
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. The Pi class GST occurs in a monomer-dimer equilibrium and monomers can bind to and regulate other proteins such as JNK and TRAF
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
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
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
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
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
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
recombinant isoform GST-theta protein can markedly improve bacterial growth under cumene hydroperoxide exposure. More importantly, the recombinant isoform can effectively prevent primary coelomocytes apoptosis after lipopolysacchride exposure. Isoform GST-theta plays significantly roles in the modulation of immune response and protect cells from pathogens infection in Apostichopus japonicus
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
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
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
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
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
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
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
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
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