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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Homo sapiens and UniProt Accession P78417

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EC Tree
IUBMB 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.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P78417
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
gst, glutathione s-transferase, gstm1, gstp1, gstt1, glutathione-s-transferase, glutathione transferase, gsta1, gst pi, gstm3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutathione S-transferase
-
glutathione S-transferase omega 1
-
GST O1-1
isozyme
Omega class GST
-
alpha class glutathione transferase
-
alpha GST
-
cGST
-
-
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
glutathione S-transferase 2
-
-
glutathione S-transferase A3-3
-
-
glutathione S-transferase P1-1
glutathione S-transferase pi
-
glutathione S-transferase X
-
-
-
-
glutathione transferase A1-1
glutathione transferase A4-4
-
-
glutathione transferase M1-1
-
-
glutathione transferase M2-2
-
-
glutathione transferase omega-1
-
-
glutathione transferase P1-1
glutathione transferase Pi
-
glutathione transferase T1-1
-
glutathione transferase zeta
-
-
glutathione transferase zeta 1
-
glutathione transferase Zeta 1-1
-
variants glutathione transferase Zeta 1a-1a, glutathione transferase Zeta 1b-1b, glutathione transferase Zeta 1c-1c, glutathione transferase Zeta 1d-1d
glutathione transferase zeta1-1
-
glutathione-S-transferase
-
-
glutathione-S-transferase pi
-
glutathione-transferase
-
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
GST A1-1
GST A2-2
GST A3-3
isozyme
GST A4-4
isozyme
GST M1-1
GST M2-2
GST M4-4
isozyme
GST M5-5
isozyme
GST P1-1
GST T1-1
GST Z1-1
isozyme
GSTA1-1
GSTA2-2
GSTA3-3
GSTA4-4
GSTk
-
-
GSTM1-1
GSTO1-1
-
-
GSTP-1
-
phi class GST
GSTP1-1
GSTT2B-2B
-
hGSTA-3
-
-
hGSTA1-1
-
-
hGSTZ1-1
-
-
kappa class glutathione transferase
-
-
Kappa class GST
-
-
MGST2
-
-
Omega class GST
-
Pi class GST
-
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
selenium-containing glutathione transferase zeta1-1
-
-
seleno-hGSTZ1-1
-
-
Sigma class GST
-
theta class glutathione transferase T1-1
-
theta class GST
theta-class glutathione transferase
-
-
Ya-GST
-
-
Zeta class GST
-
additional information
maleylacetoacetate isomerase, EC 5.2.1.2, bifunctional enzyme
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RX + glutathione = HX + R-S-glutathione
show the reaction diagram
active site structure and catalytic mechanism, overview
RX + glutathione = HX + R-S-glutathione
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aryl group transfer
-
-
-
-
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 hide
50812-37-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-chloro-2,4-dinitrobenzene + glutathione
2,4-dinitrophenyl-glutathione + HCl
show the reaction diagram
-
-
-
?
S-(4-nitrophenacyl)-glutathione
4-nitroacetophenone + glutathione
show the reaction diagram
-
-
-
?
(+)-2-bromo-3-(4-nitrophenyl)propanoic acid + glutathione
2-(glutathion-S-yl)-3-(4-nitrophenyl)propanoic acid + HBr
show the reaction diagram
-
-
-
-
?
(13S,9Z,11E)-13-hydroperoxyoctadeca-9,11-dienoic acid + GSH
?
show the reaction diagram
(15S,5Z,8Z,10E,14Z)-15-hydroperoxyeicosa-5,8,10,14-tetraenoic acid + GSH
?
show the reaction diagram
(5S,6E,8Z,11Z,14Z)-5-hydroperoxyeicosa-6,8,11,14-tetraenoic acid + GSH
?
show the reaction diagram
(9S,10E,12E)-9-hydroperoxyoctadeca-10,12-dienoic acid + GSH
?
show the reaction diagram
1,2-dichloro-4-nitrobenzene + GSH
?
show the reaction diagram
-
-
-
-
?
1,2-epoxy-3-(4-nitrophenoxy)-propane + glutathione
?
show the reaction diagram
1,2-epoxy-3-(p-nitrophenoxy)propane + GSH
?
show the reaction diagram
-
-
-
-
?
1,3,5-trinitrobenzene + glutathione
S-(2,4,6-trinitrocyclohexa-2,5-dien-1-yl)glutathione
show the reaction diagram
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
-
-
?
1,3-bis-(2-chloroethyl)-1-nitrosourea + glutathione
?
show the reaction diagram
-
-
-
-
?
1-chloro-2,3-dinitrobenzene + GSH
?
show the reaction diagram
-
-
-
-
?
1-chloro-2,3-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
show the reaction diagram
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
2,4-dinitrophenyl-glutathione + HCl
show the reaction diagram
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
show the reaction diagram
1-methyl-4-nitro-5-[(4-nitrophenyl)thio]-1H-imidazole + glutathione
?
show the reaction diagram
-
-
-
-
?
4-hydroxy-2-nonenal + glutathione
?
show the reaction diagram
-
-
-
-
?
4-hydroxy-2-nonenal + GSH
?
show the reaction diagram
-
-
-
-
?
4-hydroxynonenal + GSH
?
show the reaction diagram
-
10% of the activity with 1-chloro-2,3-dinitrobenzene
-
-
?
4-nitrobenzyl chloride + glutathione
?
show the reaction diagram
-
-
-
?
4-nitrophenethyl bromide + glutathione
?
show the reaction diagram
4-nitrophenylacetate + glutathione
?
show the reaction diagram
-
-
-
-
?
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid + glutathione
?
show the reaction diagram
-
-
-
?
5-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid + glutathione
?
show the reaction diagram
-
-
-
?
7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + glutathione
?
show the reaction diagram
-
-
-
?
7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH
?
show the reaction diagram
-
80% of the activity with 1-chloro-2,3-dinitrobenzene
-
-
?
acetyl-gamma-Glu-Cys-Gly + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
substrate for mutant enzyme I104V/A113V
-
-
?
allyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
aminochrome + glutathione
?
show the reaction diagram
-
-
-
-
?
androstenedione + glutathione
?
show the reaction diagram
-
-
-
-
?
azathioprine + glutathione
?
show the reaction diagram
-
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
-
-
?
benzyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
brostallicin + glutathione
glutathionyl-brostallicin
show the reaction diagram
butyl nitrite + glutathione
?
show the reaction diagram
-
-
-
-
?
chlorofluoroacetic acid + glutathione
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + glutathione
?
show the reaction diagram
cumene hydroperoxide + GSH
?
show the reaction diagram
dichloroacetate + glutathione
2-(glutathion-S-yl)-chloroacetate + HCl
show the reaction diagram
-
-
-
?
dichloroacetic acid + glutathione
?
show the reaction diagram
-
-
-
-
?
ethacrynic acid + glutathione
?
show the reaction diagram
gamma-Glu-Cys-Aib + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
substrate for mutant enzyme I104V/A113V
-
-
?
gamma-Glu-Cys-Nle + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
26.4% activity compared to glutathione
-
-
?
gamma-Glu-Cys-Nva + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
16% activity compared to glutathione
-
-
?
gamma-Glu-Cys-Sar + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
17% activity compared to glutathione
-
-
?
glutathione + (R)-styrene-7,8-oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + (R,R)-1-phenylpropylene oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + (R,R)-trans-stilbene oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + (S)-styrene-7,8-oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + (S,S)-1-phenylpropylene oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + (S,S)-trans-stilbene oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + 1,2-dichloro-4-nitrobenzene
?
show the reaction diagram
-
-
-
-
?
glutathione + 1,2-diiodoethane
?
show the reaction diagram
best substrate
-
-
?
glutathione + 1,2-epoxy-3-(4-nitro-phenoxy)propane
?
show the reaction diagram
-
best substrate for the wild-type GST T1-1 and mutant W234K
-
-
?
glutathione + 1,2-epoxy-3-(p-nitrophenoxy)propane
?
show the reaction diagram
-
-
-
?
glutathione + 1,4-diiodobutane
?
show the reaction diagram
-
-
-
?
glutathione + 1,6-diiodohexane
?
show the reaction diagram
-
-
-
?
glutathione + 1,8-diiodooctane
?
show the reaction diagram
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
chloride + 2,4-dinitrophenyl-glutathione
show the reaction diagram
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
show the reaction diagram
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
show the reaction diagram
glutathione + 1-fluoro-2,4-dinitrobenzene
?
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodo-3-phenylpropane
iodide + 3-phenylpropyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodobutane
iodide + butyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodoethane
iodide + ethylglutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodoheptane
iodide + heptyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodohexane
?
show the reaction diagram
-
-
-
?
glutathione + 1-iodohexane
iodide + hexyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodomethane
iodide + methylglutathione
show the reaction diagram
-
best substrate of GST T1-1 mutant W234R
-
-
?
glutathione + 1-iodooctane
iodide + octyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodopentane
iodide + pentyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-iodopropane
iodide + propyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 1-menaphthyl sulfate
?
show the reaction diagram
-
-
-
-
?
glutathione + 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole
?
show the reaction diagram
-
-
-
?
glutathione + 2-hydroxyethyl disulfide
?
show the reaction diagram
isozyme GSTO2, low activity
-
-
?
glutathione + 2-methyl-4-nitrobenzyl alcohol
?
show the reaction diagram
-
-
-
?
glutathione + 3,4-dichloro-1-nitrobenzene
?
show the reaction diagram
-
-
-
-
?
glutathione + 3,4-dinitrobenzanilide
?
show the reaction diagram
-
-
-
?
glutathione + 3-iodopropylbenzene
?
show the reaction diagram
-
-
-
?
glutathione + 4-chloro-3-nitroacetophenone
?
show the reaction diagram
-
-
-
?
glutathione + 4-chloro-3-nitrobenzophenone
?
show the reaction diagram
-
-
-
?
glutathione + 4-fluoro-3-nitrobenzanilide
?
show the reaction diagram
-
-
-
?
glutathione + 4-nitrobenzyl chloride
?
show the reaction diagram
-
-
-
-
?
glutathione + 4-nitrobenzyl chloride
chloride + 4-nitrobenzyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 4-nitrobenzyl chloride
S-(4-nitrobenzyl)glutathione + HCl
show the reaction diagram
-
-
-
?
glutathione + 4-nitrophenethyl bromide
bromide + 4-nitrophenethyl-glutathione
show the reaction diagram
-
-
-
-
?
glutathione + 7-amino-4-chloromethyl coumarin
?
show the reaction diagram
-
-
-
?
glutathione + 7-chloro-4-nitrobenz-2-oxa-1,3-diazole
?
show the reaction diagram
-
-
-
?
glutathione + 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
?
show the reaction diagram
-
poor substrate
-
-
?
glutathione + acetochlor
?
show the reaction diagram
-
-
-
-
?
glutathione + acrolein
?
show the reaction diagram
-
-
-
-
?
glutathione + adenine propenal
?
show the reaction diagram
-
-
-
-
?
glutathione + alachlor
?
show the reaction diagram
-
-
-
-
?
glutathione + atrazine
?
show the reaction diagram
-
high specific activity
-
-
?
glutathione + azathioprine
6-mercaptopurine + ?
show the reaction diagram
-
-
-
?
glutathione + benzo[a]pyrene 4,5-oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + bromosulfophthalein
?
show the reaction diagram
-
-
-
-
?
glutathione + chlorambucil
?
show the reaction diagram
-
-
-
?
glutathione + cis-6-(2-acetylvinylthio)purine
?
show the reaction diagram
-
-
-
?
glutathione + cryptophycin 52
?
show the reaction diagram
-
conjugation with the R-stereoisomer
-
-
?
glutathione + cryptophycin 53
?
show the reaction diagram
-
conjugation with the S-stereoisomer
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
glutathione + ethacrynic acid
?
show the reaction diagram
glutathione + ethylene diiodide
?
show the reaction diagram
-
-
-
?
glutathione + iodomethane
?
show the reaction diagram
-
-
-
-
?
glutathione + styrene 7,8-oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + styrene oxide
?
show the reaction diagram
-
-
-
-
?
glutathione + trans-4-phenyl-3-buten-2-one
?
show the reaction diagram
-
-
-
-
?
glutathione + trans-6-(2-acetylvinylthio)guanine
?
show the reaction diagram
-
-
-
?
hydrogen peroxide + glutathione
?
show the reaction diagram
-
-
-
?
Hyp-Cys-Gly + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
39.5% activity compared to glutathione
-
-
?
maleylacetone + glutathione
?
show the reaction diagram
-
-
-
-
?
monochlorobimane + glutathione
bimane-glutathione + HCl
show the reaction diagram
-
-
-
-
?
NMe-Glu-Cys-Gly + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
3.9% activity compared to glutathione
-
-
?
nonenal + glutathione
?
show the reaction diagram
-
-
-
-
?
pGlu-Cys-Gly + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
11.5% activity compared to glutathione
-
-
?
phenethyl isothiocyanate + glutathione
?
show the reaction diagram
Pro-Cys-Gly + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
21.6% activity compared to glutathione
-
-
?
propyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
rac-4-hydroxynonenal + glutathione
S-(4-hydroxy-1-oxononan-3-yl)glutathione
show the reaction diagram
-
elimination of the lipid peroxidation product 4-hydroxynonenal, a toxic compound that contributes to numerous diseases
-
-
?
rac-4-hydroxynonenal + glutathione
S-[(2S)-3-hydoxy-2-(2-oxoethyl)octyl]glutathione
show the reaction diagram
-
GSTA1-1 isoform has poor catalytic efficiency with 4-hydroxynonenal, GSTA4-4 has negligible stereoselectivity towards the two 4-hydroxynonenal enantiomers, despite its high catalytic chemospecificity for alkenals
product binding, overview
-
?
RSSR + glutathione
glutathione-SSR + R-SH
show the reaction diagram
-
-
-
?
RX + glutathione
HX + R-S-glutathione
show the reaction diagram
S-(4-nitrophenacyl)-glutathione
4-nitroacetophenone + glutathione
show the reaction diagram
-
-
-
-
?
Sar-Cys-Gly + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
15.8% activity compared to glutathione
-
-
?
styrene oxide + glutathione
?
show the reaction diagram
-
-
-
?
tertiary butyl hydroperoxide + glutathione
?
show the reaction diagram
-
-
-
?
Tic-Cys-Gly + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
41.3% activity compared to glutathione
-
-
?
[(methylamino)[methyl(nitroso)amino]methyl]cyanamide + glutathione
[bis(methylamino)methyl]cyanamide + S-nitrosoglutathione
show the reaction diagram
-
transnitrosylation
-
-
?
[3-(4-nitrophenyl)oxiran-2-yl]methanol + glutathione
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
brostallicin + glutathione
glutathionyl-brostallicin
show the reaction diagram
-
involved in activation of the prodrug, mechanism, overview. The reaction proceeds via the alpha-chloroamido derivative of the GSH-brostallicin adduct, is able to alkylate DNA in a sequence-specific manner and appears to be the active form of the drug, brostallicin cytotoxicity of brostallicin is higher in cells overexpressing either the GST-pi or the GST-mu gene
-
-
?
rac-4-hydroxynonenal + glutathione
S-(4-hydroxy-1-oxononan-3-yl)glutathione
show the reaction diagram
-
elimination of the lipid peroxidation product 4-hydroxynonenal, a toxic compound that contributes to numerous diseases
-
-
?
RX + glutathione
HX + R-S-glutathione
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(4-benzylpiperidin-1-yl)prop-2-en-1-one
-
1-(4-phenylpiperidin-1-yl)prop-2-en-1-one
-
2-(4-chlorophenyl)-6-[(fluorosulfonyl)oxy]quinoline-4-carboxylic acid
-
2-chloro-N,N-dimethyl-5-(vinylsulfonamido)-benzenesulfonamide
-
2-chloro-N-(4-(2-hydroxyphenyl)thiazol-2-yl)-N-((3-methylisoxazol-5-yl)methyl)acetamide
-
2-chloro-N-methyl-N-[(1-phenyl-1H-pyrazol-3-yl)methyl]acetamide
i.e. C4-10
2-chloro-N-[2-(cyclohexylamino)-2-oxo-1-(pyridin-2-yl)ethyl]-N-(3-fluorophenyl)acetamide
i.e. KT53
2-chloro-N-[4-chloro-3-(N,N-dimethylsulfamoyl)phenyl]acetamide
i.e. C1-27
2-fluoro-N-[(1,2,3,5,6,7-hexahydro-s-indacen-4-yl)carbamoyl]-5-(oxiran-2-yl)benzene-1-sulfonamide
i.e. CRID2
5-(chloromethyl)-3-oxo-3H-spiro[[2]benzofuran-1,9'-xanthene]-3',6'-diyl diacetate
i.e. CMFDA
ethyl 2-acrylamido-4-phenylthiazole-5-carboxylate
-
ethyl 2-acrylamido-4-phenylthiophene-3-carboxylate
-
ethyl 2-acrylamido-5-phenylthiophene-3-carboxylate
-
ethyl N-acryloyl-N-(4-phenylthiazol-2-yl)glycinate
-
methyl (E)-4-((4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-amino)but-2-enoate
-
methyl N-acryloyl-N-(4-phenylthiazol-2-yl)glycinate
-
N-((3-methylisoxazol-5-yl )methyl)-N-(4-(4-chloro-2-hydroxylphenyl)thiazol-2-yl)acrylamide
-
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(2-hydroxylphenyl)-thiazol-2-yl)acrylamide
-
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(2-methoxyphenyl)-thiazol-2-yl)acrylamide
-
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(4-fluoro-2-hydroxylphenyl)thiazol-2-yl)acrylamide
-
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(4-trifluoromethylphenyl)thiazol-2-yl)acrylamide
-
N-((3-methylisoxazol-5-yl)methyl)-N-(4-phenylthiazol-2-yl)-acrylamide
-
N-(1-benzyl-1H-pyrazol-4-yl)acrylamide
-
N-(1-phenyl-1H-pyrazol-4-yl)acrylamide
-
N-(2-((2-morpholinoethyl)amino)-2-oxoethyl)-N-(4-phenylthiazol-2-yl)acrylamide
-
N-(2-(cyclohexylamino)-2-oxoethyl)-N-(4-phenylthiazol-2-yl)-acrylamide
-
N-(2-(oxetan-3-ylamino)-2-oxoethyl)-N-(4-phenylthiazol-2-yl)-acrylamide
-
N-(2-morpholino-2-oxoethyl)-N-(4-phenylthiazol-2-yl)-acrylamide
-
N-(4-(2-chlorophenyl)thiazol-2-yl)acrylamide
-
N-(4-(2-fluorophenyl)thiazol-2-yl)acrylamide
-
N-(4-(2-hydroxylphenyl)thiazol-2-yl)acrylamide
-
N-(4-(2-hydroxyphenyl)thiophen-2-yl)-N-((3-methylisoxazol-5-yl)methyl)acrylamide
-
N-(4-(2-methoxyphenyl)thiazol-2-yl)acrylamide
-
N-(4-(3,4-dioxylphenyl)thiazol-2-yl)acrylamide
-
N-(4-(3-chlorophenyl)thiazol-2-yl)acrylamide
-
N-(4-(4-chlorophenyl)thiazol-2-yl)acrylamide
-
N-(4-(4-hydroxylphenyl)thiazol-2-yl)acrylamide
-
N-(4-(4-methoxyphenyl)thiazol-2-yl)acrylamide
-
N-(4-(4-methylphenyl)thiazol-2-yl)acrylamide
-
N-(4-(4-trifluoromethylphenyl)thiazol-2-yl)acrylamide
-
N-(4-(naphthalen-2-yl)thiazol-2-yl)acrylamide
-
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)acrylamide
-
N-(4-phenyl-5-methyl-thiazol-2-yl)acrylamide
-
N-(4-phenylthiazol-2-yl)-N-(pyridin-3-ylmethyl)acrylamide
-
N-(4-phenylthiazol-2-yl)acrylamide
-
N-(5-phenylthiazol-2-yl)acrylamide
-
N-acryloyl-N-(4-phenylthiazol-2-yl)glycine
-
N-benzyl-N-(4-phenylthiazol-2-yl)acrylamide
-
N-[3-[(chloroacetyl)(4-nitrophenyl)amino]propyl]-2,2,2-trifluoroacetamide
i.e. ML175
tert-butyl N-acryloyl-N-(4-phenylthiazol-2-yl)glycinate
-
(+)-catechin hydrate
-
inhibition of isozymes GST M1-1 and M2-2
(2R,3S)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-chromene-3,5,7-triol
-
a coumaroflavan from Treculia africana, 26% total inhibition at 0.033 mM
(2Z)-2-[(4-methoxyphenyl)carbonyl]-3-(2,3,4-trimethoxyphenyl)prop-2-enoic acid
-
-
(2Z)-2-[(4-methylphenyl)carbonyl]-3-(2,3,4-trimethoxyphenyl)prop-2-enoic acid
-
-
(2Z)-2-[(4-methylphenyl)carbonyl]-3-phenylprop-2-enoic acid
-
8.1% inhibition at 0.02 mM
(2Z)-3-(1,3-benzodioxol-5-yl)-2-[(4-methoxyphenyl)carbonyl]prop-2-enoic acid
-
10% inhibition at 0.02 mM
(2Z)-3-(1,3-benzodioxol-5-yl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
9.6% inhibition at 0.02 mM
(2Z)-3-(2-methylphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
9.3% inhibition at 0.02 mM
(2Z)-3-(3,4-dihydroxyphenyl)-2-[(4-methoxyphenyl)carbonyl]prop-2-enoic acid
-
-
(2Z)-3-(3,4-dihydroxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
-
(2Z)-3-(3-hydroxyphenyl)-2-[(4-methoxyphenyl)carbonyl]prop-2-enoic acid
-
6.6% inhibition at 0.02 mM
(2Z)-3-(3-hydroxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
13.9% inhibition at 0.02 mM
(2Z)-3-(3-methoxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
19.0% inhibition at 0.02 mM
(2Z)-3-(4-chlorophenyl)-2-[(4-methoxyphenyl)carbonyl]prop-2-enoic acid
-
14.4% inhibition at 0.02 mM
(2Z)-3-(4-chlorophenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
14.4% inhibition at 0.02 mM
(2Z)-3-(4-fluorophenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
-
(2Z)-3-(4-hydroxy-3-methoxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
8.8% inhibition at 0.02 mM
(2Z)-3-(4-hydroxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
12.5% inhibition at 0.02 mM
(2Z)-3-(4-methoxyphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
-
(2Z)-3-(4-methylphenyl)-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
-
(2Z)-3-[4-(dimethylamino)phenyl]-2-[(4-methylphenyl)carbonyl]prop-2-enoic acid
-
9.3% inhibition at 0.02 mM
(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)methanesulfonyl fluoride
-
-
(4S,6Z,10Z,11aS)-4-ethoxy-6-(hydroxymethyl)-3-methylidene-10-propoxy-3a,4,5,8,9,11a-hexahydrocyclodeca[b]furan-2(3H)-one
-
a sesquiterpene lactone from Dicoma anomala collected from Namibia, 75% total inhibition at 0.033 mM
(E)-2-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)ethene-1-sulfonyl fluoride
-
-
(E)-N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)but-2-enamide
-
-
1,4-pentadiene-3-one
-
curcumin derivative
1,7-dihydroxyanthracen-9(10H)-one
-
a xanthone from Mammea africana, 21% total inhibition at 0.033 mM
1-chloro-2,4-dinitrobenzene
-
competitive inhibition by the substrate
1-methyl-2-[((2-nitrobenzyl)sulfonyl)]-1H-pyrrole
-
44.3% inhibition at 0.1 mM
1-methyl-2-[(2-nitrobenzyl)sulfanyl]-1H-pyrrole
-
-
2,5-dibenzylidenecyclopentanone
-
curcumin derivative
2,6-dibenzylidenecyclohexanone
-
curcumin derivative
2-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)ethane-1-sulfonyl fluoride
-
-
2-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)imidazole
-
-
2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)-N-((1E)-[4-(trifluoromethyl)phenyl]methylene)aniline
-
68.4% inhibition at 0.1 mM
2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)-N-[(1E)-(4-nitrophenyl)methylene]aniline
-
90.0% inhibition at 0.1 mM
2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)-N-[(1E)-(phenyl)methylene]aniline
-
30.2% inhibition at 0.1 mM
2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)-N-[(1E)-1H-pyrrol-2-ylmethylene]aniline
-
36.0% inhibition at 0.1 mM
2-chloro-5-((cyanomethyl)amino)-N,N-dimethylbenzenesulfonamide
-
-
2-chloro-N,N-dimethyl-5 -(oxiran-2-ylmethyl) -benzenesulfonamide
-
-
2-chloro-N,N-dimethyl-5-(oxiran-2-yl)benzenesulfonamide
-
-
2-chloro-N-(2-(N,N-dimethylsulfamoyl)-[1,1'-biphenyl]-4-yl)-acetamide
-
-
2-chloro-N-(3-(morpholinosulfonyl)-4-(trifluoromethyl)phenyl)-acetamide
-
-
2-chloro-N-(3-(N,N-dimethylsulfamoyl)-4-(trifluoromethoxy)-phenyl)acetamide
-
-
2-chloro-N-(3-(N,N-dimethylsulfamoyl)-4-(trifluoromethyl)-phenyl)acetamide
-
-
2-chloro-N-(3-(N,N-dimethylsulfamoyl)-4-iodophenyl)-acetamide
-
-
2-chloro-N-(4-chloro-3-(morpholinosulfonyl)phenyl)acetamide
-
-
2-chloro-N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-propanamide
-
-
2-chloro-N-(4-chloro-3-(N-((tetrahydrofuran-2-yl)methyl)-sulfamoyl)phenyl)acetamide
-
-
2-chloro-N-(4-chloro-3-(N-(2-hydroxyethyl)-N-methylsulfamoyl)phenyl)acetamide
-
-
2-chloro-N-(4-chloro-3-(N-(2-hydroxyethyl)sulfamoyl)phenyl)-acetamide
-
-
2-chloro-N-(4-chloro-3-(N-(2-methoxyethyl)-N-methylsulfamoyl)phenyl)acetamide
-
-
2-chloro-N-(4-chloro-3-(N-(2-methoxyethyl)sulfamoyl)phenyl)-acetamide
-
-
2-chloro-N-(4-chloro-3-(N-(3-methoxypropyl)-N-methylsulfamoyl)phenyl)acetamide
-
-
2-chloro-N-(4-chloro-3-(N-(3-methoxypropyl)sulfamoyl)phenyl)-acetamide
-
-
2-chloro-N-(4-chloro-3-(N-(tetrahydrofuran-3-yl)sulfamoyl)-phenyl)acetamide
-
-
2-chloro-N-(4-chloro-3-(N-isopropylsulfamoyl)phenyl)-acetamide
-
-
2-chloro-N-(4-chloro-3-(N-methylsulfamoyl)phenyl)acetamide
-
-
2-chloro-N-[4-chloro-3-(N,N-dimethylsulfamoyl)phenyl]acetamide
-
i.e. C1-27
2-hydroxyanthracen-9(10H)-one
-
a xanthone Mammea from africana, 38% total inhibition at 0.033 mM
2-[(1-methyl-1H-pyrrol-2-ylsulfonyl)methyl]aniline
-
28.0% inhibition at 0.1 mM
3-(3,4-dihydroxybenzoyl)-4-hydroxy-8-methyl-1,5,7-tris(3-methylbut-2-en-1-yl)-8-(4-methylpent-3-en-1-yl)bicyclo[3.3.1]non-3-ene-2,9-dione
-
a benzophenone Garcinia smeathmannii, 41% total inhibition at 0.033 mM
3-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)propane-1-sulfonyl fluoride
-
-
3-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)propionic acid
-
-
3-chloro-N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-propenamide
-
-
3-ethyl-2-oxo-3,3a,7a,9b-tetrahydro-2H,4aH-1,4,5-trioxadicyclopenta[a,hi]indene-7-carboxylic acid
-
an iridoid from Plumeeria rubra, 51% total inhibition at 0.033 mM
4-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)butanol
-
-
4-(acryloylamino)-N-(5-[[5-([5-[(2-carbamimidamidoethyl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)-1-methyl-1H-pyrrole-2-carboxamide
-
a brostallicin derivative, the debrominated derivative of brostallicin is almost completely ineffective as an inhibitor of GSTP1-1
4-[(2-bromoacryloyl)amino]-N-(5-[[5-([5-[(2-carbamimidamidoethyl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)-1-methyl-1H-pyrrole-2-carboxamide
-
i.e. brostallicin, mixed-type inhibition, inhibits GSTP1-1 and GSTM2-2, thereby being much more efficient in inhibiting GSTM2-2 than in inhibiting GSTP1-1. Brostallicin sensitivity for brostallicin is higher in cells overexpressing either the GST-pi or the GST-mu gene
4-[3-(5,5-dimethyl-4-oxo-4,5-dihydrofuran-2-yl)-3-hydroxybutoxy]-7H-furo[3,2-g]chromen-7-one
-
a furocoumarin from Dorstenia elliptica, 34% total inhibition at 0.033 mM
5,7-dihydroxy-6-(2-hydroxybutanoyl)-8-(3-methylbut-2-en-1-yl)-4-propyl-2H-chromen-2-one
-
a coumarin from Mammea africana, 33% total inhibition at 0.033 mM
5,8-dihydroxy-1-(hydroxymethyl)naphtho[2,3-c]furan-4,9-dione
-
an isofuranonaphthoquinone from Bulbine frutescens, the mode of inhibition is mixed, partial (G site) and noncompetitive (H site), 68% total inhibition at 0.033 mM
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-chlorobenzyl)-1,2,4-oxadiazol
-
-
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
-
-
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-methoxyphenyl)-1,2,4-oxadiazol
-
-
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-nitrobenzyl)-1,2,4-oxadiazol
-
-
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
-
-
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
-
-
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
-
-
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-chlorobenzyl)-1,2,4-oxadiazol
-
-
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
-
-
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-hydroxyphenyl)-1,2,4-oxadiazol
-
-
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-nitrobenzyl)-1,2,4-oxadiazol
-
-
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
-
-
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
-
-
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
-
-
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
-
-
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
-
-
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
-
-
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
-
-
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
-
-
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
-
-
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
-
-
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
-
-
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
-
-
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-hydroxyphenyl)-1,2,4-oxadiazol
-
-
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-nitrobenzyl)-1,2,4-oxadiazol
-
-
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
-
-
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazole
-
-
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazole
-
-
6-(7-nitro-2,1,3-benzoxadiazol-4-ylamino)hexanol
-
-
6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol
-
-
6-butanoyl-5,7-dihydroxy-4-phenyl-2H-chromen-2-one
-
a coumarin from Mammea africana, 23% total inhibition at 0.033 mM
7-nitro-2,1,3-benzoxadiazole derivatives
-
non-GSH peptidomimetic compounds, suicide inhibitors of the enzyme, binding structure and mechanism, overview, the compounds show strong GST inhibition and accumulation in tumor cells avoiding the extrusion mechanisms mediated by the multidrug resistance protein pumps
-
bilirubin
bromosulfophthalein
chlorambucil
very poor inhibitor of the enzyme in contrast to ethacrynic acid
curcumin
daidzein
-
inhibition of isozymes GST A1-1, M1-1, and P1-1
Dichloroacetic acid
i.e. DC, used to treat lactic acidosis and has also been proposed as a novel anticancer agent is both a substrate and a mechanism-based inactivator of GSTZ1-1. Treatment with DCA progressively inactivates GSTZ1-1 and increases the elimination half-life of subsequent doses of DCA. recombinant GSTZ1*A protein is relatively resistant to DCA mediated inactivation when compared with the other isoforms
dieldrin
-
a potent reversible inhibitor toward hGSTA1-1, mixed-type inhibition, dieldrin binds specifically to the enzyme presumably at a position that partially overlaps with both the G- and H-site, a site distinct from binding of spiromesifen, binding structure overview
ellagic acid
-
inhibition of isozymes GST A1-1, A2-2, M1-1, M2-2, and P1-1, effects on substrate kinetics, overview
Ethacrynic acid
ferulic acid
-
inhibition of isozyme GST M1-1
gamma-Glu-Cys(Acm)-Gly
85.2% remaining activity at 0.0003 mM
gamma-Glu-Cys(t-buthio)-Gly
85.6% remaining activity at 0.0003 mM
gamma-Glu-Met-Gly
79.4% remaining activity at 0.0003 mM
gamma-Glu-Thi-Gly
67.4% remaining activity at 0.0003 mM
genistein
-
inhibition of isozymes GST M1-1 and M2-2
glutathione
-
competitive inhibition by the substrate
Gly-Cys-Hyp
87.4% remaining activity at 0.0003 mM
Hematin
Hyp-Cys-Ala
98.7% remaining activity at 0.0003 mM
kaempferol
-
inhibition of isozymes GST M1-1 and M2-2
L-g-glutamyl-S-[3-([5-[(5-[[5-([5-[(2-carbamimidamidoethyl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]amino)-2-hydroxy-3-oxopropyl]-L-cysteinylglycine
-
a brostallicin derivative, inhibits GSTP1-1 and GSTM2-2
L-g-glutamyl-S-[3-([5-[(5-[[5-([5-[(2-carbamimidamidoethyl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]amino)-3-oxo-2-(phosphonooxy)propyl]-L-cysteinylglycine
-
a brostallicin derivative, inhibits GSTP1-1 and GSTM2-2
N-((1E)-[4-(dimethylamino)phenyl]methylene)-2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)aniline
-
78.9% inhibition at 0.1 mM
N-(4-bromo-3-(N,N-dimethylsulfamoyl)phenyl)-2-chloroacetamide
-
-
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-2-cyanoacetamide
-
-
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-2-fluoroacetamide
-
-
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-2-oxopropanamide
-
-
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)acrylamide
-
-
N-acetyl-p-benzoquinoneimine
concentration-dependent inhibition
N-ethylmaleimide
N-[(1E)-(2-chlorophenyl)methylene]-2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)aniline
-
88.8% inhibition at 0.1 mM
N-[(1E)-(4-chlorophenyl)methylene]-2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)aniline
-
60.4% inhibition at 0.1 mM
N-[(1E)-(4-fluorophenyl)methylene]-2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)aniline
-
37.1% inhibition at 0.1 mM
N-[(1E)-(5-bromo-2-methoxyphenyl)methylene]-2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)aniline
-
646% inhibition at 0.1 mM
N1-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)oxalamide
-
-
pGlu-Cys(Trt)-Gly
82.3% remaining activity at 0.0003 mM
Prostaglandins
-
isozyme GST P1-1 forms covalent complexes with cyclopentenone prostaglandins, i.e. cyPG 15-deoxy-DELTA12,14-PGJ2 and biotinylated 15d-PGJ2, mass spectrometry analysis, overview, irreversible inhibition
-
quercetin
-
inhibition of isozymes GST M1-1 and M2-2
resveratrol
-
inhibition of isozymes GST A2-2, M1-1, M2-2, and P1-1
S-(2,4-dinitrophenyl)glutathione
-
product inhibition
S-(2,4-dinitrophenyl)GSH
-
-
S-(4-azidophenacryl)-glutathione
-
competitive inhibitor, 27% loss of activity after 5 min
S-hexyl glutathione
-
S-hexylglutathione
S-methyl-GSH
-
-
S-Methylglutathione
-
competitive
spiromesifen
-
a potent reversible inhibitor toward hGSTA1-1, mixed-type inhibition, spiromesifen binds specifically to the enzyme presumably at a position that partially overlaps with both the G- and H-site, a site distinct from binding of dieldrin, binding structure overview
Tic-Cys(Acm)-Gly
68.5% remaining activity at 0.0003 mM
Tic-Cys-Aib
80.1% remaining activity at 0.0003 mM
Tic-Cys-Sar
53% remaining activity at 0.0003 mM
Tributyltin acetate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 0.417
(+)-2-bromo-3-(4-nitrophenyl)propanoic acid
4.2 - 8.8
(R)-styrene-7,8-oxide
0.8 - 2.4
(R,R)-1-phenylpropylene oxide
0.035 - 0.1
(R,R)-trans-stilbene oxide
1.3 - 4.9
(S)-styrene-7,8-oxide
2.2 - 3.8
(S,S)-1-phenylpropylene oxide
0.08 - 0.12
(S,S)-trans-stilbene oxide
0.27 - 0.84
1,2-dichloro-4-nitrobenzene
0.13 - 1.84
1,2-epoxy-3-(p-nitrophenoxy)propane
0.6 - 1
1,3-Bis-(2-chloroethyl)-1-nitrosourea
0.17 - 6.6
1-chloro-2,4-dinitrobenzene
0.232
3,4-dinitrobenzanilide
in phosphate buffered saline, pH 7.4, at 37°C
0.002 - 0.011
7-chloro-4-nitrobenz-2-oxa-1,3-diazole
2.24
acetyl-gamma-Glu-Cys-Gly
mutant enzyme I104V/A113V, at pH 7.4 and 25°C
0.005
brostallicin
-
pH 6.5, 25°C, GSTM2-2
0.00324
cryptophycin 52
-
pH 7.4, 37°C
0.3 - 8
cumene hydroperoxide
0.06 - 0.21
Ethacrynic acid
1.48
gamma-Glu-Cys-Aib
mutant enzyme I104V/A113V, at pH 7.4 and 25°C
0.014 - 3.18
gamma-Glu-Cys-Sar
0.003 - 123.6
glutathione
0.0139 - 1.76
GSH
3.22
Hyp-Cys-Gly
wild type enzyme, at pH 7.4 and 25°C
0.083
iodobutane
pH 8.0, 30°C, recombinant wild-type enzyme
0.058
iodohexane
pH 8.0, 30°C, recombinant wild-type enzyme
0.085
iodomethane
pH 8.0, 30°C, recombinant wild-type enzyme
0.064 - 0.768
maleylacetone
1.25
Tic-Cys-Gly
wild type enzyme, at pH 7.4 and 25°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 13
(+)-2-bromo-3-(4-nitrophenyl)propanoic acid
2.7 - 4.8
(R)-styrene-7,8-oxide
0.83 - 17.7
(R,R)-1-phenylpropylene oxide
0.37 - 7.7
(R,R)-trans-stilbene oxide
2.3 - 8.4
(S)-styrene-7,8-oxide
1.1 - 9
(S,S)-1-phenylpropylene oxide
0.07 - 0.46
(S,S)-trans-stilbene oxide
110 - 320
1,2-dichloro-4-nitrobenzene
31 - 302
1,2-epoxy-3-(p-nitrophenoxy)propane
0.035 - 3.6
1,3-Bis-(2-chloroethyl)-1-nitrosourea
1.19 - 761
1-chloro-2,4-dinitrobenzene
106
1-Fluoro-2,4-dinitrobenzene
-
-
367
3,4-dinitrobenzanilide
in phosphate buffered saline, pH 7.4, at 37°C
1.03
acetyl-gamma-Glu-Cys-Gly
mutant enzyme I104V/A113V, at pH 7.4 and 25°C
200 - 9600
cumene hydroperoxide
1.91
gamma-Glu-Cys-Aib
wild type enzyme, at pH 7.4 and 25°C
0.39 - 0.56
gamma-Glu-Cys-Sar
0.17 - 47.3
glutathione
0.19 - 1700
GSH
1.04
Hyp-Cys-Gly
wild type enzyme, at pH 7.4 and 25°C
0.037
iodobutane
pH 8.0, 30°C, recombinant wild-type enzyme
0.068
iodohexane
pH 8.0, 30°C, recombinant wild-type enzyme
9.16
iodomethane
pH 8.0, 30°C, recombinant wild-type enzyme
0.347 - 464
maleylacetone
0.31
Tic-Cys-Gly
wild type enzyme, at pH 7.4 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.036 - 6.3
1,3-Bis-(2-chloroethyl)-1-nitrosourea
0.737 - 17.3
1-chloro-2,4-dinitrobenzene
0.46
acetyl-gamma-Glu-Cys-Gly
mutant enzyme I104V/A113V, at pH 7.4 and 25°C
4 - 11
brostallicin
1.29
gamma-Glu-Cys-Aib
wild type enzyme, at pH 7.4 and 25°C
0.12 - 39.68
gamma-Glu-Cys-Sar
0.00304 - 34
glutathione
0.32
Hyp-Cys-Gly
wild type enzyme, at pH 7.4 and 25°C
0.701
iodobutane
pH 8.0, 30°C, recombinant wild-type enzyme
1.17
iodohexane
pH 8.0, 30°C, recombinant wild-type enzyme
107
iodomethane
pH 8.0, 30°C, recombinant wild-type enzyme
0.25
Tic-Cys-Gly
wild type enzyme, at pH 7.4 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
1-chloro-2,4-dinitrobenzene
-
pH 6.5, 25°C, GSTM2-2
0.071
2-([(1-methyl-1H-pyrrol-2-yl)sulfonyl]methyl)-N-[(1E)-(4-nitrophenyl)methylene]aniline
-
pH 6.5, 25°C
0.00061
2-chloro-N-(3-(morpholinosulfonyl)-4-(trifluoromethyl)phenyl)-acetamide
-
at pH 8.0 and 37°C
0.0012
2-chloro-N-(3-(N,N-dimethylsulfamoyl)-4-(trifluoromethyl)-phenyl)acetamide
-
at pH 8.0 and 37°C
0.00044
2-chloro-N-[4-chloro-3-(N,N-dimethylsulfamoyl)phenyl]acetamide
-
at pH 8.0 and 37°C
0.00021 - 0.0088
5,8-dihydroxy-1-(hydroxymethyl)naphtho[2,3-c]furan-4,9-dione
0.068
bromosulfophthalein
-
minor form
0.0001 - 0.0023
dieldrin
0.028
glutathione
-
pH 6.5, 25°C, GSTM2-2
0.002 - 0.032
Hematin
0.1
S-Methylglutathione
-
-
0.0004 - 0.0021
spiromesifen
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
1-(4-benzylpiperidin-1-yl)prop-2-en-1-one
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.01
1-(4-phenylpiperidin-1-yl)prop-2-en-1-one
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.00129
2-chloro-N,N-dimethyl-5-(vinylsulfonamido)-benzenesulfonamide
Homo sapiens
at pH 8.0 and 37°C
0.0000056
2-chloro-N-(4-(2-hydroxyphenyl)thiazol-2-yl)-N-((3-methylisoxazol-5-yl)methyl)acetamide
Homo sapiens
at pH 8.0 and 37°C
0.000021
2-chloro-N-[4-chloro-3-(N,N-dimethylsulfamoyl)phenyl]acetamide
Homo sapiens
at pH 8.0 and 37°C
0.00027
ethyl 2-acrylamido-4-phenylthiazole-5-carboxylate
Homo sapiens
at pH 8.0 and 37°C
0.00101
ethyl 2-acrylamido-4-phenylthiophene-3-carboxylate
Homo sapiens
at pH 8.0 and 37°C
0.00022
ethyl 2-acrylamido-5-phenylthiophene-3-carboxylate
Homo sapiens
at pH 8.0 and 37°C
0.00057
ethyl N-acryloyl-N-(4-phenylthiazol-2-yl)glycinate
Homo sapiens
at pH 8.0 and 37°C
0.01
methyl (E)-4-((4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-amino)but-2-enoate
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.00037
methyl N-acryloyl-N-(4-phenylthiazol-2-yl)glycinate
Homo sapiens
at pH 8.0 and 37°C
0.00000032
N-((3-methylisoxazol-5-yl )methyl)-N-(4-(4-chloro-2-hydroxylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00000022
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(2-hydroxylphenyl)-thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00036
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(2-methoxyphenyl)-thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00004
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(4-fluoro-2-hydroxylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.000025
N-((3-methylisoxazol-5-yl)methyl)-N-(4-(4-trifluoromethylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.000051
N-((3-methylisoxazol-5-yl)methyl)-N-(4-phenylthiazol-2-yl)-acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.01
N-(1-benzyl-1H-pyrazol-4-yl)acrylamide
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.01
N-(1-phenyl-1H-pyrazol-4-yl)acrylamide
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.00023
N-(2-((2-morpholinoethyl)amino)-2-oxoethyl)-N-(4-phenylthiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00008
N-(2-(cyclohexylamino)-2-oxoethyl)-N-(4-phenylthiazol-2-yl)-acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00003
N-(2-(oxetan-3-ylamino)-2-oxoethyl)-N-(4-phenylthiazol-2-yl)-acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00053
N-(2-morpholino-2-oxoethyl)-N-(4-phenylthiazol-2-yl)-acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00088
N-(4-(2-chlorophenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00158
N-(4-(2-fluorophenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00086
N-(4-(2-hydroxylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00019
N-(4-(2-hydroxyphenyl)thiophen-2-yl)-N-((3-methylisoxazol-5-yl)methyl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.01
N-(4-(2-methoxyphenyl)thiazol-2-yl)acrylamide
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.00122
N-(4-(3,4-dioxylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.0006
N-(4-(3-chlorophenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00017
N-(4-(4-chlorophenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.01
N-(4-(4-hydroxylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.00449
N-(4-(4-methoxyphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00081
N-(4-(4-methylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.0003
N-(4-(4-trifluoromethylphenyl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.0004
N-(4-(naphthalen-2-yl)thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00314
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00311
N-(4-phenyl-5-methyl-thiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00074
N-(4-phenylthiazol-2-yl)-N-(pyridin-3-ylmethyl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00047
N-(4-phenylthiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00103
N-(5-phenylthiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00204
N-acryloyl-N-(4-phenylthiazol-2-yl)glycine
Homo sapiens
at pH 8.0 and 37°C
0.00072
N-benzyl-N-(4-phenylthiazol-2-yl)acrylamide
Homo sapiens
at pH 8.0 and 37°C
0.00015
tert-butyl N-acryloyl-N-(4-phenylthiazol-2-yl)glycinate
Homo sapiens
at pH 8.0 and 37°C
0.0008
(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)methanesulfonyl fluoride
Homo sapiens
-
at pH 8.0 and 37°C
0.01
(E)-2-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)ethene-1-sulfonyl fluoride
Homo sapiens
-
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.1
(E)-N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)but-2-enamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 37°C
0.01
2-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)ethane-1-sulfonyl fluoride
Homo sapiens
-
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.00001 - 0.011
2-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)imidazole
0.1
2-chloro-5-((cyanomethyl)amino)-N,N-dimethylbenzenesulfonamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 37°C
0.1
2-chloro-N,N-dimethyl-5 -(oxiran-2-ylmethyl) -benzenesulfonamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 37°C
0.0012
2-chloro-N,N-dimethyl-5-(oxiran-2-yl)benzenesulfonamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00071
2-chloro-N-(2-(N,N-dimethylsulfamoyl)-[1,1'-biphenyl]-4-yl)-acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00025
2-chloro-N-(3-(morpholinosulfonyl)-4-(trifluoromethyl)phenyl)-acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00021
2-chloro-N-(3-(N,N-dimethylsulfamoyl)-4-(trifluoromethoxy)-phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00006
2-chloro-N-(3-(N,N-dimethylsulfamoyl)-4-(trifluoromethyl)-phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00013
2-chloro-N-(3-(N,N-dimethylsulfamoyl)-4-iodophenyl)-acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00016
2-chloro-N-(4-chloro-3-(morpholinosulfonyl)phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.01
2-chloro-N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-propanamide
Homo sapiens
-
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.0002
2-chloro-N-(4-chloro-3-(N-((tetrahydrofuran-2-yl)methyl)-sulfamoyl)phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00018
2-chloro-N-(4-chloro-3-(N-(2-hydroxyethyl)-N-methylsulfamoyl)phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.0007
2-chloro-N-(4-chloro-3-(N-(2-hydroxyethyl)sulfamoyl)phenyl)-acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00008
2-chloro-N-(4-chloro-3-(N-(2-methoxyethyl)-N-methylsulfamoyl)phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00003
2-chloro-N-(4-chloro-3-(N-(2-methoxyethyl)sulfamoyl)phenyl)-acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00016
2-chloro-N-(4-chloro-3-(N-(3-methoxypropyl)-N-methylsulfamoyl)phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00011
2-chloro-N-(4-chloro-3-(N-(3-methoxypropyl)sulfamoyl)phenyl)-acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00034
2-chloro-N-(4-chloro-3-(N-(tetrahydrofuran-3-yl)sulfamoyl)-phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00007
2-chloro-N-(4-chloro-3-(N-isopropylsulfamoyl)phenyl)-acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00058
2-chloro-N-(4-chloro-3-(N-methylsulfamoyl)phenyl)acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.00013
2-chloro-N-[4-chloro-3-(N,N-dimethylsulfamoyl)phenyl]acetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.0032
3-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)propane-1-sulfonyl fluoride
Homo sapiens
-
at pH 8.0 and 37°C
0.0003 - 0.066
3-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)propionic acid
0.01
3-chloro-N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-propenamide
Homo sapiens
-
IC50 above 0.01 mM, at pH 8.0 and 37°C
0.00003 - 0.056
4-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)butanol
0.06
4-(acryloylamino)-N-(5-[[5-([5-[(2-carbamimidamidoethyl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)-1-methyl-1H-pyrrole-2-carboxamide
Homo sapiens
-
pH 6.5, 25°C, with isozyme GSTM2-2
0.0068
5,8-dihydroxy-1-(hydroxymethyl)naphtho[2,3-c]furan-4,9-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0054
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-chlorobenzyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0039
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0038
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-methoxyphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0033
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-nitrobenzyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.04
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.004
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0036
5-[2,3-dichloro-4-(2-methylene-1-oxobutyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.002
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-chlorobenzyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0024
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0034
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-hydroxyphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0023
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-nitrobenzyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0039
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.004
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0018
5-[2,3-dimethyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0014
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0013
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0032
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.002
5-[3-bromo-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0007
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0007
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0021
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0006
5-[3-chloro-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0035
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-fluorophenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0021
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-hydroxyphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0029
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-nitrobenzyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0033
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-(4-trifluoromethylphenyl)-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.005
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-methyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.002
5-[3-methyl-4-(2-methylene-1-oxopropyl)phenoxymethyl]-3-phenyl-1,2,4-oxadiazol
Homo sapiens
-
25°C, isozyme GSTP1-1
0.0018 - 0.1
6-(7-nitro-2,1,3-benzoxadiazol-4-ylamino)hexanol
0.00001 - 0.025
6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol
0.00004 - 0.005
curcumin
Homo sapiens
-
pH 7.4, 30°C, purified recombinant isozymes GST A1-1, A2-2, M1-1, M2-2, and P1-1
0.0179 - 0.0983
dieldrin
0.00013 - 0.005
ellagic acid
Homo sapiens
-
pH 7.4, 30°C, purified recombinant isozymes GST A1-1, A2-2, M1-1, M2-2, and P1-1
0.0034
Ethacrynic acid
Homo sapiens
-
-
0.004 - 0.005
genistein
Homo sapiens
-
pH 7.4, 30°C, purified recombinant isozymes GST M1-1 and M2-2
0.001 - 0.002
kaempferol
Homo sapiens
-
pH 7.4, 30°C, purified recombinant isozymes GST M1-1 and M2-2
0.00015
N-(4-bromo-3-(N,N-dimethylsulfamoyl)phenyl)-2-chloroacetamide
Homo sapiens
-
at pH 8.0 and 37°C
0.1
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-2-cyanoacetamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 37°C
0.1
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-2-fluoroacetamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 8.0 and 37°C
0.01
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)-2-oxopropanamide
Homo sapiens
-
IC50 above 0.01 mM, at pH 8.0 and 37°C
1
N-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)acrylamide
Homo sapiens
-
IC50 above 1.0 mM, at pH 8.0 and 37°C
1
N1-(4-chloro-3-(N,N-dimethylsulfamoyl)phenyl)oxalamide
Homo sapiens
-
IC50 above 1.0 mM, at pH 8.0 and 37°C
0.0003 - 0.0005
quercetin
Homo sapiens
-
pH 7.4, 30°C, purified recombinant isozymes GST M1-1 and M2-2
0.0121 - 0.0795
spiromesifen
additional information
additional information
Homo sapiens
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0029 - 0.0036
-
with 1-chloro-2,4-dinitrobenzene as substrate
0.019
mutant enzyme D90N, in phosphate buffer (pH 6.5), at 25°C
0.03
-
with cumene hydroperoxide as substrate
0.039
using 3-iodopropylbenzene as substrate
0.066
using 3-iodopropylbenzene as substrate
0.07
-
with styrene oxide as substrate
0.081
using 1,6-diiodohexane as substrate
0.086
using iodohexane as substrate
0.0936
-
-
0.1
using 3-iodopropylbenzene as substrate
0.18
mutant enzyme R74Q, in phosphate buffer (pH 6.5), at 25°C
0.335
purified recombinant enzyme, substrate 2-hydroxyethyl disulfide
0.37
-
with 1,2-epoxy-3-(4-nitrophenoxy)propane as substrate
0.5
mutant enzyme Y7F, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5
0.53
isozyme GST A2-2, using azathioprine as a substrate
0.56
using 1,4-diiodobutane as substrate
0.7
-
with adenine propenal, isoenzyme A1-1
0.81
using 1,4-diiodobutane as substrate
0.84 - 0.92
-
with glutathione as substrate
0.86
-
with acrolein, isoenzyme A1-1
0.91
using 1,4-diiodobutane as substrate
1.03
using 1,6-diiodohexane as substrate
1.38
using iodohexane as substrate
1.4
mutant enzyme A113V, with ethacrynic acid
1.5 - 8.3
-
with cumene hydroperoxide as substrate
1.7
wild type enzyme, with ethacrynic acid
1.8
mutant enzyme I104V, with ethacrynic acid
10.45
purified recombinant enzyme, substrate 1-chloro-2,4-dinitrobenzene in absence of 10 mM EDTA
102
mutant enzyme T67A, in phosphate buffer (pH 6.5), at 25°C
105
-
with 1-chloro-2,4-dinitrobenzene as substrate
129
-
purified recombinant isozyme GST P1-1
14.56
purified recombinant enzyme, substrate 1-chloro-2,4-dinitrobenzene in presence of 10 mM EDTA
157
-
purified recombinant isozyme GST M1-1
16
-
isoenzyme beta
16.4
-
-
17
-
isoenzyme gamma
182
-
purified recombinant isozyme GST M2-2
2.52
mutant enzyme C14A/C47A/C101A/C169A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5
254.9
-
-
26.3
-
with acrolein, isoenzyme P1-1
3
mutant enzyme I104V/A113V, with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole
3 - 3.9
using 1,2-diiodoethane as substrate
3.4
mutant enzyme R70Q, in phosphate buffer (pH 6.5), at 25°C
31.5
using 1,2-diiodoethane as substrate
33 - 94
-
with 1-chloro-2,4-dinitrobenzene as substrate
34
-
isoenzyme epsilon
36.13
mutant enzyme C47A/C101A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5
37
-
isoenzyme delta
4
mutant enzyme A113V, with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole
4.75
mutant enzyme C14A/C47A/C101A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5
4.96
-
purified wild-type GST T1-1, substrate 1-iodomethane
53.2
isozyme GST A2-2, using 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole as a substrate
56.4
using 1,2-diiodoethane as substrate
56.5 - 79.4
-
-
60
mutant enzyme I104V, with 1-chloro-2,4-dinitrobenzene
61.07
His-tagged wild type enzyme, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5
61.8
isozyme GST A1-1, using 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole as a substrate
66
-
species with very low isoelectric point from erythrocytes
7.05
-
with acrolein, isoenzyme M1-1
7.26
isozyme GST A3-3, using 1-methyl-4-nitro-5-(4-nitrophenylthio)-1H-imidazole as a substrate
7.84
-
purified wild-type GST T1-1, substrate 1,2-epoxy-3-(4-nitro-phenoxy)propane
70
mutant enzyme I104V/A113V, with 1-chloro-2,4-dinitrobenzene
71.7
untagged wild type enzyme, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5
75
wild type enzyme, in phosphate buffer (pH 6.5)
77
-
with adenine propenal, isoenzyme P1-1
78
-
purified recombinant isozyme GST A2-2
80 - 272
-
with 1-chloro-2,4-dinitrobenzene as substrate
84
-
purified recombinant isozyme GST A1-1
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
activity with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid
6.5 - 8
assay at, dependent on the substrate
6.8
-
assay at
7
-
assay at
7.5
assay at
7.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 11
-
pH 6.5: about 65% of maximal activity, pH 11: about 85% of maximal activity, activity with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
assay at
24
-
aasay at
25 - 30
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
a small cell lung carcinoma cell line
Manually annotated by BRENDA team
-
a myeloid leukemia cell line
Manually annotated by BRENDA team
-
GSTP1-1 is overexpressed in liver cancer cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
malfunction
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
physiological 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. GSTO1 is a determinant of the age at onset of Alzheimer's and Parkinson's diseases
evolution
malfunction
metabolism
-
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
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GSTO1_HUMAN
241
0
27566
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
2 * 22000, SDS-PAGE
23000
24300
-
x * 24300, recombinant His6-tagged wild-type GSTZ1-1, SDS-PAGE
25000
-
2 * 25000, basic isoenzyme, SDS-PAGE
25200
-
2 * 25200, form I-XII, SDS-PAGE
25500
25600
-
2 * 25600, form XIII, SDS-PAGE
25630
His-tagged wild type enzyme, calculated from amino acid sequence
45000
45000 - 49000
-
-
47000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 24300, recombinant His6-tagged wild-type GSTZ1-1, SDS-PAGE
homodimer
monomer or dimer
the class GST occurs in a monomer-dimer equilibrium
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 100 mM MES pH 6.5, 25% (w/v) poly(ethylene glycol) 3350, and 3% (v/v) methanol
enzyme in complex with GSH is determined at 2.4 A
-
hanging drop vapor diffusion method, using 1.7-2.2 M (NH4)2SO4, 0.2 M sodium potassium tartrate, 0.75 mM ZnSO4, 17 mM citric acid
-
hanging drop vapour diffusion method
in complex with chlorambucil, hanging drop vapour diffusion method
purified isozyme GST A1-1 in complex with substrate glutathione, hanging drop vapour diffusion method, room temperature, 10 mg/ml protein in 0.1 M Tris-HCl, pH 8.5, with 19% methyl PEG 2000, 0.03 M sodium acetate, pH 4.6, and 1% 2-mercaptoethanol for the apoenzyme, or in 0.1 M Tris–HCl, pH 7.8, with 24% PEG 4000, and 1% 2-mercaptoethanol, with glutathione for wild-type and mutant enzyme complexed with the substrate, the mutant apoenzyme is crystallized from 0.1 M Tris–HCl, pH 7.8, with 24% PEG 4000, 2 mM DTT and 30% MPD, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
purified recombinant hGSTk in apo-form and in complex with S-hexylglutathione, hanging drop vapour diffusion method, apo-form of hGSTk in 20 mM NaH2PO4, pH 7.4, 20 mM NaCl, 1 mM EDTA and 7.2 mM 2-mercaptoethanol, hGSTk in complex in 20 mM HEPES, pH 7.0, 50 mM NaCl, 1 mM EDTA and 1 mM DTT, supplemented with S-hexylglutathione at a molar ratio of 1:2, is mixed with an equal volume of reservoir solution containing 0.2 M NaSCN and 20% PEG3350, 20°C, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution
-
purified recombinant wild-type and mutant isozyme GST T1-1 complexed with S-hexyl-glutathione and the 1-iodohexane-glutathione conjugate, X-ray diffraction structure determination and analysis at 1.5-2.4 A resolution
-
purified recombinant wild-type isozyme GSTA4-4 and recombinant mutant GSTA1-1 GIMFhelix in complex with reaction product 4-hydroxynonenal-3S-glutathione, 0.002 ml of protein solution containing 10 mg/ml protein in 10 mM HEPES, pH 7.0, with a 10fold molar excess of ligand are mixed with 0.002 ml of reservoir solution containing containing 24% PEG 4000, 0.1 M sodium acetate trihydrate, pH 4.6, and 0.2 M ammonium sulfate, or mixing of 0.002 ml protein solution with 500 nl of EtOH and 0.003 ml of reservoir solution containing 16% PEG monomethyl ester 5000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, X-ray diffraction structure determination and analysis at 1.90-2.10 A resolution, molecular replacement
-
recombinant I71A and I71V hGSTA1-1, hanging drop vapour diffusion method, protein solution, containing 10 mg/ml I71A hGSTA1-1 or 15 mg/ml I71V hGSTA1-1 in 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, 2.5 mM S-hexylglutathione and 0.02% sodium azide is mixed with an equal volume of reservoir solution containing 19%w/v PEG 4000, 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, and 0.02% sodium azide, 20°C, X-ray diffraction structure determmination and analysis at 1.75-2.51 A resolution
recombinant mutant R15L isozyme GSTA1-1 complexed with inhibitor S-hexylglutathione, hanging drop vapor diffusion method, 0.002 ml of 14 mg/ml R15L GSTA1-1 in 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, 0.02% sodium azide solution are mixed with 0.002 ml of reservoir buffer containing 5 mM S-hexylglutathione, 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, 5-30% PEG 2000 or 4000, equilibration against 1 ml reservoir solution, 3 days, X-ray diffraction structure determination and analysis at 1.80 A resolution, molecular replacement method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A140D
naturally occuring mutation, most common missense polymorphism found in each of the populations studied so far, the substitution involves a charge change it does not seem to have a significant effect on enzymatic activity with a range of substrates
A236V
naturally occuring mutation, the substitution occurs in individuals from Chile and Mexico
C32Y
naturally occuring mutation at the primary active site residue, the rare C32Y substitution is identified in Europeans and appears to degrade rapidly. This variant does not catalyze the typical thioltransferase and reductase reactions that are a feature of the Omega class GSTs
delE155
naturally occuring mutation, the polymorphic deletion of E155, from the deletion of AGG from the 5' splice donor site of exon 4, occurs at a low frequency in most populations and is strongly linked to K208 in Europeans and to E208 in Chinese individuals. Although active enzyme can be expressed in Escherichia coli, the delE155 enzyme appears to be unstable in vivo. T47D cells that are hemizygous for the GSTO1delE155 allele are completely deficient in GSTO1-1 activity. Variable protein expression in platelets found evidence that the delE155 enzyme is present in platelets obtained from subjects that are heterozygous for the GSTO1delE155, K208 allele
E208K
naturally occuring mutation, the single E208K substitution alone, created independently of the E155 deletion, does not have a significant impact on activity. Variable protein expression in platelets found evidence that the delE155 enzyme is present in platelets obtained from subjects that are heterozygous for the GSTO1delE155, K208 allele
A113V
wild type specific activity with 1-chloro-2,4-dinitrobenzene
A85S
a naturally occuring polymorphism in Caucasian population
C115A
-
mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity
C130Y
naturally occuring mutation, the substitution is rare and may generate unstable protein
C14A/C47A/C101A
mutant shows 92% decrease in the specific activity towards 1-chloro-2,4-dinitrobenzene compared to the His-tagged wild type enzyme
C14A/C47A/C101A/C169A
mutant shows 96% decrease in the specific activity towards 1-chloro-2,4-dinitrobenzene compared to the His-tagged wild type enzyme
C14S/T226I/W234R
-
construction of chimeric mutant F2:1215 comprising sequences from the human isozymes GST-T1-1 and GST-T2, as well as from the GST-T1-1 of Mus musculus, the mutant F2:1215 shows highly increased activity compared to the human enzyme and increased activity compared to the murine enzyme, overview
C16A
-
mutation causes a high increase in the KM-value. Mutation diminishes activity with both chlorofluoroacetic acid and maleylacetone but shows significantly elevated activity with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid as a substrate. This elevated activity appears to be driven by a high turnover number. The diminished activity with maleylacetone results from a low turnover number
C174A
-
mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity
C47A/C101A
mutant shows 41% decrease in the specific activity towards 1-chloro-2,4-dinitrobenzene compared to the His-tagged wild type enzyme
C47S/C101S
C78A
-
mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity
C87A/C115A/C174A/M212C
-
site-directed mutagensis of isozyme GST M2-2, mutation of the catalytic site residue M212 and of all cysteines, the mutant shows altered substrate specificity compared to the wild-type isozyme. C87A/C115A/C174A/M212C, which serves as the parental enzyme for the alkylated variants, is more active than mutant C87A/C115A/C174A with 1-chloro-2,4-dinitrobenzene, cyanoDMNG, and aminochrome but shows only half of the NPG activity. Effects of alkylation of the C87A/C115A/C174A/M212C mutant on the substrate selectivity profile, overview
C88A
-
mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity
D141N
site-directed mutagenesis of isozyme GST T1-1, the mutant enzyme behaves similarly to the wild-type enzyme, in terms of expression level and specific activity. The mutant activity with ethidium bromide is highly reduced compared to the wild-type enzyme
D201A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
D43N
naturally occuring mutation, the mutant is expressed at low levels causing GSTT1 deficiency
D69A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
D69T
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
D90N
greatly decreased specific activity, shows no appreciable changes in Km for 1-chloro-2,4-dinitrobenzene and has similar circular dichroism spectra to that of wild type enzyme, the dimer-monomer equilibrium is shifted toward monomer
D94N
greatly decreased specific activity, shows no appreciable changes in Km for 1-chloro-2,4-dinitrobenzene and has similar circular dichroism spectra to that of wild type enzyme, the dimer-monomer equilibrium is shifted toward monomer
E173K
site-directed mutagenesis of isozyme GST T1-1, the mutant shows reduced expression levels and enzyme activity with all substrates compared to the wild-type enzyme. The mutant is not active with ethidium bromide
F83A
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
F83W
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
F87A
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
F87W
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
G112C
-
mutant displays as high catalytic activity as wild type GST M1-1
G147W
the natural polymorphism occurs in a rare variant in Chinese individual
G147W/V224I
site-directed mutagenesis, the double mutation results in a gain of function with a three fold increase in the specific activity with 1-chloro-2,4-dinitrobenzene as a substrate. This increase in activity appears to result from a decrease in the Km GSH and a large increase in the catalytic efficiency of the enzyme
I104V
I104V/A113V
I10A/G112C
-
mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity
I10C
-
mutant displays significant decrease in 1-chloro-2,4-dinitrobenzene activity
I44A
-
site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
I71V
site-directed mutagensis, structure analysis
II71A
site-directed mutagensis, structure analysis
K62A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
K62E
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
L158I
naturally occuring mutation, the substitution is rare and may generate unstable protein
L15A
-
site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
L183A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
L58A
-
site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
L88A
-
site-directed mutagenesis, H-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
L92A
-
site-directed mutagenesis, H-site mutation, inactive mutant
M212C
-
site-directed mutagensis of isozyme GST M2-2, mutation of the catalytic site residue M212. Additionall chemical modifications at mutant Cys212, e.g. by attachment of alkyl chains, alter the substrate specificity and activity of the mutant enzyme with alternative substrates, effects of alkylation of the C87A/C115A/C174A/M212C mutant on the substrate selectivity profile, overview
M66A
-
site-directed mutagenesis, H-site mutation, inactive mutant
M91A
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
M91K
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
N142D
naturally occuring mutation, the N142D substitution is the most frequent in all populations studied so far and does not appear to influence catalytic activity or stability
N53A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
P17A
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
P55A
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
R15L
site-directed mutagenesis, the mutation substantially diminishes the 1-chloro-2,4-dinitrobenzene-GSH conjugating activity of the enzyme, it has little effect on protein structure and stability
R175A
-
mutation results in a significant lowering of the turnover number for (+)-2-bromo-3-(4-nitrophenyl)propanoic acid and maleylacetone, elevated KM-value for maleylacetone
R175K
-
mutation results in a significant lowering of the turnover number for (+)-2-bromo-3-(4-nitrophenyl)propanoic acid and maleylacetone
R202A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
R70Q
greatly decreased specific activity, shows no appreciable changes in Km for 1-chloro-2,4-dinitrobenzene and has similar circular dichroism spectra to that of wild type enzyme, the dimer-monomer equilibrium is shifted toward monomer
R74Q
greatly decreased specific activity, shows no appreciable changes in Km for 1-chloro-2,4-dinitrobenzene and has similar circular dichroism spectra to that of wild type enzyme, the dimer-monomer equilibrium is shifted toward monomer
S112T
naturally occuring polymorphism, recombinant enzyme containing the S110 allele has elevated activity towards 4-nitrophenylacetate and azathioprene and lower activity with 1-chloro-2,4-dinitrobenzene and organic hydroperoxides compared to the wild-type. The T112 substitution causes a reduction in levels of GSTA2-2 to around 25% of those associated with the other haplotypes
S14A
-
inactive mutant enzyme
S15A
-
mutant enzyme shows low isomerase activity with maleylacetone as a substrate (about 15% of wild-type) and low activity with chlorofluoroacetic acid, it shows elevated activity with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid as the substrate
S16A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
S19A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
S200A
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
T104P
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
T65M
naturally occuring mutation, the mutant is expressed at low levels causing GSTT1 deficiency
T67A
increased specific activity
T68E
-
site-directed mutagenesis, crystal structure comparison with the wild-type isozyme GST-A1-1, overview
V169
naturally occuring mutation, the mutant is expressed at low levels causing GSTT1 deficiency
V224I
a naturally occuring polymorphism common in African, Asian and European individuals
V41I
naturally occuring mutation, catalytic activity of the V41I substitution is not evaluated but the expressed protein appears to be stable.
W126A
-
site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme
W234K
-
site-directed mutagenesis, isozyme GST T1-1, the mutant shows altered substrate specificity compared to the wild-type enzyme
W234R
Y108A
-
mutant enzyme shows 58% of the wild-type activity with 1,2-dichloro-4-nitrobenzene as substrate and 37% of the wild-type activity with 1,2-epoxy-3-(p-nitrophenoxy)propane, 2% of the wild-type GSH peroxidase activity towards cumene hydroperoxide and 163% of the wild-type steroid isomerase activity towards DELTA5-androstene-3,17-dione
Y108F
-
mutant enzyme is as active as wild-type enzyme with 1,2-dichloro-4-nitrobenzene as substrate and shows 7% of the wild-type activity with 1,2-epoxy-3-(p-nitrophenoxy)propane, 77% of the wild-type GSH peroxidase activity towards cumene hydroperoxide and 149% of the wild-type steroid isomerase activity towards DELTA5-androstene-3,17-dione. Mutation results in an approximately 3fold decrease in the I50 value of S-methyl-GSH
Y108W
-
mutant enzyme shows 215% of the wild-type activity with 1,2-dichloro-4-nitrobenzene as substrate and 35% of the wild-type activity with 1,2-epoxy-3-(p-nitrophenoxy)propane, 16% of the wild-type GSH peroxidase activity towards cumene hydroperoxide and 36% of the wild-type steroid isomerase activity towards DELTA5-androstene-3,17-dione. Mutation results in an approximately 3fold decrease in the I50 value of S-methyl-GSH. Lower heat stability than wild-type enzyme
Y18A
-
site-directed mutagenesis, G-site mutation, inactive mutant
Y18F
-
site-directed mutagenesis, G-site mutation, the mutant shows reduced activity compared to the wild-type enzyme
Y18H
-
site-directed mutagenesis, G-site mutation, inactive mutant
Y18L
-
site-directed mutagenesis, G-site mutation, inactive mutant
Y7F
mutant shows 99% decrease in the specific activity towards 1-chloro-2,4-dinitrobenzene compared to the His-tagged wild type enzyme
Y9F
-
site-directed mutagenesis of isozyme GSTA4-4
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 50
the I105 variant and the V105 variant show different stability
53
-
midpoint of inactivation of mutant enzyme Y108W
77
-
midpoint of inactivation of wild-type enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
guanidine hydrochloride, 6 M, denaturation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
13 isoforms
-
3 forms, homogeneity
-
an acidic and a basic form
-
forms: alpha, beta, gamma, delta, epsilon and a species with a very low isoelectric point
-
glutathione Sepharose column chromatography
-
GSH-affinity column chromatography
-
GST pi
-
GSTrap-Hp column chromatography
hexyl-glutathione-agarose bead chromatography
IDA-Ni2+ affinity column chromatography and glutathione Sepharose 4B column chromatography
isoenzyme P1-1
-
multiple forms
-
Ni-IMAC affinity column chromatography
Ni-NTA column chromatography
nickel-agarose column chromatography
nickel-immobilized metal ion affinity chromatography
P1-1, A1-1 and M1-1
-
recombinant
-
recombinant GSTP1-1 from Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and dialysis
-
recombinant His-tagged isozyme GSTO2 by glutathione affinity chromatography
recombinant His6-tagged wild-type hGSTZ1-1 and mutant seleno-hGSTZ1-1 from HEK-293T cells by nickel affinity chromatography
-
recombinant isozyme GSTA1-1 from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography
-
recombinant isozyme GSTA1-1 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, recombinant His-tagged isozymes GSTO1-1 and GSTT2-2 in Escherichia coli strain M15[pREP4] by nickel affinity chromatography
-
recombinant isozymes from Escherichia coli by S-hexylglutathione affinity chromatography to homogeneity
-
recombinant isozymes GST A1-1 and GST A4-4 and recombinant mutant GIMFhelix from Escherichia coli by glutathione affinity chromatography
-
recombinant isozymes GSTP1-1 and GSTM2-2 from Escherichia coli
-
recombinant wild-type and mutant enzymes from Escherichia coli by cation exchange chromatography and S-hexylglutathione affinity chromatography, respectively
-
recombinant wild-type and mutant isozyme GSTA4-4, and recombinant isozyme GSTA1-1GIMFhelix mutant from Escherichia coli by glutathione affinity chromatography and gel filtration
-
recombinant wild-type and mutant N-terminally His6-tagged isozymes GST T1-1 from Escherichia coli strain XL-1 blue by nickel affinity chromatography
-
recombinant wild-type and mutant R15L isozyme GSTA1-1 from Escherichia coli strain BL21(DE3) by ion exchange chromatography
wild type and mutants
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GSTO1, localized at 10q25.1, phylogenetic classification of the cytosolic GSTs, overview
co-expression of HA-tagged GST P1 with Flag-tagged DELTAMEKK1 in HEK-293 cells, the overexpression of isozyme GST P1 leads to inhibition of both DELTAMEKK1- and etoposide-induced apoptosis, and inhibition of procaspase-3 activation and PARP cleavage, overview
-
construction of large libraries of isozyme GST T1-1 constructed by error prone PCR, DNA shuffling, saturation mutagenesis, or a random mutagenesis in conjunction with homologous recombination, screening for improved catalytic activity towards CMAC in a quantitative fashion using flow cytometry, up to a 20000fold increase in kcat/KM compared to wild-type GSTT1-1 is achieved, residue Trp234 is important, overview, recombinant expression of wild-type and mutants as His6-tagged enzymes
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli XL-1 Blue cells
expression of His-tagged enzyme in Escherichia coli
-
expression of isozyme GSTA1-1 in Escherichia coli strain BL21 (DE3)
-
expression of isozymes in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli
-
expression of wild-type and mutant isozyme GST T1-1
-
expression of wild-type and mutant isozyme GSTA4-4, and of isozyme GSTA1-1GIMFhelix mutant in Escherichia coli
-
expression of wild-type and mutant N-terminally His6-tagged isozymes GST T1-1 in Escherichia coli strain XL-1 blue
-
expression of wild-type GSTA1-1 and mutants in Escherichia coli strain BL21 (DE3) pLysS
gene GSTA1, localized at 6p12.2, phylogenetic classification of the cytosolic GSTs, overview. Expression in HepG2, GLC4 and Caco-2 cell lines
gene GSTA2, localized at 6p12.2, phylogenetic classification of the cytosolic GSTs, overview
gene GSTA3, localized at 6p12.2, phylogenetic classification of the cytosolic GSTs, overview
gene GSTA4, localized at 6p12.2, phylogenetic classification of the cytosolic GSTs, overview
gene GSTA5, localized at 6p12.2, phylogenetic classification of the cytosolic GSTs, overview
gene GSTM1, localized at 1p13.3, phylogenetic classification of the cytosolic GSTs, overview
gene GSTM2, localized at 1p13.3, phylogenetic classification of the cytosolic GSTs, overview
gene GSTM3, localized at 1p13.3, phylogenetic classification of the cytosolic GSTs, overview
gene GSTM4, localized at 1p13.3, phylogenetic classification of the cytosolic GSTs, overview
gene GSTM5, localized at 1p13.3, phylogenetic classification of the cytosolic GSTs, overview
gene GSTO2, localized at 10q25.1, phylogenetic classification of the cytosolic GSTs, overview
gene GSTP1, localized at 11p13.3, phylogenetic classification of the cytosolic GSTs, overview
gene GSTS1, localized at 4q22.3, phylogenetic classification of the cytosolic GSTs, overview
gene GSTT1, localized at 22q11.23, phylogenetic classification of the cytosolic GSTs, overview
gene GSTZ1, localized at 14q24.3, phylogenetic classification of the cytosolic GSTs, overview
genes GSTT2 and GSTT2B, localized at 22q11.23, phylogenetic classification of the cytosolic GSTs, overview
GSTP1-1 expression in Escherichia coli
-
isozyme GSTA1-1 expression in Escherichia coli strain BL21(DE3), expression of His-tagged isozymes GSTO1-1 and GSTT2-2 in Escherichia coli strain M15[pREP4]
-
isozyme GSTO2, cloning from a human fetal brain cDNA library, DNA and amino acid sequence determination and analysis, expression analysis, expression of isozyme GSTO2-EGFP fusion protein in cytoplasm of COS-7 cells and in cytoplasma and nucleus of L-02, QGY-7703 and SMMC-7721 cells, expression of His-tagged isozyme GSTO2 in Escherichia coli strain M15
isozymes GST A1-1 and GST A4-4, expression in Escherichia coli strain XL-1 Blue, expression of mutant GIMFhelix in Escherichia coli strain Rosetta-gami B(DE3)
-
isozymes GSTP1-1 and GSTM2-2, expression in Escherichia coli
-
mutant enzymes expressed in Escherichia coli
overexpression of wild-type and mutant R15L isozyme GSTA1-1 in Escherichia coli strain BL21(DE3)
recombinant expression of the His6-tagged wild-type and mutant isozymes GST T1-1 in Escherichia coli
-
transient expression of His6-tagged wild-type hGSTZ1-1 and mutant seleno-hGSTZ1-1 in HEK-293T cells, expression of GSTZ1-1 in Escherichia coli strain M15
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the enzyme is a target for development of irreversible GST inhibitors as anticancer agents based on prostaglandins
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Radulovic, L.L.; Kulkarni, A.P.
A rapid, novel high performance liquid chromatography method for the purification of glutathione S-transferase: an application to the human placental enzyme
Biochem. Biophys. Res. Commun.
128
75-81
1985
Homo sapiens
Manually annotated by BRENDA team
Jakoby, W.B.
Glutathione transferases: an overview
Methods Enzymol.
113
495-499
1985
Ovis aries, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Habig, W.H.; Jakoby, W.B.
Glutathione S-transferases (rat and human)
Methods Enzymol.
77
218-231
1981
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Rogerson, K.S.; Mitchell, A.L.; Ibbotson, R.; Cotton, W.; Strange, R.C.
Studies on the glutathione S-transferase of human platelets and erythrocytes
Biochem. Soc. Trans.
13
200-201
1985
Homo sapiens
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Mannervik, B.; Guthenberg, C.
Glutathione transferase (human placenta)
Methods Enzymol.
77
231-235
1981
Homo sapiens
Manually annotated by BRENDA team
Guthenberg, C.; Warholm, M.; Rane, A.; Mannervik, B.
Two distinct forms of glutathione transferase from human foetal liver. Purification and comparison with isoenzymes isolated from adult liver and placenta
Biochem. J.
235
741-745
1986
Homo sapiens
Manually annotated by BRENDA team
Stockman, P.K.; McLellan, L.I.; Hayes, J.D.
Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver
Biochem. J.
244
55-61
1987
Homo sapiens
Manually annotated by BRENDA team
Vander Jagt, D.L.; Hunsaker, L.A.; Garcia, K.B.; Royer, R.E.
Isolation and characterization of the multiple glutathione S-transferases from human liver. Evidence for unique heme-binding sites
J. Biol. Chem.
260
11603-11610
1985
Homo sapiens
Manually annotated by BRENDA team
Warholm, M.; Guthenberg, C.; van Bahr, C.; Mannervik, B.
Glutathione transferases from human liver
Methods Enzymol.
113
499-504
1985
Homo sapiens
Manually annotated by BRENDA team
Rogerson, K.S.; Mitchell, D.; Lawton, A.; Ibbotson, R.; Cotton, W.; Strange, R.C.
Studies on the glutathione S-transferase of human platelets
Biochem. Biophys. Res. Commun.
122
407-412
1984
Homo sapiens
Manually annotated by BRENDA team
Awasthi, Y.C.; Singh, S.V.
Purification and characterization of a new form of glutathione S-transferase from human erythrocytes
Biochem. Biophys. Res. Commun.
125
1053-1060
1984
Homo sapiens
Manually annotated by BRENDA team
Habig, W.H.; Jakoby, W.B.
Assays for differentiation of glutathione S-transferases
Methods Enzymol.
77
398-405
1981
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Simons, P.C.; Vander Jagt, D.L.
Purification of glutathione S-transferases by glutathione-affinity chromatography
Methods Enzymol.
77
235-237
1981
Homo sapiens
Manually annotated by BRENDA team
Simons, P.C.; Vander Jagt, D.L.
Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography
Anal. Biochem.
82
334-341
1977
Homo sapiens
Manually annotated by BRENDA team
Vander Jagt, D.L.; Wilson, S.P.; Heidrich, J.E.
Purification and bilirubin binding properties of glutathione S-transferase from human placenta
FEBS Lett.
136
319-321
1981
Homo sapiens
Manually annotated by BRENDA team
Caccuri, A.M.; Ascenzi, P.; Antonini, G.; Parker, M.W.; Oakley, A.J.; Chiessi, E.; Nuccetelli, M.; Battistoni, A.; Bellizia, A.; Ricci, G.
Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor co-substrate on dynamics and kinetics of human glutathione transferase
J. Biol. Chem.
271
16193-16198
1996
Homo sapiens
Manually annotated by BRENDA team
Berhane, K.; Widersten, M.; Engstroem, A.; Kozarich, J.W.; Mannervik, B.
Detoxication of base propenals and other alpha,beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases
Proc. Natl. Acad. Sci. USA
91
1480-1484
1994
Homo sapiens
Manually annotated by BRENDA team
Ricci, G.; Caccuri, A.M.; Lo Bello, M.; Rosato, N.; Mei, G.; Nicotra, M.; Chiessi, E.; Mazzetti, A.P.; Federici, G.
Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism
J. Biol. Chem.
271
16187-16192
1996
Homo sapiens
Manually annotated by BRENDA team
Whalen, R.; Kempner, E.S.; Boyer, T.D.
Structural studies of a human pi class glutathione S-transferase. Photoaffinity labeling of the active site and target size analysis
Biochem. Pharmacol.
52
281-288
1996
Homo sapiens
Manually annotated by BRENDA team
Board, P.G.; Taylor, M.C.; Coggan, M.; Parker, M.W.; Lantum, H.B.; Anders, M.W.
Clarification of the role of key active site residues of glutathione transferase zeta/maleylacetoacetate isomerase by a new spectrophotometric technique
Biochem. J.
374
731-737
2003
Homo sapiens
Manually annotated by BRENDA team
Prabhu, K.S.; Reddy, P.V.; Liken, A.D.; Jones, E.C.; Yennawar, H.P.; Reddy, C.C.
Identification, characterization, and properties of a class alpha microsomal glutathione S-transferase
Adv. Exp. Med. Biol.
525
189-192
2003
Ovis aries, Homo sapiens
Manually annotated by BRENDA team
Prabhu, K.S.; Reddy, P.V.; Jones, E.C.; Liken, A.D.; Reddy, C.C.
Characterization of a class alpha glutathione-S-transferase with glutathione peroxidase activity in human liver microsomes
Arch. Biochem. Biophys.
424
72-80
2004
Homo sapiens
Manually annotated by BRENDA team
Gu, Y.; Guo, J.; Pal, A.; Pan, S.S.; Zimniak, P.; Singh, S.V.; Ji, X.
Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity
Biochemistry
43
15673-15679
2004
Homo sapiens
Manually annotated by BRENDA team
Park, H.J.; Koh, J.U.; Ahn, S.Y.; Kong, K.H.
Functional studies of tyrosine 108 residue in the active site of human glutathione S-transferase P1-1
Bull. Korean Chem. Soc.
26
433-439
2005
Homo sapiens
-
Manually annotated by BRENDA team
Grahn, E.; Novotny, M.; Jakobsson, E.; Gustafsson, A.; Grehn, L.; Olin, B.; Madsen, D.; Wahlberg, M.; Mannervik, B.; Kleywegt, G.J.
New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix
Acta crystallogr. Sect. D
62
197-207
2006
Homo sapiens
Manually annotated by BRENDA team
Sanchez-Gomez, F.J.; Gayarre, J.; Avellano, M.I.; Perez-Sala, D.
Direct evidence for the covalent modification of glutathione-S-transferase P1-1 by electrophilic prostaglandins: implications for enzyme inactivation and cell survival
Arch. Biochem. Biophys.
457
150-159
2007
Homo sapiens
Manually annotated by BRENDA team
Shokeer, A.; Larsson, A.K.; Mannervik, B.
Residue 234 in glutathione transferase T1-1 plays a pivotal role in the catalytic activity and the selectivity against alternative substrates
Biochem. J.
388
387-392
2005
Homo sapiens
Manually annotated by BRENDA team
Hayeshi, R.; Mutingwende, I.; Mavengere, W.; Masiyanise, V.; Mukanganyama, S.
The inhibition of human glutathione S-transferases activity by plant polyphenolic compounds ellagic acid and curcumin
Food Chem. Toxicol.
45
286-295
2007
Homo sapiens
Manually annotated by BRENDA team
Wang, L.; Xu, J.; Ji, C.; Gu, S.; Lv, Y.; Li, S.; Xu, Y.; Xie, Y.; Mao, Y.
Cloning, expression and characterization of human glutathione S-transferase Omega 2
Int. J. Mol. Med.
16
19-27
2005
Homo sapiens (Q9H4Y5), Homo sapiens
Manually annotated by BRENDA team
Ricci, G.; De Maria, F.; Antonini, G.; Turella, P.; Bullo, A.; Stella, L.; Filomeni, G.; Federici, G.; Caccuri, A.M.
7-Nitro-2,1,3-benzoxadiazole derivatives, a new class of suicide inhibitors for glutathione S-transferases. Mechanism of action of potential anticancer drugs
J. Biol. Chem.
280
26397-26405
2005
Homo sapiens
Manually annotated by BRENDA team
Tars, K.; Larsson, A.K.; Shokeer, A.; Olin, B.; Mannervik, B.; Kleywegt, G.J.
Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant
J. Mol. Biol.
355
96-105
2006
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Zhao, X.; Fan, Y.; Shen, J.; Wu, Y.; Yin, Z.
Human glutathione S-transferase P1 suppresses MEKK1-mediated apoptosis by regulating MEKK1 kinase activity in HEK293 cells
Mol. Cells
21
395-400
2006
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Eklund, B.I.; Gunnarsdottir, S.; Elfarra, A.A.; Mannervik, B.
Human glutathione transferases catalyzing the bioactivation of anticancer thiopurine prodrugs
Biochem. Pharmacol.
73
1829-1841
2007
Homo sapiens (O15217), Homo sapiens (O43708), Homo sapiens (P08263), Homo sapiens (P09210), Homo sapiens (P09211), Homo sapiens (P09488), Homo sapiens (P28161), Homo sapiens (P30711), Homo sapiens (P46439), Homo sapiens (P78417), Homo sapiens (Q03013), Homo sapiens (Q16772), Homo sapiens
Manually annotated by BRENDA team
Ivarsson, Y.; Norrgard, M.A.; Hellman, U.; Mannervik, B.
Engineering the enantioselectivity of glutathione transferase by combined active-site mutations and chemical modifications
Biochim. Biophys. Acta
1770
1374-1381
2007
Homo sapiens
Manually annotated by BRENDA team
Cho, H.Y.; Kong, K.H.
Study on the biochemical characterization of herbicide detoxification enzyme, glutathione S-transferase
Biofactors
30
281-287
2007
Homo sapiens, Oryza sativa
Manually annotated by BRENDA team
Zheng, K.; Board, P.G.; Fei, X.; Sun, Y.; Lv, S.; Yan, G.; Liu, J.; Shen, J.; Luo, G.
A novel selenium-containing glutathione transferase zeta1-1, the activity of which surpasses the level of some native glutathione peroxidases
Int. J. Biochem. Cell Biol.
40
2090-2097
2008
Homo sapiens (O43708)
Manually annotated by BRENDA team
Fujikawa, Y.; Urano, Y.; Komatsu, T.; Hanaoka, K.; Kojima, H.; Terai, T.; Inoue, H.; Nagano, T.
Design and synthesis of highly sensitive fluorogenic substrates for glutathione S-transferase and application for activity imaging in living cells
J. Am. Chem. Soc.
130
14533-14543
2008
Homo sapiens (P09211)
Manually annotated by BRENDA team
Huang, Y.C.; Misquitta, S.; Blond, S.Y.; Adams, E.; Colman, R.F.
Catalytically active monomer of glutathione S-transferase pi and key residues involved in the electrostatic interaction between subunits
J. Biol. Chem.
283
32880-32888
2008
Homo sapiens (P09211), Homo sapiens
Manually annotated by BRENDA team
Parker, L.J.; Ciccone, S.; Italiano, L.C.; Primavera, A.; Oakley, A.J.; Morton, C.J.; Hancock, N.C.; Bello, M.L.; Parker, M.W.
The anti-cancer drug chlorambucil as a substrate for the human polymorphic enzyme glutathione transferase P1-1: kinetic properties and crystallographic characterisation of allelic variants
J. Mol. Biol.
380
131-144
2008
Homo sapiens (P09211), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Wu, Y.; Shen, J.; Yin, Z.
Expression, purification and functional analysis of hexahistidine-tagged human glutathione S-transferase P1-1 and its cysteinyl mutants
Protein J.
26
359-370
2007
Homo sapiens (P09211), Homo sapiens
Manually annotated by BRENDA team
Jenkins, R.E.; Kitteringham, N.R.; Goldring, C.E.; Dowdall, S.M.; Hamlett, J.; Lane, C.S.; Boerma, J.S.; Vermeulen, N.P.; Park, B.K.
Glutathione-S-transferase pi as a model protein for the characterisation of chemically reactive metabolites
Proteomics
8
301-315
2008
Homo sapiens (P09211), Homo sapiens
Manually annotated by BRENDA team
Josephy, P.D.; Kent, M.; Mannervik, B.
Single-nucleotide polymorphic variants of human glutathione transferase T1-1 differ in stability and functional properties
Arch. Biochem. Biophys.
490
24-29
2009
Homo sapiens (P30711), Homo sapiens
Manually annotated by BRENDA team
Larsson, A.K.; Shokeer, A.; Mannervik, B.
Molecular evolution of theta-class glutathione transferase for enhanced activity with the anticancer drug 1,3-bis-(2-chloroethyl)-1-nitrosourea and other alkylating agents
Arch. Biochem. Biophys.
497
28-34
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Balogh, L.M.; Le Trong, I.; Kripps, K.A.; Shireman, L.M.; Stenkamp, R.E.; Zhang, W.; Mannervik, B.; Atkins, W.M.
Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal
Biochemistry
49
1541-1548
2010
Homo sapiens
Manually annotated by BRENDA team
Pezzola, S.; Antonini, G.; Geroni, C.; Beria, I.; Colombo, M.; Broggini, M.; Mongelli, N.; Leboffe, L.; MacArthur, R.; Mozzi, A.F.; Federici, G.; Caccuri, A.M.
Role of glutathione transferases in the mechanism of brostallicin activation
Biochemistry
49
226-235
2010
Homo sapiens
Manually annotated by BRENDA team
Blikstad, C.; Shokeer, A.; Kurtovic, S.; Mannervik, B.
Emergence of a novel highly specific and catalytically efficient enzyme from a naturally promiscuous glutathione transferase
Biochim. Biophys. Acta
1780
1458-1463
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Gildenhuys, S.; Dobreva, M.; Kinsley, N.; Sayed, Y.; Burke, J.; Pelly, S.; Gordon, G.P.; Sayed, M.; Sewell, T.; Dirr, H.W.
Arginine 15 stabilizes an S(N)Ar reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1
Biophys. Chem.
146
118-125
2010
Homo sapiens (P08263), Homo sapiens
Manually annotated by BRENDA team
Wang, J.; Wang, S.; Song, D.; Zhao, D.; Sha, Y.; Jiang, Y.; Jing, Y.; Cheng, M.
Chalcone derivatives inhibit glutathione S-transferase P1-1 activity: insights into the interaction mode of alpha, beta-unsaturated carbonyl compounds
Chem. Biol. Drug Des.
73
511-514
2009
Homo sapiens
Manually annotated by BRENDA team
Yang, X.; Liu, G.; Li, H.; Zhang, Y.; Song, D.; Li, C.; Wang, R.; Liu, B.; Liang, W.; Jing, Y.; Zhao, G.
Novel oxadiazole analogues derived from ethacrynic acid: design, synthesis, and structure-activity relationships in inhibiting the activity of glutathione S-transferase P1-1 and cancer cell proliferation
J. Med. Chem.
53
1015-1022
2010
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Achilonu, I.; Gildenhuys, S.; Fisher, L.; Burke, J.; Fanucchi, S.; Sewell, B.T.; Fernandes, M.; Dirr, H.W.
The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function
Acta Crystallogr. Sect. F
66
776-780
2010
Homo sapiens (P08263), Homo sapiens
Manually annotated by BRENDA team
Wang, B.; Peng, Y.; Zhang, T.; Ding, J.
Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism
Biochem. J.
439
215-225
2011
Homo sapiens
Manually annotated by BRENDA team
Board, P.; Menon, D.
Glutathione transferases, regulators of cellular metabolism and physiology
Biochim. Biophys. Acta
1830
3267-3288
2013
Homo sapiens (O15217), Homo sapiens (O43708), Homo sapiens (O60760), Homo sapiens (P08263), Homo sapiens (P09210), Homo sapiens (P09211), Homo sapiens (P09488), Homo sapiens (P0CG30), Homo sapiens (P21266), Homo sapiens (P28161), Homo sapiens (P46439), Homo sapiens (P78417), Homo sapiens (Q03013), Homo sapiens (Q16772), Homo sapiens (Q7RTV2), Homo sapiens (Q9H4Y5)
Manually annotated by BRENDA team
Norrgard, M.A.; Hellman, U.; Mannervik, B.
Cys-X scanning for expansion of active-site residues and modulation of catalytic functions in a glutathione transferase
J. Biol. Chem.
286
16871-16878
2011
Homo sapiens
Manually annotated by BRENDA team
Mukanganyama, S.; Bezabih, M.; Robert, M.; Ngadjui, B.T.; Kapche, G.F.; Ngandeu, F.; Abegaz, B.
The evaluation of novel natural products as inhibitors of human glutathione transferase P1-1
J. Enzyme Inhib. Med. Chem.
26
460-467
2011
Homo sapiens
Manually annotated by BRENDA team
Koutsoumpli, G.E.; Dimaki, V.D.; Thireou, T.N.; Eliopoulos, E.E.; Labrou, N.E.; Varvounis, G.I.; Clonis, Y.D.
Synthesis and study of 2-(pyrrolesulfonylmethyl)-N-arylimines: a new class of inhibitors for human glutathione transferase A1-1
J. Med. Chem.
55
6802-6813
2012
Homo sapiens
Manually annotated by BRENDA team
Chronopoulou, E.; Papageorgiou, A.; Markoglou, A.; Labrou, N.
Inhibition of human glutathione transferases by pesticides: development of a simple analytical assay for the quantification of pesticides in water
J. Mol. Catal. B
81
43-51
2012
Homo sapiens
-
Manually annotated by BRENDA team
Yin, L.; Song, J.; Board, P.G.; Yu, Y.; Han, X.; Wei, J.
Characterization of selenium-containing glutathione transferase zeta1-1 with high GPX activity prepared in eukaryotic cells
J. Mol. Recognit.
26
38-45
2013
Homo sapiens
Manually annotated by BRENDA team
Dourado, D.F.; Fernandes, P.A.; Ramos, M.J.
Glutathione transferase classes alpha, pi, and mu: GSH activation mechanism
J. Phys. Chem. B
114
12972-12980
2010
Homo sapiens
Manually annotated by BRENDA team
Ahmad, S.; Niegowski, D.; Wetterholm, A.; Haeggstroem, J.Z.; Morgenstern, R.; Rinaldo-Matthis, A.
Catalytic characterization of human microsomal glutathione S-transferase 2: identification of rate-limiting steps
Biochemistry
52
1755-1764
2013
Homo sapiens
Manually annotated by BRENDA team
Shroads, A.L.; Coats, B.S.; Langaee, T.; Shuster, J.J.; Stacpoole, P.W.
Chloral hydrate, through biotransformation to dichloroacetate, inhibits maleylacetoacetate isomerase and tyrosine catabolism in humans
Drug Metab. Pers. Ther.
30
49-55
2015
Homo sapiens (O43708), Homo sapiens
Manually annotated by BRENDA team
Zompra, A.; Georgakis, N.; Pappa, E.; Thireou, T.; Eliopoulos, E.; Labrou, N.; Cordopatis, P.; Clonis, Y.
Glutathione analogues as substrates or inhibitors that discriminate between allozymes of the MDR-involved human glutathione transferase P1-1
Biopolymers
106
330-344
2016
Homo sapiens (P09211), Homo sapiens
Manually annotated by BRENDA team
Dai, W.; Samanta, S.; Xue, D.; Petrunak, E.M.; Stuckey, J.A.; Han, Y.; Sun, D.; Wu, Y.; Neamati, N.
Structure-based design of N-(5-phenylthiazol-2-yl)acrylamides as novel and potent glutathione S-transferase omega 1 inhibitors
J. Med. Chem.
62
3068-3087
2019
Homo sapiens (P78417)
Manually annotated by BRENDA team
Xie, Y.; Tummala, P.; Oakley, A.J.; Deora, G.S.; Nakano, Y.; Rooke, M.; Cuellar, M.E.; Strasser, J.M.; Dahlin, J.L.; Walters, M.A.; Casarotto, M.G.; Board, P.G.; Baell, J.B.
Development of benzenesulfonamide derivatives as potent glutathione transferase omega-1 inhibitors
J. Med. Chem.
63
2894-2914
2020
Homo sapiens
Manually annotated by BRENDA team