Any feedback?
Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Rattus norvegicus and UniProt Accession P04904
for references in articles please use BRENDA:EC2.5.1.18Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.5.1.18 glutathione transferaseIUBMB Comments
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.
Specify your search results
Word Map
- 2.5.1.18
- catalase
- dismutase
- sod
-
pull-down
- malondialdehyde
- carcinogenesis
-
detoxify
- hepatocytes
-
smoke
- isoenzymes
- cyp1a1
-
smoking
-
case-control
-
electrophilic
- epoxide
-
aquatic
- wistar
-
genotoxic
-
insecticide
-
chemopreventive
- gill
-
hepatocarcinogenesis
- acetylcholinesterase
-
polycyclic
-
pesticide
- hydroperoxide
-
thiobarbituric
-
hepatotoxicity
-
tbars
-
ache
-
albino
- metallothioneins
-
cigarette
-
benzoapyrene
- phenobarbital
-
drug-metabolizing
-
preneoplastic
-
alt
- aflatoxin
- gssg
-
hepatoprotective
- schistosoma
- comet
- carboxylesterase
- mussel
-
udp-glucuronosyltransferase
-
methylation-specific
- gsh-px
-
organophosphate
- drug development
- medicine
- cyp2d6
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gst, glutathione s-transferase, gstm1, gstp1, gstt1, glutathione-s-transferase, glutathione transferase, gsta1, gst pi, gstm3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha class glutathione transferase
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
glutathione S-transferase X
-
-
-
-
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
GST
MGST1
microsomal glutathione transferase-1
membrane-bound enzyme with both glutathione transferase and hydroperoxidase activities
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
additional information
glutathione S-transferase
-
-
-
-
additional information
-
MGST1 that belongs to the membrane associated proteins in eicosanoid and glutathione metabolism, MAPEG, superfamily
additional information
-
overview of nomenclature of rat glutathione transferase isoenzymes
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aryl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
50812-37-8
-
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
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
glutathione + 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole
?
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
-
?
glutathione + 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole
?
-
-
-
?
glutathione + 4-nitrobenzyl chloride
?
-
-
-
-
?
glutathione + 7-amino-4-chloromethyl coumarin
?
-
isozyme GSt T2-2 shows high activity
-
-
?
glutathione + anti-benzo(a)pyrene-7,8-dihydrodiol-9,10-epoxide
?
-
-
-
-
?
glutathione + cryptophycin 52
?
-
conjugation with the R-stereoisomer
-
-
?
glutathione + cryptophycin 53
?
-
conjugation with the S-stereoisomer
-
-
?
glutathione + cumene hydroperoxide
?
-
-
-
-
?
glutathione + ethacrynic acid
?
-
-
-
-
?
glutathione + 1,2-dichloro-4-nitrobenzene
?
-
-
637893, 637894, 637903, 637905, 637908, 637914, 637915, 637918, 637921, 637928, 637934, 637936, 637938
-
-
?
glutathione + 1,2-epoxy-3-(4-nitrophenoxy)propane
?
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
-
i.e. CDNB
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
-
best substrate
-
-
?
glutathione + trans-4-phenyl-3-buten-2-one
?
-
-
-
-
?
RX + glutathione
HX + R-S-glutathione
-
RX: R: aliphatic, aromatic or heterocyclic, X: sulfate, nitrite or halide, enzyme also catalyzes: the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrite, certain isomerization reactions and disulfide interchange
-
-
?
RX + glutathione
HX + R-S-glutathione
-
participates in detoxification
-
-
?
RX + glutathione
HX + R-S-glutathione
-
biotransformation and detoxification of electrophilic xenobiotics
-
-
?
RX + glutathione
HX + R-S-glutathione
-
detoxification of electrophilic products of cytochrome P-450-dependent reactions, toxic catabolite of heme, bilirubin is bound and thereby neutralized
-
-
?
RX + glutathione
HX + R-S-glutathione
-
detoxification of products of oxidative metabolism, e.g. 4-hydroxyalkenals, epoxides, organic hydroperoxides
-
-
?
RX + glutathione
HX + R-S-glutathione
-
may be involved in preventing lipid peroxidation
-
-
?
RX + glutathione
HX + R-S-glutathione
-
microsomal enzyme is likely to be involved in drug metabolism
-
-
?
RX + glutathione
HX + R-S-glutathione
-
first step in mercapturic acid synthesis
-
-
?
additional information
?
-
-
any compound bearing a sufficiently electrophilic atom may be attacked, reactions with C,S,N and O atoms are possible
-
-
?
additional information
?
-
-
catalyzes the reaction of glutathione with a large number of compounds bearing an electrophilic carbon to form the corresponding thioether
-
-
?
additional information
?
-
-
isomerization of DELTA5- to DELTA4- unsaturated 3-keto steroids
-
-
?
additional information
?
-
-
no substrate: 1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
?
additional information
?
-
-
no substrate: trans-4-phenyl-3-buten-2-one
-
-
?
additional information
?
-
-
no substrate: trans-4-phenyl-3-buten-2-one
-
-
?
additional information
?
-
-
assays for differentiation of glutathione S-transferase isoenzymes from rat and human by different specific acitivities with selected substrates
-
-
?
additional information
?
-
-
glutathione transferase X: no reaction of menaphthyl sulfate with glutathione, potent in inactivation of tert-10,11-epoxy-r-8,tert-9-dihydroxy-8,9,10,11-tetrahydrobenz/a/anthracene
-
-
?
additional information
?
-
-
the wild-type dimeric form is not required for catalytic activity
-
-
?
additional information
?
-
-
MGST1 possesses glutathione transferase and peroxidase activity. Native MGST1 binds three GSH molecules per trimer but with different affinities for GSH, it possesses only one high affinity catalytically competent site per trimer, nanoelectrospray mass spectrometric analysis, overview
-
-
?
additional information
?
-
-
quantitative structure-activity relationship analyses, overview
-
-
?
additional information
?
-
-
substrate specificity, overview. A major structural determinant of substrate recognition is the H-site, which binds the electrophile in proximity to the nucleophilic sulfur of the second substrate glutathione. H-site residue 234 has a key role in governing the activity and substrate selectivity profile of GST T1-1
-
-
?
additional information
?
-
-
glutathione transferases from rat liver are able to conjugate GSH to many hydrophobic toxic compounds. Small and hydrophilic disulfides like cystine, cystamine and dithioethanol, and hydrophilic alkylating compounds like iodoacetate, are no substrates of this enzyme. Omega class GST and a peculiar lens GST display a moderate thiol transferase activity with dithioethanol
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
glutathione transferases from rat liver are able to conjugate GSH to many hydrophobic toxic compounds. Small and hydrophilic disulfides like cystine, cystamine and dithioethanol, and hydrophilic alkylating compounds like iodoacetate, are no substrates of this enzyme. Omega class GST and a peculiar lens GST display a moderate thiol transferase activity with dithioethanol
-
-
?
RX + glutathione
HX + R-S-glutathione
-
participates in detoxification
-
-
?
RX + glutathione
HX + R-S-glutathione
-
biotransformation and detoxification of electrophilic xenobiotics
-
-
?
RX + glutathione
HX + R-S-glutathione
-
detoxification of electrophilic products of cytochrome P-450-dependent reactions, toxic catabolite of heme, bilirubin is bound and thereby neutralized
-
-
?
RX + glutathione
HX + R-S-glutathione
-
detoxification of products of oxidative metabolism, e.g. 4-hydroxyalkenals, epoxides, organic hydroperoxides
-
-
?
RX + glutathione
HX + R-S-glutathione
-
may be involved in preventing lipid peroxidation
-
-
?
RX + glutathione
HX + R-S-glutathione
-
microsomal enzyme is likely to be involved in drug metabolism
-
-
?
RX + glutathione
HX + R-S-glutathione
-
first step in mercapturic acid synthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KBr
-
KBr greatly influences the monomer-dimer equilibrium of the wildtype isozyme GST-M1-1
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3,5,6-tetrachloro-1,4-benzoquinone
-
i.e. TCBQ, inhibition of GSTA1-2 and GSTA1-1 by 70-80%, and GSTA2-2 by 25%, binds to cysteine residues of the enzyme, e.g. Cys17 of GSTA1-1, via a first reversible step to covalent binding, overview, Kitz-Wilson inactivation model
Al3+
-
68% inhibition at 100 mg/kg for male rats, 24% inhibition at 172.5 mg/kg for female rats
ascorbate
-
ascorbate enhances the inhibitory effects of SH reagents, overview, inactivation of total cytosolic GST activity from liver by the oxygen radical-generating system Cu2+/ascorbate, two mechanisms: ROS-induced oxidation and non-specific Cu2+ binding to protein thiol groups
Cu2+
-
inhibitory in either the absence or presence of ascorbate, inactivation of total cytosolic GST activity from liver by the oxygen radical-generating system Cu2+/ascorbate, two mechanisms: ROS-induced oxidation and non-specific Cu2+ binding to protein thiol groups, the inhibition is prevented by glutathione but not 1-chloro-2,4-dinitrobenzene, Cu2+ inhibition affects the Km for glutathione but not of 1-chloro-2,4-dinitrobenzene, overview
Indocyanine green
-
inhibition of transferase B is greater than inhibition of transferase AA
S-(2,4-dinitrophenyl)glutathione
-
mixed-type inhibition by reaction product, complex inhibition pattern
S-carvone
S-carvone inhibits 26% of the enzyme activity at 0.01 mM and 84% at 0.1 mM
superoxide anion
-
generated by a Fe3+/ascorbate system, inhibits cytosolic GSTs and microsomal GSTs by 30% and 65%, respectively. Addition of 2 mM DTT fails to completely reverse microsomal GST inhibition elicited by Fe3+/ascorbate, recovering only about 10% of this activity, but it completely reverses the inhibitory effect of Fe3+/ascorbate on cytosolic GST activity
H2O2
-
inhibits cytosolic GST by about 65% and activates microsomal GST to about 175%
additional information
-
construction of three series of curcumin derivatives, inhibitory potencies on GSt isozymes, overview
-
additional information
-
presence of superoxide dismutase and catalase reduces the activity of the microsomal GST isozyme, but only catalase can reduce the activity of the cytosolic GST
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
1-chloro-2,4-dinitrobenzene
-
pH 6.5, 25°C, recombinant wild-type enzyme
additional information
additional information
-
Cu2+ effects on Km, overview
-
additional information
additional information
-
kinetics, single-enzyme Michaelis-Menten model
-
additional information
additional information
-
kinetic analysis, overview
-
additional information
additional information
-
single turnover stopped flow kinetics and equilibrium dialysis analysis of GSH biniding affinity and stoichiometry, dissociation constants, overview
-
additional information
additional information
-
pseudo-first order kinetic constants, simplified Michaelis-Menten steady-state model for simulation of the overall dependence of the rate of product formationon either substrate or enzyme concentrations, with substrate 1-chloro-2,4-dinitrobenzene
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.035
isozyme GST A3-3, using 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole as a substrate
0.11
2.57
isozyme GST A2-2, using 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole as a substrate
30.9
5.6
wild type enzyme, using 1-chloro-2,4-dinitrobenzene as a substrate
additional information
additional information
-
activities of wild-type and mutant isozymes GST T2-2, overview
additional information
-
substrate specificity of recombinant His-tagged enzyme, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
different isoenzyme patterns in rat lung and liver
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
637908, 637914, 637917, 637918, 637928, 637930, 637934, 637936, 673034, 677269, 702529, 706920, 759685
-
highest activity in rough endoplasmic reticulum
additional information
-
microsomal enzyme is clearly distinct from cytosolic
-
additional information
-
microsomal enzyme is clearly distinct from cytosolic
-
additional information
-
microsomal enzyme is clearly distinct from cytosolic
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GSTA3_RAT
221
0
25319
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
50000
-
about, recombinant wild-type enzyme, analytical ultracentrifugation
additional information
-
monomer-dimer equilibrium and average molecular weights with and without bound glutathione at different concentrations of KBr, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
trimer
additional information
dimer
-
dimer composed of two of the following subunits: Ya MW 23000, Yb MW 23500, Yc MW 25000, SDS-PAGE
dimer
-
wild-type isozyme GST-M1-1, homodimer, crystal structure determination
trimer
-
native MGST1 binds three GSH molecules per trimer but with different affinities for GSH, it possesses only one high affinity catalytically competent site per trimer, nanoelectrospray mass spectrometric analysis, overview
additional information
-
homology modeling of recombinant isozyme GSTA1-1 with and without bound inhibitor 2,3,5,6-tetrachloro-1,4-benzoquinone
additional information
-
molecular structure modeling, the wild-type dimeric form is not required for catalytic activity, overview
additional information
-
quantitative structure-activity relationship analyses, calculation, overview
additional information
-
the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D97K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D97R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E100K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E100R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N101D
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
N101K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R131M
-
mutant enzyme shows 60% of wild-type activity with 1-chloro-2,4-dinitrobenzene as substrate
R131Q
-
mutant enzyme shows 50% of wild-type activity with 1-chloro-2,4-dinitrobenzene as substrate
R131W
-
mutant enzyme shows 24% of wild-type activity with 1-chloro-2,4-dinitrobenzene as substrate
R15Q
-
mutant enzyme shows 0.02% of wild-type activity with 1-chloro-2,4-dinitrobenzene as substrate
R77E
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
R77Q
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y9F
-
mutant enzyme shows 0.8% of wild-type activity with 1-chloro-2,4-dinitrobenzene as substrate. 4.3fold increase in KM-value for GSH compared to wild-type value, 1.3fold decrease in KM-value for 1-chloro-2,3-dinitrobenzene
Y9T
-
mutant enzyme shows 0.06% of wild-type activity with 1-chloro-2,4-dinitrobenzene as substrate
additional information
additional information
-
construction of heterodimers (WT-Y9F, WT-Y9T, WT-R15Q, WT-R131M, WT-R131Q, and WT-R131E) by incubation of a mixture of wild-type and mutant enzyme at pH 7.5 in buffer containing 1,6-hexanediol, followed by dialysis against buffer lacking the organic solvent. The Vmax values of the resultant heterodimers are lower than expected for independent active sites. Mutation of an amino acid residue in one active site affects the activity in the other active site
additional information
-
chimeric enzymes constructed by homology-independent recombination of human GST T-1 and rat GST T2-2 exhibit very different substrate promiscuity profiles, and show a more defined relationship between evolved and promiscuous activities, overview
additional information
-
construction of the monomeric mutant isozyme M1, GST M1, by introducing point mutations in the electrostatic region of the subunit interface and residues Arg77, Asp97, Glu100, Asn101, the mutation leads to formation of monomers instead of dimers and partially reduced activity, at 3 M KBr GST M1 has a specific activity close to that of GST M1-1, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native alpha class isozymes GSTA2-2, GSTA1-2 and GSTA1-1 from kidney by anion exchange and glutathione affinity chromatography, followed by another step of ion exchange chromatography
-
recombinant His-tagged wild-type enzyme from Escherichia coli strain XL1-Blue by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type enzyme in Escherichia coli strain XL1-Blue
-
expression of wild-type and mutant enzymes in Escherichia coli strain JM105
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morgenstern, R.; DePierre, J.W.
Microsomal glutathione transferase. Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition
Eur. J. Biochem.
134
591-597
1983
Rattus norvegicus
Morgenstern, R.; Guthenberg, C.; DePierre, J.W.
Microsomal glutathione S-transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione S-transferases A, B and C
Eur. J. Biochem.
128
243-248
1982
Rattus norvegicus
Morgenstern, R.; Meijer, J.; DePierre, J.W.; Ernster, L.
Characterization of rat-liver microsomal glutathione S-transferase activity
Eur. J. Biochem.
104
167-174
1980
Rattus norvegicus
Friedberg, T.; Bentley, P.; Stasiecki, P.; Glatt, H.R.; Raphael, D.; Oesch, F.
The identification, solubilization, and characterization of microsome-associated glutathione S-transferases
J. Biol. Chem.
254
12028-12033
1979
Rattus norvegicus
Jakoby, W.B.
Glutathione transferases: an overview
Methods Enzymol.
113
495-499
1985
Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus
Habig, W.H.; Jakoby, W.B.
Glutathione S-transferases (rat and human)
Methods Enzymol.
77
218-231
1981
Homo sapiens, Rattus norvegicus
Jakoby, W.B.; Keen, J.H.
A triple-threat in detoxification: the glutathione S-transferases
Trends Biochem. Sci.
2
229-231
1977
Homo sapiens, Pisum sativum, Rattus norvegicus, Zea mays
-
Robertson, I.G.C.; Jensson, H.; Guthenberg, C.; Tahir, M.K.; Jernstrm, B.; Mannervik, B.
Differences in the occurrence of glutathione transferase isoenzymes in rat lung and liver
Biochem. Biophys. Res. Commun.
127
80-86
1985
Rattus norvegicus
Meyer, D.J.; Beale, D.; Tan, K.H.; Coles, B.; Ketterer, B.
Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity
FEBS Lett.
184
139-143
1985
Rattus norvegicus
Alin, P.; Jensson, H.; Guthenberg, C.; Danielson, U.H.; Tahir, M.K.; Mannervik, B.
Purification of major basic glutathione transferase isoenzymes from rat liver by use of affinity chromatography and fast protein liquid chromatofocusing
Anal. Biochem.
146
313-320
1985
Rattus norvegicus
Guthenberg, C.; Alin, P.; Mannervik, B.
Glutathione transferase from rat testis
Methods Enzymol.
113
507-510
1985
Rattus norvegicus
Jensson, H.; Alin, P.; Mannervik, B.
Glutathione transferase isoenzymes from rat liver cytosol
Methods Enzymol.
113
504-507
1985
Rattus norvegicus
Reddy, C.C.; Li, N.Q.; Tu, C.P.D.
Identification of a new glutathione S-transferase from rat liver cytosol
Biochem. Biophys. Res. Commun.
121
1014-1020
1984
Rattus norvegicus
Satoh, K.; Kitahara, A.; Soma, Y.; Inaba, Y.; Hatayama, I.; Sata, K.
Purification, induction, and distribution of placental glutathione transferase: a new marker enzyme for preneoplastic cells in the rat chemical hepatocarcinogenesis
Proc. Natl. Acad. Sci. USA
82
3964-3968
1985
Rattus norvegicus
Habig, W.H.; Jakoby, W.B.
Assays for differentiation of glutathione S-transferases
Methods Enzymol.
77
398-405
1981
Homo sapiens, Rattus norvegicus
Pattinson, N.
Purification by affinity chromatography of glutathione S-transferases A and C from rat liver cytosol
Anal. Biochem.
115
424-427
1981
Rattus norvegicus
Ketterer, B.; Beale, D.; Meyer, D.
The structure and multiple functions of glutathione transferases
Biochem. Soc. Trans.
10
82-84
1982
Rattus norvegicus
Guthenberg, C.; Mannervik, B.
Purification of glutathione S-transferases from rat lung by affinity chromatography. Evidence for an enzyme form absent in rat liver
Biochem. Biophys. Res. Commun.
86
1304-1310
1979
Rattus norvegicus
Reddy, C.C.; Burgess, J.R.; Tu, C.P.D.
Isolation and characterization of an anionic glutathione S-transferase from rat liver cytosol
Biochem. Biophys. Res. Commun.
111
840-846
1983
Rattus norvegicus
Friedberg, T.; Milbert, U.; Bentley, P.; Guenther, T.M.; Oesch, F.
Purification and characterization of a new cytosolic glutathione S-transferase (glutathione S-transferase X) from rat liver
Biochem. J.
215
617-625
1983
Rattus norvegicus
Kraus, P.
Resolution, purification and some properties of three glutathione transferases from rat liver mitochondria
Hoppe-Seyler's Z. Physiol. Chem.
361
9-15
1980
Rattus norvegicus
Misquitta, S.A.; Colman, R.F.
Communication between the two active sites of glutathione S-transferase A1-1, probed using wild-type-mutant heterodimers
Biochemistry
44
8608-8619
2005
Rattus norvegicus
O'Sullivan, S.M.; McCarthy, R.M.; Vargo, M.A.; Colman, R.F.; Sheehan, D.
Chemical modification at subunit 1 of rat kidney alpha class glutathione transferase with 2,3,5,6-tetrachloro-1,4-benzoquinone: close structural connectivity between glutathione conjugation activity and non-substrate ligand binding
Biochem. Pharmacol.
71
1629-1636
2006
Rattus norvegicus
Hearne, J.L.; Colman, R.F.
Catalytically active monomer of class mu glutathione transferase from rat
Biochemistry
45
5974-5984
2006
Rattus norvegicus
Letelier, M.E.; Martinez, M.; Gonzalez-Lira, V.; Faundez, M.; Aracena-Parks, P.
Inhibition of cytosolic glutathione S-transferase activity from rat liver by copper
Chem. Biol. Interact.
164
39-48
2006
Rattus norvegicus
Griswold, K.E.; Aiyappan, N.S.; Iverson, B.L.; Georgiou, G.
The evolution of catalytic efficiency and substrate promiscuity in human theta class 1-1 glutathione transferase
J. Mol. Biol.
364
400-410
2006
Rattus norvegicus, Homo sapiens (P30711), Homo sapiens
Cannady, E.A.; Chien, C.; Jones, T.M.; Borel, A.G.
In vitro metabolism of the epoxide substructure of cryptophycins by cytosolic glutathione S-transferase: species differences and stereoselectivity
Xenobiotica
36
659-670
2006
Canis lupus familiaris, Macaca fascicularis, Homo sapiens, Mus musculus, Rattus norvegicus, Mus musculus CD1
Torres-Rivera, A.; Landa, A.
Glutathione transferases from parasites: a biochemical view
Acta Trop.
105
99-112
2008
Homo sapiens, Echinococcus granulosus (O16058), Rattus norvegicus (P04905), Schistosoma mansoni (P15964), Mus musculus (P24472), Schistosoma japonicum (P26624), Onchocerca volvulus (P46427), Ascaris suum (P46436), Fasciola hepatica (P56598), Sus scrofa (P80031), Clonorchis sinensis (Q1L2C7), Taenia solium (Q3ZJN3), Ancylostoma caninum (Q6J1M5), Plasmodium yoelii (Q7REH6), Wuchereria bancrofti (Q86LL8), Plasmodium falciparum (Q8MU52)
Kurtovic, S.; Grehn, L.; Karlsson, A.; Hellman, U.; Mannervik, B.
Glutathione transferase activity with a novel substrate mimics the activation of the prodrug azathioprine
Anal. Biochem.
375
339-344
2008
Bos taurus, Homo sapiens, Homo sapiens (P08263), Homo sapiens (Q16772), Rattus norvegicus (P04903), Rattus norvegicus (P04904)
Busenlehner, L.S.; Alander, J.; Jegerscoehld, C.; Holm, P.J.; Bhakat, P.; Hebert, H.; Morgenstern, R.; Armstrong, R.N.
Location of substrate binding sites within the integral membrane protein microsomal glutathione transferase-1
Biochemistry
46
2812-2822
2007
Rattus norvegicus (P08011)
Kurtovic, S.; Shokeer, A.; Mannervik, B.
Diverging catalytic capacities and selectivity profiles with haloalkane substrates of chimeric alpha class glutathione transferases
Protein Eng. Des. Sel.
21
329-341
2008
Rattus norvegicus (P04903), Rattus norvegicus (P04904), Homo sapiens (P08263), Homo sapiens (P09210), Homo sapiens (Q16772), Homo sapiens, Bos taurus (Q28035), Bos taurus
Alander, J.; Lengqvist, J.; Holm, P.J.; Svensson, R.; Gerbaux, P.; Heuvel, R.H.; Hebert, H.; Griffiths, W.J.; Armstrong, R.N.; Morgenstern, R.
Microsomal glutathione transferase 1 exhibits one-third-of-the-sites-reactivity towards glutathione
Arch. Biochem. Biophys.
487
42-48
2009
Rattus norvegicus
Shokeer, A.; Mannervik, B.
Residue 234 is a master switch of the alternative-substrate activity profile of human and rodent theta class glutathione transferase T1-1
Biochim. Biophys. Acta
1800
466-473
2010
Mus musculus, Rattus norvegicus, Homo sapiens (P30711), Homo sapiens
Letelier, M.E.; Molina-Berrios, A.; Cortes-Troncoso, J.; Jara-Sandoval, J.A.; Mueller, A.; Aracena-Parks, P.
Comparative effects of superoxide anion and hydrogen peroxide on microsomal and cytosolic glutathione S-transferase activities of rat liver
Biol. Trace Elem. Res.
134
203-211
2010
Rattus norvegicus
Appiah-Opong, R.; Commandeur, J.N.; Istyastono, E.; Bogaards, J.J.; Vermeulen, N.P.
Inhibition of human glutathione S-transferases by curcumin and analogues
Xenobiotica
39
302-311
2009
Homo sapiens, Rattus norvegicus
Imaizumi, N.; Aniya, Y.
The role of a membrane-bound glutathione transferase in the peroxynitrite-induced mitochondrial permeability transition pore: formation of a disulfide-linked protein complex
Arch. Biochem. Biophys.
516
160-172
2011
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Fabrini, R.; Bocedi, A.; Dawood, K.F.; Turella, P.; Stella, L.; Parker, M.W.; Pedersen, J.Z.; Federici, G.; Antonini, G.; Ricci, G.
The extended catalysis of glutathione transferase
FEBS Lett.
585
341-345
2011
Rattus norvegicus
Dobritzsch, D.; Grancharov, K.; Hermsen, C.; Krauss, G.J.; Schaumloeffel, D.
Inhibitory effect of metals on animal and plant glutathione transferases
J. Trace Elem. Med. Biol.
57
48-56
2020
Armoracia rusticana, Astacus astacus, Brassica juncea, Oryctolagus cuniculus, Lemna minor, Meleagris gallopavo, Mus musculus, Oncorhynchus mykiss, Oreochromis mossambicus, Oryza sativa, Pacifastacus leniusculus, Picea abies, Pleuronectes platessa, Populus sp., Pelophylax ridibundus, Rattus norvegicus, Typha latifolia, Rhabdosargus sarba, Chelon saliens, Protaetia brevitarsis, Alburnus tarichi, Salvelinus alpinus, Siganus canaliculatus, Laeonereis acuta
Heydel, J.M.; Menetrier, F.; Belloir, C.; Canon, F.; Faure, P.; Lirussi, F.; Chavanne, E.; Saliou, J.M.; Artur, Y.; Canivenc-Lavier, M.C.; Briand, L.; Neiers, F.
Characterization of rat glutathione transferases in olfactory epithelium and mucus
PLoS ONE
14
e0220259
2019
Rattus norvegicus (P08010)
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
