Information on EC 1.8.5.7 - glutathionyl-hydroquinone reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.8.5.7
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RECOMMENDED NAME
GeneOntology No.
glutathionyl-hydroquinone reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glutathione + 2-(glutathione-S-yl)-hydroquinone = glutathione disulfide + hydroquinone
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pentachlorophenol degradation
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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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-mercaptoethanol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathionyl 2-mercaptoethanyl disulfide + trichloro-p-hydroquinone
show the reaction diagram
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-
-
-
?
dithiothreitol + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathionyl dithiothreityl disulfide + trichloro-p-hydroquinone
show the reaction diagram
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-
-
-
?
glutathione + (glutathione-S-yl)-2-chloro-1,4-benzoquinone
glutathione disulfide + 2-chloro-1,4-benzoquinone
show the reaction diagram
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-
-
-
?
glutathione + 2-(glutathione-S-yl)-1,4-benzoquinone
glutathione disulfide + 1,4-benzoquinone
show the reaction diagram
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-
-
-
?
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
show the reaction diagram
glutathione + 2-(glutathione-S-yl)-hydroxy-p-hydroquinone
glutathione disulfide + hydroxy-p-hydroquinone
show the reaction diagram
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadiol
show the reaction diagram
glutathione + 2-(glutathione-S-yl)-menadiol
glutathione disulfide + menadione
show the reaction diagram
glutathione + 2-(glutathione-S-yl)-menadione
glutathione disulfide + menadione
show the reaction diagram
glutathione + 2-(glutathione-S-yl)-methyl-p-hydroquinone
glutathione disulfide + methyl-p-hydroquinone
show the reaction diagram
glutathione + 2-(glutathione-S-yl)-quercetin
glutathione disulfide + quercetin
show the reaction diagram
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-
-
-
?
glutathione + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathione disulfide + trichloro-p-hydroquinone
show the reaction diagram
glutathione + 3-(glutathione-S-yl)-2,6-dichloro-p-hydroquinone
glutathione disulfide + 2,6-dichloro-p-hydroquinone
show the reaction diagram
L-cysteine + 2-(glutathione-S-yl)-trichloro-p-hydroquinone
glutathionyl cysteinyl disulfide + trichloro-p-hydroquinone
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutathione + 2-(glutathione-S-yl)-hydroquinone
glutathione disulfide + hydroquinone
show the reaction diagram
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-
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?
additional information
?
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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 hide
LITERATURE
IMAGE
0.072
(glutathione-S-yl)-2-chloro-1,4-benzoquinone
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wild-type, pH 8.0, 20°C
0.0926
2-(glutathione-S-yl)-1,4-benzoquinone
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wild-type, pH 8.0, 20°C
0.24 - 0.43
2-(glutathione-S-yl)-hydroquinone
0.012 - 0.13
2-(glutathione-S-yl)-hydroxy-p-hydroquinone
0.003 - 0.017
2-(glutathione-S-yl)-menadiol
0.27
2-(glutathione-S-yl)-menadione
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wild-type, pH 8.0, 20°C
0.034 - 0.19
2-(glutathione-S-yl)-methyl-p-hydroquinone
0.0044
2-(glutathione-S-yl)-trichloro-p-hydroquinone
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pH 6.5, 30°C
0.93
2-mercaptoethanol
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pH 6.5, 30°C
0.26
dithiothreitol
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pH 6.5, 30°C
0.35 - 1.3
glutathione
1.97
L-cysteine
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pH 6.5, 30°C
0.0027
S-glutathionylquercetin
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wild-type, pH 8.0, 20°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.96
(glutathione-S-yl)-2-chloro-1,4-benzoquinone
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wild-type, pH 8.0, 20°C
1.62
2-(glutathione-S-yl)-1,4-benzoquinone
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wild-type, pH 8.0, 20°C
11 - 22
2-(glutathione-S-yl)-hydroquinone
4.4 - 19
2-(glutathione-S-yl)-hydroxy-p-hydroquinone
4.6 - 14
2-(glutathione-S-yl)-menadiol
4.75
2-(glutathione-S-yl)-menadione
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wild-type, pH 8.0, 20°C
8.4 - 31
2-(glutathione-S-yl)-methyl-p-hydroquinone
1.09
2-mercaptoethanol
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pH 6.5, 30°C
0.89
dithiothreitol
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pH 6.5, 30°C
2.08 - 37
glutathione
0.37
L-cysteine
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pH 6.5, 30°C
0.013
S-glutathionylquercetin
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wild-type, pH 8.0, 20°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
110.6
(glutathione-S-yl)-2-chloro-1,4-benzoquinone
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wild-type, pH 8.0, 20°C
17.5
2-(glutathione-S-yl)-1,4-benzoquinone
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wild-type, pH 8.0, 20°C
26 - 91
2-(glutathione-S-yl)-hydroquinone
15 - 590
2-(glutathione-S-yl)-hydroxy-p-hydroquinone
760 - 3215
2-(glutathione-S-yl)-menadiol
17.4
2-(glutathione-S-yl)-menadione
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wild-type, pH 8.0, 20°C
56 - 410
2-(glutathione-S-yl)-methyl-p-hydroquinone
1.17
2-mercaptoethanol
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pH 6.5, 30°C
3.43
dithiothreitol
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pH 6.5, 30°C
1.6 - 42
glutathione
0.19
L-cysteine
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pH 6.5, 30°C
4.95
S-glutathionylquercetin
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wild-type, pH 8.0, 20°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.16
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mutant Y253F, pH 7.5, temperature not specified in the publication
0.19
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mutant Y195F, pH 7.5, temperature not specified in the publication
0.4
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mutant Y296F, pH 7.5, temperature not specified in the publication
8.65
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wild-type, pH 7.5, temperature not specified in the publication
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 36900, calculated
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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
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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
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C63A
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catalytic residue, mutant displays negligible activity
Y195F
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catalytic residue, mutant displays negligible activity
Y253F
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catalytic residue, mutant displays negligible activity
Y296F
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catalytic residue, mutant displays negligible activity
C49A
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mutation of catalytic cysteine, loss of activity
C49S
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mutation of catalytic cysteine, loss of activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.5.7)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)