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Information on EC 2.5.1.18 - glutathione transferase
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2.5.1.18 glutathione transferaseIUBMB Comments
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
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Word Map
- 2.5.1.18
- peroxidase
- catalase
- superoxide
- dismutase
- sod
-
carcinogen
-
pull-down
-
xenobiotic
- malondialdehyde
- carcinogenesis
-
detoxify
-
smoke
- hepatocytes
- fish
-
smoking
- isoenzymes
-
case-control
- cyp1a1
- placental
-
electrophilic
- hydrocarbon
- epoxide
-
genotoxic
- wistar
-
co-immunoprecipitation
-
chemopreventive
-
benzoapyrene
- acetylcholinesterase
-
aquatic
-
thiobarbituric
-
pesticide
-
hepatocarcinogenesis
- gill
-
tbars
- hydroperoxide
-
insecticide
-
polycyclic
-
hepatotoxicity
- aflatoxin
-
preneoplastic
-
cigarette
- schistosoma
- phenobarbital
- gssg
-
drug-metabolizing
-
ache
-
udp-glucuronosyltransferase
- cyp2d6
- gsh-px
-
methylation-specific
- biotechnology
- drug development
- analysis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
2-hydroxychromene-2-carboxylic acid isomerase, 26GST, adGSTD4-4, agGSTe2, allergen Der p 2, allergen Der p 8, alpha class glutathione transferase, Alpha class GST, alpha GST, alpha-class glutathione transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
26GST
alpha class glutathione transferase
alpha GST
alpha-class glutathione transferase
AtuGSTH1-1
cGST
Chi class GST
Chi GST
delta-class glutathione S-transferase
Delta-class glutathione transferase
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
glutathione S-transferase P1-1
glutathione S-transferase X
-
-
-
-
glutathione S-transferases
glutathione transferase
glutathione transferase A1-1
glutathione transferase P1-1
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-S-transferase
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
GST
GST A1-1
GST A2-2
GST A3-3
GST I
GST M1-1
GST M2-2
GST P1-1
GST pi
GST T1-1
GST-1
GST1
GST2
GST4
GST5
GSTA1-1
GSTA2-2
GSTA3
GSTA3-3
GSTA4
GSTA4-4
GSTA5
GSTD
GSTD1
GSTD10
GSTE2
GSTE6
GSTE7
GSTF3
GSTFuA1
GSTK1
GSTM1-1
GSTM2
GSTM3
GSTM4
GSTO1
GSTO2
GSTP
GSTP1
GSTP1-1
GSTS
GSTS1
GSTT1
GSTT2
Gstz1
GTT1.2
kappa class glutathione transferase
MGST1
microsomal glutathione transferase-1
membrane-bound enzyme with both glutathione transferase and hydroperoxidase activities
mtMGST1
Omega class GST
pGSTA1
PtGSTU1
RX:glutathione R-transferase
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
sigma-class glutathione S-transferase
ssGST3
ssGST5
tau class glutathione transferase
theta class glutathione transferase T1-1
theta class GST
theta-class glutathione transferase
Ya-GST
additional information
glutathione S-transferase
-
-
-
-
glutathione S-transferase
-
-
glutathione S-transferase
O04437, P30110, P30111, Q6U6G6, Q8GRI3, Q8GTB7, Q8GTB8, Q8GTB9, Q8GTC0, Q8GTC1, Q8LGN5, Q8LGN6, Q8LL15, Q8RW00, Q8RW01, Q8RW02, Q8RW03, Q8RW04, Q9SP56
-
glutathione-S-transferase
A0A023JBX1, A0A023JBX8, A0A023JCA5, A0A023JCC0, A0A023JCF9, A0A023JCM9, A0A023JCN4, A0A023JCQ9, A0A023JCR5, G7P4V9, G7P5X8, Q2PFL7
-
glutathione-S-transferase
A0A023JBX5, A0A023JCA8, A0A023JCQ7, A0A023JCR6, F6TP78, F6WWX7, F6Z1G0, F7H5D7, G7N132, G8F1C9, H9Z845, KC734495
-
GST
-
-
GST
-
GST
O04437, P30110, P30111, Q6U6G6, Q8GRI3, Q8GTB7, Q8GTB8, Q8GTB9, Q8GTC0, Q8GTC1, Q8LGN5, Q8LGN6, Q8LL15, Q8RW00, Q8RW01, Q8RW02, Q8RW03, Q8RW04, Q9SP56
-
additional information
two major GST subunits are mu-class GSTs, one minor GST subunit is a putative theta-class GST
additional information
two major GST subunits are mu-class GSTs, one minor GST subunit is a putative theta-class GST
additional information
-
the enzyme belongs to the glutathione-S-transferase family of multifunctional enzymes
additional information
maleylacetoacetate isomerase, EC 5.2.1.2, bifunctional enzyme
additional information
the Necator americanus GST isozymes belong to a nematode-specific nu-class GST family
additional information
the enzyme belongs to the family of glutathione S-transferases
additional information
-
MGST1 that belongs to the membrane associated proteins in eicosanoid and glutathione metabolism, MAPEG, superfamily
additional information
-
overview of nomenclature of rat glutathione transferase isoenzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RX + glutathione = HX + R-S-glutathione
mechanisms for formation of specific mono(glutathionyl) or bis(glutathionyl) conjugates
-
RX + glutathione = HX + R-S-glutathione
the enzyme uses a rapid-equilibrium random-order ternary-complex mechanism or a compulsory order ternary-complex mechanism
-
RX + glutathione = HX + R-S-glutathione
active site involving residue Trp234, and substrate binding structure, isozyme GST T1-1
-
RX + glutathione = HX + R-S-glutathione
the enzyme uses a rapid equilibrium random sequential bi-bi mechanism with intrasubunit modulation between GSH binding site, the G-site, and electrophile binding site, the H-site, Trp12, Phe35 and Ile118 are involved in substrate binding, Phe35 is important for catalytic activity
-
RX + glutathione = HX + R-S-glutathione
substrate binding: Tyr9 is responsible for the deprotonation of GSH and Lys15, but also Gln71 are involved, active site and substrate binding structure, overview
-
RX + glutathione = HX + R-S-glutathione
active site structure: Tyr111 indirectly stabilizes glutathione binding, Tyr119 modulates hydrophobic substrate binding, and Phe123 indirectly modulates catalysis. An aromatic zipper in the H-site contributing a network of aromatic pi-pi interactions. Several residues of the cluster directly interact with the hydrophobic substrate while others indirectly maintain conformational stability of the dimeric structure through the C-terminal domain II
RX + glutathione = HX + R-S-glutathione
catalytic mechanism of kappa class GST, overview. Substrate binding induces a conformational change of the active site from an open conformation in the apo-form to a closed conformation in the S-hexylglutathione-bound complex, facilitating formations of the G site (GSH-binding site) and the H site (hydrophobic substrate-binding site). The conserved Ser16 at the G site functions as the catalytic residue in the deprotonation of the thiol group and the conserved Asp69, Ser200,Asp201 andArg202 form a network of interactions with gamma -glutamyl carboxylate to stabilize the thiolate anion. The H site is a large hydrophobic pocket with conformational flexibility to allow the binding of different hydrophobic substrates. The kinetic mechanism of hGSTk conforms to a rapid equilibrium random sequential Bi Bi model
-
RX + glutathione = HX + R-S-glutathione
active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview; active site structure and catalytic mechanism, overview
RX + glutathione = HX + R-S-glutathione
the mutant C169A exhibits cooperative behaviour and a ping pong mechanism whereby liberation of a proton from a reduced enzyme-glutathione complex to form an enzyme-unprotonated glutathione complex is essentially irreversible
RX + glutathione = HX + R-S-glutathione
substrate binding structure and reaction mechanism, conformational changes, detailed overview
I6ZUH3
RX + glutathione = HX + R-S-glutathione
substrate specificity and catalytic mechanism, overview
-
RX + glutathione = HX + R-S-glutathione
catalytic mechanism of isozyme GSTH1-1
-
RX + glutathione = HX + R-S-glutathione
catalytic mechanism of isozyme GSTH1-1
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
RX + glutathione = HX + R-S-glutathione
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aryl group transfer
aryl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
RX:glutathione R-transferase
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
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CAS REGISTRY NUMBER
COMMENTARY
50812-37-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-2-bromo-3-(4-nitrophenyl)propanoic acid + glutathione
2-(glutathion-S-yl)-3-(4-nitrophenyl)propanoic acid + HBr
-
-
-
-
?
(2,3-dichloro-4-[2-methylenebutyryl]phenoxy)acetic acid + glutathione
?
-
i.e. ethacrynic acid
-
-
?
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione
1,1-dichloro-2,2-bis-(4-chlorophenyl)ethylene + ?
i.e. DDT, modeling of DDT into the putative DDT-binding pocket, catalytic mechanism of isozyme agGSTe2 that shows high activity through the inclination of the upper part of H4 helix, H4'' helix, which brings residues Arg112, Glu116, and Phe120 closer to the GSH-binding site resulting in a more efficient GS- stabilizing hydrogen-bond-network and higher DDT-binding affinity, overview
product formation through an elimination reaction triggered by the nucleophilic attack of the thiolate group of GS- on the beta-hydrogen of DDT
-
?
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione
?
detoxification of the insecticide DDT, especially by isozyme agGSTe2
-
-
?
1,2-dichloro-4-nitrobenzene + glutathione
S-(2-chloro-4-nitro-phenyl)glutathione + HCl
binding structure with wild-type and mutant Y119E and F123A enzymes, overview
-
-
?
1,3,5-triacryloyl-1,3,5-triazinane + glutathione
L-gamma-glutamyl-S-[3-(3,5-diacryloyl-1,3,5-triazinan-1-yl)-3-oxopropyl]-L-cysteinylglycine
-
-
-
-
?
1,3,5-trinitrobenzene + glutathione
S-(2,4,6-trinitrocyclohexa-2,5-dien-1-yl)glutathione
an anionic sigma-complex is formed between GSH and 1,3,5-trinitrobenzene and is stabilized by Arg15. The trinitrocyclohexadienate moiety of the sigma-complex binds the H-site where the catalytic residue, Tyr9, was identified to hydrogen bond to an o-nitro group of the sigma-complex
-
-
?
1-bromo-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HBr
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
chloride + L-gamma-glutamyl-S-(2,4-dinitrophenyl)-L-cysteinylglycine
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,3-dinitrophenyl)-glutathione + HCl
Tyr119 not only plays a role in hydrophobic substrate binding but also in packing of the active site pocket, which influences chemical interactions involved in enzyme catalysis
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrobenzyl)glutathione + HCl
-
-
-
-
?
1-iodo-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HI
-
-
-
-
?
12-oxo-phytodienoic acid + glutathione
10-S-glutathionyl-12-oxo-phytodienoic acid + H2O
-
-
-
-
?
2,3-hexadienal + GSH
?
-
at 7.5% of the activity with 1-chloro-2,4-dinitrobenzene
-
-
?
2-chloro-5-nitropyridine + glutathione
chloride + L-gamma-glutamyl-S-(5-nitropyridin-2-yl)-L-cysteinylglycine
-
-
-
-
?
4-nitrophenethyl bromide + glutathione
S-(4-nitrophenyl)glutathione + HBr
-
-
-
?
4-nitrophenyl butyrate + glutathione
S-(4-nitrophenyl)glutathione + butyrate
I6ZUH3
-
-
-
?
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid + glutathione
?
-
-
-
-
?
5-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid + glutathione
?
-
-
-
-
?
7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH
7-chloro-4-glutathionylbenzo-2-oxa-1,3-diazole
-
-
-
-
?
7-oxabicyclo[4.1.0]heptan-2-one + glutathione
chloride + L-gamma-glutamyl-S-(6-oxocyclohex-1-en-1-yl)-L-cysteinylglycine
-
-
-
-
?
azathioprine + glutathione
?
-
aromatic substitution. Wild-type hGST M2-2 has modest activity with azathioprine, but mutant C87A/C115A/C174A/M212C displays no detectable activity. The azathioprine activity of wild-type hGST M2-2 can be enhanced 30fold by two point mutations of other residues in the active site
-
-
?
dichloroacetate + glutathione
2-(glutathion-S-yl)-chloroacetate + HCl
-
-
-
?
glutathione + (2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
chloride + 5-glutathionyl-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
-
-
?
glutathione + (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
chloride + 3-glutathionyl-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
glutathione + (2Z,4E)-3-chloro-6-(3,5-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
?
-
-
-
-
?
glutathione + 1,2-epoxy-3-(4-nitro-phenoxy)propane
?
-
best substrate for the wild-type GST T1-1 and mutant W234K
-
-
?
glutathione + 1,2-epoxy-3-(p-nitrophenoxy)-propane
?
-
substrate of the theta class isozyme
-
-
?
glutathione + 1-bromo-4-nitrobenzene
bromide + 4-nitrophenyl-glutathione
-
recombinant catalytically active monoclonal antibody fragment ScFv2F3
-
-
?
glutathione + 1-iodo-3-phenylpropane
iodide + 3-phenylpropyl-glutathione
-
-
-
-
?
glutathione + 1-iodomethane
iodide + methylglutathione
-
best substrate of GST T1-1 mutant W234R
-
-
?
glutathione + 2-hydroxyethyl disulfide
?
isozyme GSTO2, low activity
-
-
?
glutathione + 4-nitrobenzyl chloride
chloride + 4,4'-dichlorodiphenyltrichloroethane
-
-
-
-
?
glutathione + 4-nitrobenzyl chloride
chloride + 4-nitrobenzyl-glutathione
-
-
-
-
?
glutathione + 4-nitrobenzyl chloride
chloride + 4-nitrophenyl-glutathione
-
substrate of the alpha class isozyme
-
-
?
glutathione + 4-nitrobenzyl chloride
chloride + S-(4-nitrophenyl)-glutathione
-
-
-
?
glutathione + 4-nitrobenzyl chloride
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
glutathione + 4-nitrophenethyl bromide
bromide + 4-nitrophenethyl-glutathione
-
-
-
-
?
glutathione + 4-nitrophenyl acetate
S-(4-nitrophenyl)glutathione + HCl
-
-
-
?
glutathione + anti-benzo(a)pyrene-7,8-dihydrodiol-9,10-epoxide
?
-
-
-
-
?
glutathione + cis-6-(2-acetylvinylthio)purine
?
-
-
-
?
glutathione + fenoxaprop
4-hydroxyphenoxypropanoic acid + glutathione conjugate
-
herbicide
-
?
glutathione + fluorodifen
4-nitrophenol + (2-nitro-4-trifluoromethylphenyl)glutathione
-
-
-
-
?
glutathione + nitrobutyl chloride
chloride + nitrobutyl-glutathione
-
-
-
?
glutathione + trans-6-(2-acetylvinylthio)guanine
?
-
-
-
?
harderoporphyrinogen + glutathione
harderoporphyrinogen-S-glutathione + H2O
-
-
-
-
?
methyl 3-(4-methoxyphenyl)oxirane-2-carboxylate + glutathione
chloride + L-gamma-glutamyl-S-[2-hydroxy-3-methoxy-1-(4-methoxyphenyl)-3-oxopropyl]-L-cysteinylglycine
-
-
-
-
?
nitrophenyl acetate + GSH
?
-
6.5% of the activity with 1-chloro-2,3-dinitrobenzene
-
-
?
protoporphyrinogen + glutathione
protoporphyrinogen-S-glutathione + H2O
-
-
-
-
?
rac-4-hydroxynonenal + glutathione
S-(4-hydroxy-1-oxononan-3-yl)glutathione
-
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
-
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
-
?
reduced glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
-
-
-
-
?
S-glutathionyl-phenylacetophenone + glutathione
?
-
-
-
?
trans-2-nonenal + GSH
?
-
at 1% of the activity with 1-chloro-2,4-dinitrobenzene
-
-
?
[(methylamino)[methyl(nitroso)amino]methyl]cyanamide + glutathione
[bis(methylamino)methyl]cyanamide + S-nitrosoglutathione
-
transnitrosylation
-
-
?
(13S,9Z,11E)-13-hydroperoxyoctadeca-9,11-dienoic acid + GSH
?
-
12% of the activity with 1-chloro-2,3-dinitrobenzene
-
-
?
(15S,5Z,8Z,10E,14Z)-15-hydroperoxyeicosa-5,8,10,14-tetraenoic acid + GSH
?
-
-
-
-
?
(15S,5Z,8Z,10E,14Z)-15-hydroperoxyeicosa-5,8,10,14-tetraenoic acid + GSH
?
-
2.3% of the activity with 1-chloro-2,3-dinitrobenzene
-
-
?
(15S,5Z,8Z,10E,14Z)-15-hydroperoxyeicosa-5,8,10,14-tetraenoic acid + GSH
?
-
-
-
-
?
(5S,6E,8Z,11Z,14Z)-5-hydroperoxyeicosa-6,8,11,14-tetraenoic acid + GSH
?
-
-
-
-
?
(5S,6E,8Z,11Z,14Z)-5-hydroperoxyeicosa-6,8,11,14-tetraenoic acid + GSH
?
-
4.6% of the activity with 1-chloro-2,3-dinitrobenzene
-
-
?
(5S,6E,8Z,11Z,14Z)-5-hydroperoxyeicosa-6,8,11,14-tetraenoic acid + GSH
?
-
-
-
-
?
(9S,10E,12E)-9-hydroperoxyoctadeca-10,12-dienoic acid + GSH
?
-
8% of the activity with 1-chloro-2,3-dinitrobenzene
-
-
?
1,2-dichloro-4-nitrobenzene + GSH
?
-
at 8% of the activity with 1-chloro-2,4-dinitrobenzene
-
-
?
1,2-epoxy-3-(4-nitrophenoxy)propane + glutathione
?
A0A023JBX1, A0A023JBX8, A0A023JCA5, A0A023JCC0, A0A023JCF9, A0A023JCM9, A0A023JCN4, A0A023JCQ9, A0A023JCR5, G7P4V9, G7P5X8, Q2PFL7
-
-
-
?
1,2-epoxy-3-(4-nitrophenoxy)propane + glutathione
?
A0A023JBX5, A0A023JCA8, A0A023JCQ7, A0A023JCR6, F6TP78, F6WWX7, F6Z1G0, F7H5D7, G7N132, G8F1C9, H9Z845, KC734495
-
-
-
?
1-chloro-2,3-dinitrobenzene + glutathione
S-(2,3-dinitrophenyl)glutathione + HCl
-
-
-
-
?
1-chloro-2,3-dinitrobenzene + glutathione
S-(2,3-dinitrophenyl)glutathione + HCl
-
-
-
-
?
1-chloro-2,3-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
-
-
-
-
?
1-chloro-2,3-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
-
-
-
-
?
1-chloro-2,3-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
2,4-dinitrobenzyl-glutathione + HCl
residue Ser13 is directly involved in the reaction chemistry and the correct positioning of GSH and CDNB in the ternary catalytic complex. Asn48 and Pro49 have a direct role on the structural integrity of the GSH-binding site (G-site)
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
2,4-dinitrobenzyl-glutathione + HCl
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
2,4-dinitrobenzyl-glutathione + HCl
O15217, O43708, O60760, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
A0A023JBX1, A0A023JBX8, A0A023JCA5, A0A023JCC0, A0A023JCF9, A0A023JCM9, A0A023JCN4, A0A023JCQ9, A0A023JCR5, G7P4V9, G7P5X8, Q2PFL7
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1-chloro-2,4-dinitrobenzene + glutathione
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A0A023JBX5, A0A023JCA8, A0A023JCQ7, A0A023JCR6, F6TP78, F6WWX7, F6Z1G0, F7H5D7, G7N132, G8F1C9, H9Z845, KC734495
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
Agrobacterium tumefaciens C58 / ATCC 33970
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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synthetic substrate of GST
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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isoform GST-1 is 18.3times more active than GST-2 and 26.8times more active than GST-3
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
Q9FQE8
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
O15217, O43708, O60760, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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aromatic substitution
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
A0A023I760
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
best substrate
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
I6ZUH3
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
D2WL48, D2WL57
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
D2WL48, D2WL57
isoform GSTU45 shows highest activity with 1-chloro-2,4-dinitrobenzene
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene is conjugated through a classic SNAr reaction that proceeds in two steps with the formation of an intermediate Meisenheimer complex
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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best substrate
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
E5SSF0
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
1-glutathionyl-2,3-dinitrobenzene + HCl
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1-chloro-2,4-dinitrobenzene + GSH
1-glutathionyl-2,3-dinitrobenzene + HCl
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1-chloro-2,4-dinitrobenzene + GSH
1-glutathionyl-2,3-dinitrobenzene + HCl
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1-chloro-2,4-dinitrobenzene + GSH
1-glutathionyl-2,3-dinitrobenzene + HCl
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1-chloro-2,4-dinitrobenzene + GSH
1-glutathionyl-2,3-dinitrobenzene + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,3-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
Myathropa florea
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
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1-fluoro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HF
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1-fluoro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HF
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1-fluoro-2,4-dinitrobenzene is conjugated through a classic SNAr reaction that proceeds in two steps with the formation of an intermediate Meisenheimer complex
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2,4-dinitro-1-iodobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HI
Myathropa florea
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2,4-dinitro-1-iodobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HI
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2-hydroxychromene-2-carboxylic acid
trans-o-hydroxybenzylidene pyruvic acid
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HCCA isomerase catalyzes the glutathione-dependent interconversion of 2-hydroxychromene-2-carboxylic acid and trans-o-hydroxybenzylidene pyruvic acid in the naphthalene catabolic pathway of Pseudomonas putida, mechanisms in the naphthalene catabolic pathwayoverview
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2-hydroxychromene-2-carboxylic acid
trans-o-hydroxybenzylidene pyruvic acid
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the dimeric protein binds one molecule of GSH very tightly and a second molecule of GSH with much lower affinity, GSH acts as a tightly bound cofactor in the reaction, binding structure, overview
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4-hydroxynonenal + GSH
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90% of the activity with 1-chloro-2,4-dinitrobenzene
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4-hydroxynonenal + GSH
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10% of the activity with 1-chloro-2,3-dinitrobenzene
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4-nitrobenzyl chloride + glutathione
S-(4-nitrobenzyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrobenzyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride + glutathione
S-(4-nitrophenyl)glutathione + HCl
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4-nitrobenzyl chloride is conjugated through a single-step bimolecular nucleophilic substitution (SN2) with a pentacoordinate intermediate
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4-nitrophenyl acetate + GSH
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198% of the activity with 1-chloro-2,4-dinitrobenzene
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4-nitrophenyl acetate + GSH
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0.2% of the activity with 1-chloro-2,3-dinitrobenzene
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4-nitrophenyl acetate + GSH
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at 0.2% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme
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7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + glutathione
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O15217, O43708, O60760, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5
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7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH
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15% of the activity with 1-chloro-2,3-dinitrobenzene
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7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH
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80% of the activity with 1-chloro-2,3-dinitrobenzene
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7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH
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23.4% of the activity with 1-chloro-2,3-dinitrobenzene
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7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH
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at 23% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme
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bromosulfophthalein + GSH
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10.3% of the activity with 1-chloro-2,4-dinitrobenzene, isoenzyme II
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bromosulfophthalein + GSH
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8.6% of the activity with 1-chloro-2,4-dinitrobenzene, isoenzyme I
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brostallicin + glutathione
glutathionyl-brostallicin
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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
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brostallicin + glutathione
glutathionyl-brostallicin
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isoenzymes GSTP1-1 and GSTM2-2
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