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Information on EC 1.8.5.7 - glutathionyl-hydroquinone reductase
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1.8.5.7 glutathionyl-hydroquinone reductaseIUBMB Comments
This type of enzymes, which are found in bacteria, halobacteria, fungi, and plants, catalyse the glutathione-dependent reduction of glutathionyl-hydroquinones. The enzyme from the bacterium Sphingobium chlorophenolicum can act on halogenated substrates such as 2,6-dichloro-3-(glutathione-S-yl)-hydroquinone and 2,3,5-trichloro-6-(glutathione-S-yl)-hydroquinone. Substrates for these enzymes are often formed spontaneously by interaction of benzoquinones with glutathione.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
ECM4, GHR1, glutathionyl-hydroquinone lyase, glutathionyl-hydroquinone reductase, pcpF, yqjG, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ECM4
glutathionyl-hydroquinone lyase
pcpF
yqjG
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
2-(glutathione-S-yl)-hydroquinone:glutathione oxidoreductase
This type of enzymes, which are found in bacteria, halobacteria, fungi, and plants, catalyse the glutathione-dependent reduction of glutathionyl-hydroquinones. The enzyme from the bacterium Sphingobium chlorophenolicum can act on halogenated substrates such as 2,6-dichloro-3-(glutathione-S-yl)-hydroquinone and 2,3,5-trichloro-6-(glutathione-S-yl)-hydroquinone. Substrates for these enzymes are often formed spontaneously by interaction of benzoquinones with glutathione.
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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-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
-
-
-
?
glutathione + (glutathione-S-yl)-2-chloro-1,4-benzoquinone
glutathione disulfide + 2-chloro-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)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
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 + 3-(glutathione-S-yl)-2,6-dichloro-p-hydroquinone
glutathione disulfide + 2,6-dichloro-p-hydroquinone
L-cysteine + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathionyl cysteinyl disulfide + trichloro-p-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
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.072
(glutathione-S-yl)-2-chloro-1,4-benzoquinone
-
wild-type, pH 8.0, 20°C
0.0044
2-(glutathione-S-yl)-trichloro-p-hydroquinone
-
pH 6.5, 30°C
0.34
2-(glutathione-S-yl)-hydroquinone
wild-type, pH 7.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.96
(glutathione-S-yl)-2-chloro-1,4-benzoquinone
-
wild-type, pH 8.0, 20°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
110.6
(glutathione-S-yl)-2-chloro-1,4-benzoquinone
-
wild-type, pH 8.0, 20°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.16
mutant Y253F, pH 7.5, temperature not specified in the publication
0.19
mutant Y195F, pH 7.5, temperature not specified in the publication
0.4
mutant Y296F, pH 7.5, temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
primarily expressed in reproductive organs
brenda
additional information
-
enzyme is constitutively expressed
brenda
additional information
-
enzyme is constitutively expressed
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A5B8REC9_9ZZZZ
336
0
37987
TrEMBL
other Location (Reliability: 1)
A0A6A7SGT1_9ZZZZ
318
0
36138
TrEMBL
other Location (Reliability: 2)
A0A644TW64_9ZZZZ
321
0
35559
TrEMBL
other Location (Reliability: 3)
A0A5B8RG24_9ZZZZ
318
0
36138
TrEMBL
other Location (Reliability: 2)
A0A6A7SEE7_9ZZZZ
336
0
37987
TrEMBL
other Location (Reliability: 1)
GTO2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
370
0
43274
Swiss-Prot
other Location (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
binary complex structure with glutathionyl-menadione. The structure reveals a large H-site that could accommodate various substituted hydroquinones and a hydrogen network of three Tyr residues that could provide the proton for reductive deglutathionylation
structure in complex with glutathione, to 2.5 A resolution. Isoform GHR1 adopts a typical glutathionyl-hydroquinone reductase fold, with a dimerization interface comparable to that of the bacterial and fungal counterparts
-
isoform ECM4 shows extensions including a huge loop which contributes to the quaternary assembly. Soaking of ECM4 crystals with glutathionyl-menadione results in a structure where glutathione forms a mixed disulfide bond with the cysteine 46. Residues H345 and H350, F228, Y224 and W48 could play crucial roles in binding of glutathionyl-(hydro)quinones, and in assisting C46 during catalysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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