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1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
2-mercaptoethanol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathionyl 2-mercaptoethanyl disulfide + trichloro-p-hydroquinone
-
-
-
-
?
dithiothreitol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathionyl dithiothreityl disulfide + trichloro-p-hydroquinone
-
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutathione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + ethacrynic acid
?
-
-
-
?
glutathione + (glutathione-S-yl)-2-chloro-1,4-benzoquinone
glutathione disulfide + 2-chloro-1,4-benzoquinone
-
-
-
-
?
glutathione + 1,4-benzoquinone
?
-
-
-
?
glutathione + 2'-(glutathione-S-yl)-quercetin
glutathione disulfide + quercetin
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-1,4-benzoquinone
glutathione disulfide + 1,4-benzoquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadiol
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadione
glutathione + 2-(glutathione-S-yl)-menadione
glutathione disulfide + menadione
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
glutathione + 2-(glutathione-S-yl)-quercetin
glutathione disulfide + quercetin
-
-
-
-
r
glutathione + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathione disulfide + trichloro-p-hydroquinone
glutathione + 2-hydroxyethyldisulfide
?
-
-
-
?
glutathione + 3-(glutathione-S-yl)-2,6-dichloro-p-hydroquinone
glutathione disulfide + 2,6-dichloro-p-hydroquinone
glutathione + dehydroascorbic acid
?
-
-
-
?
L-cysteine + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathionyl cysteinyl disulfide + trichloro-p-hydroquinone
-
-
-
-
?
additional information
?
-
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
1,4-benzoquinone + 2-(glutathione-S-yl)-hydroquinone
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 1-chloro-2,4-dinitrobenzene
?
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadiol
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadiol
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadiol
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadiol
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadiol
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadione
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadione
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadione
glutathione disulfide + menadione
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-menadione
glutathione disulfide + menadione
-
-
-
?
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathione disulfide + trichloro-p-hydroquinone
-
-
-
-
?
glutathione + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathione disulfide + trichloro-p-hydroquinone
-
-
-
-
?
glutathione + 3-(glutathione-S-yl)-2,6-dichloro-p-hydroquinone
glutathione disulfide + 2,6-dichloro-p-hydroquinone
-
-
-
-
?
glutathione + 3-(glutathione-S-yl)-2,6-dichloro-p-hydroquinone
glutathione disulfide + 2,6-dichloro-p-hydroquinone
-
-
-
-
?
additional information
?
-
-
several benzoquinones spontaneously react with glutathione to form glutathionyl-hydroquinones via Michael addition. The enzyme reduces the glutathionyl-hydroquinones to the corresponding hydroquinones. The spontaneous and enzymatic reactions lead to the reduction of benzoquinones to hydroquinones with the concomitant oxidation of glutathione to glutathione disulfide. The enzyme does not use glutathionyl-benzoquinones or other thiol-hydroquinones, for example, S-cysteinylhydroquinone, as substrates. Hydrophobic, bulky substrates, such as glutathionyl-menadiol, are preferred
-
-
?
additional information
?
-
-
several benzoquinones spontaneously react with glutathione to form glutathionyl-hydroquinones via Michael addition. The enzyme reduces the glutathionyl-hydroquinones to the corresponding hydroquinones. The spontaneous and enzymatic reactions lead to the reduction of benzoquinones to hydroquinones with the concomitant oxidation of glutathione to glutathione disulfide. The enzyme does not use glutathionyl-benzoquinones or other thiol-hydroquinones, for example, S-cysteinylhydroquinone, as substrates. Hydrophobic, bulky substrates, such as glutathionyl-menadiol, are preferred
-
-
?
additional information
?
-
several benzoquinones spontaneously react with glutathione to form glutathionyl-hydroquinones via Michael addition. The enzyme reduces the glutathionyl-hydroquinones to the corresponding hydroquinones. The spontaneous and enzymatic reactions lead to the reduction of benzoquinones to hydroquinones with the concomitant oxidation of glutathione to glutathione disulfide. The enzyme does not use glutathionyl-benzoquinones or other thiol-hydroquinones, for example, S-cysteinylhydroquinone, as substrates. Hydrophobic, bulky substrates, such as glutathionyl-menadiol, are preferred
-
-
?
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
the enzyme shows preference for gamma-glutamyl-cysteine over glutathione as a reducing thiol. The main activity of Xi class GSTs is thought to be the S-glutathionyl-hydroquinone thiol-dependent reduction, which is monitored using benzoquinone as a model substrate
-
-
-
additional information
?
-
-
isoform GHR1 catalyzes the deglutathionylation of both reduced and oxidized glutathionylated quinones, but the enzyme is more catalytically efficient with the reduced forms
-
-
?
additional information
?
-
-
several benzoquinones spontaneously react with glutathione to form glutathionyl-hydroquinones via Michael addition. The enzyme reduces the glutathionyl-hydroquinones to the corresponding hydroquinones. The spontaneous and enzymatic reactions lead to the reduction of benzoquinones to hydroquinones with the concomitant oxidation of glutathione to glutathione disulfide. The enzyme does not use glutathionyl-benzoquinones or other thiol-hydroquinones, for example, S-cysteinylhydroquinone, as substrates. Hydrophobic, bulky substrates, such as glutathionyl-menadiol, are preferred
-
-
?
additional information
?
-
-
PcpF catalyzes glutathione-dependent reduction of glutathionyl-trichloro-p-hydroquinone via a Ping Pong mechanism. First, PcpF reacts with glutathionyl-trichloro-p-hydroquinone to release trichloro-p-hydroquinone and forms a disulfide bond between its Cys53 residue and the glutathione moiety. Then, a glutathione comes in to regenerate PcpF and release glutathione disulfide
-
-
?
additional information
?
-
-
several benzoquinones spontaneously react with glutathione to form glutathionyl-hydroquinones via Michael addition. The enzyme reduces the glutathionyl-hydroquinones to the corresponding hydroquinones. The spontaneous and enzymatic reactions lead to the reduction of benzoquinones to hydroquinones with the concomitant oxidation of glutathione to glutathione disulfide. The enzyme does not use glutathionyl-benzoquinones or other thiol-hydroquinones, for example, S-cysteinylhydroquinone, as substrates. Hydrophobic, bulky substrates, such as glutathionyl-menadiol, are preferred
-
-
?
additional information
?
-
-
several benzoquinones spontaneously react with glutathione to form glutathionyl-hydroquinones via Michael addition. The enzyme reduces the glutathionyl-hydroquinones to the corresponding hydroquinones. The spontaneous and enzymatic reactions lead to the reduction of benzoquinones to hydroquinones with the concomitant oxidation of glutathione to glutathione disulfide. The enzyme does not use glutathionyl-benzoquinones or other thiol-hydroquinones, for example, S-cysteinylhydroquinone, as substrates. Hydrophobic, bulky substrates, such as glutathionyl-menadiol, are preferred
-
-
?
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gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
additional information
?
-
-
PcpF catalyzes glutathione-dependent reduction of glutathionyl-trichloro-p-hydroquinone via a Ping Pong mechanism. First, PcpF reacts with glutathionyl-trichloro-p-hydroquinone to release trichloro-p-hydroquinone and forms a disulfide bond between its Cys53 residue and the glutathione moiety. Then, a glutathione comes in to regenerate PcpF and release glutathione disulfide
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
gamma-glutamylcysteine + 2-(glutathione-S-yl)-hydroquinone
gamma-glutamylcysteine glutahione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
-
-
-
-
?
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evolution
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
evolution
-
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
-
evolution
-
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
-
evolution
-
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
-
evolution
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Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
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evolution
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Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
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evolution
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Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
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evolution
-
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
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evolution
-
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
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evolution
-
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview
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physiological function
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the disruption of PcpF in makes the mutant lose the glutathionyl-hydroquinone lyase activities in the cell extracts. The mutant becomes more sensitive to pentachlorophenol toxicity and has a significantly decreased pentachlorophenol degradation rate
physiological function
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the disruption of PcpF in makes the mutant lose the glutathionyl-hydroquinone lyase activities in the cell extracts. The mutant becomes more sensitive to pentachlorophenol toxicity and has a significantly decreased pentachlorophenol degradation rate
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additional information
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
additional information
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enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
additional information
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enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
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additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
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additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
-
additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
-
additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
-
additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
-
additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
-
additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
-
additional information
-
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR
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Xun, L.; Belchik, S.M.; Xun, R.; Huang, Y.; Zhou, H.; Sanchez, E.; Kang, C.; Board, P.G.
S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of glutathione transferases
Biochem. J.
428
419-427
2010
Sphingobium chlorophenolicum
brenda
Lam, L.; Zhang, Z.; Board, P.; Xun, L.
Reduction of benzoquinones to hydroquinones via spontaneous reaction with glutathione and enzymatic reaction by S-glutathionyl-hydroquinone reductases
Biochemistry
51
5014-5021
2012
Cupriavidus necator, Saccharomyces cerevisiae, Sphingobium chlorophenolicum, Escherichia coli (P42620), Sphingobium chlorophenolicum ATCC 29327, Cupriavidus necator JMP 134-1
brenda
Lallement, P.; Meux, E.; Gualberto, J.; Dumarcay, S.; Favier, F.; Didierjean, C.; Saul, F.; Haouz, A.; Morel-Rouhier, M.; Gelhaye, E.; Rouhier, N.; Hecker, A.
Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones
FEBS Lett.
589
37-44
2015
Populus trichocarpa
brenda
Huang, Y.; Xun, R.; Chen, G.; Xun, L.
Maintenance role of a glutathionyl-hydroquinone lyase (PcpF) in pentachlorophenol degradation by Sphingobium chlorophenolicum ATCC 39723
J. Bacteriol.
190
7595-7600
2008
Sphingobium chlorophenolicum, Sphingobium chlorophenolicum ATCC 39723
brenda
Green, A.R.; Hayes, R.P.; Xun, L.; Kang, C.
Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases
J. Biol. Chem.
287
35838-35848
2012
Escherichia coli (P42620)
brenda
Schwartz, M.; Didierjean, C.; Hecker, A.; Girardet, J.M.; Morel-Rouhier, M.; Gelhaye, E.; Favier, F.
Crystal structure of Saccharomyces cerevisiae ECM4, a Xi-class glutathione transferase that reacts with glutathionyl-(hydro)quinones
PLoS ONE
11
e0164678
2016
Saccharomyces cerevisiae (P36156)
brenda
Di Matteo, A.; Federici, L.; Masulli, M.; Carletti, E.; Santorelli, D.; Cassidy, J.; Paradisi, F.; Di Ilio, C.; Allocati, N.
Structural characterization of the Xi class glutathione transferase from the haloalkaliphilic archaeon Natrialba magadii
Front. Microbiol.
10
9
2019
Natrialba magadii (D3SS28), Natrialba magadii, Natrialba magadii ATCC 43099 (D3SS28), Natrialba magadii NBRC 102185 (D3SS28), Natrialba magadii DSM 3394 (D3SS28), Natrialba magadii CCM 3739 (D3SS28), Natrialba magadii NCIMB 2190 (D3SS28), Natrialba magadii JCM 8861 (D3SS28), Natrialba magadii CIP 104546 (D3SS28), Natrialba magadii MS3 (D3SS28), Natrialba magadii IAM 13178 (D3SS28)
brenda