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Enzyme Nomenclature
Information on EC 1.8.1.7 - glutathione-disulfide reductase
Word Map on EC 1.8.1.7
- 1.8.1.7
- peroxidase
- superoxide
- catalase
- radical
- erythrocyte
- malondialdehyde
- hepatic
- glutathione-s-transferase
- ascorbate
- glucose-6-phosphate
- thiols
- injury
- lactate
-
thiobarbituric
- wistar
- dehydroascorbate
-
tbars
-
non-enzymatic
- gsh-px
-
albino
-
histopathological
-
intraperitoneal
- cadmium
-
hydroperoxide
- selenium
- riboflavin
-
buthionine
- guaiacol
-
selenium-dependent
-
glutathione-dependent
-
gamma-glutamyl
-
lipoperoxidation
- dt-diaphorase
- mn-sod
-
hepatoprotective
- trypanothione
-
acid-reactive
- sulfoximine
- lipoamide
-
hepatotoxicity
- cumene
- gamma-glutamylcysteine
-
dienes
- medicine
-
1.15.1.1
-
cuznsod
- transpeptidase
-
gsh-dependent
- alpha-tocopherol
-
pro-oxidant
- glutaredoxins
- pharmacology
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.1.7
-
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RECOMMENDED NAME
GeneOntology No.
glutathione-disulfide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
; activity is dependent on a redox-active disulfide in each of the active centres; a dimeric flavoprotein (FAD)
-
-
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
GSSG-binding site; mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
ping-pong mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
ping-pong mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
ping-pong mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
substrate and cofactor binding site, three-dimensional structure
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
cofactor binding of glutathione reductase with FAD analogues, reconstitution; mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
cofactor binding of glutathione reductase with FAD analogues, reconstitution
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
inhibition mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
analogous to trypanothione reductase
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
analogous to trypanothione reductase
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
branching mechanism
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
molecular modeling of enzyme inactivation by peroxynitrite, structure analysis
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
member of pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes; substrate and cofactor binding site, three-dimensional structure
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
sulfhydryl groups and histidine residues are essential for the catalytic properties of the enzyme
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
catalytic cycle; mechanism; member of pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes; substrate and cofactor binding site, three-dimensional structure
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
member of pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes; recombinant glutathione-trypanothione reductase-like enzyme, substrate binding, three dimensional structure, complex formation
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
enzyme contains a catalytic selenocysteine
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
active site structure
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
active site structure, Cys39/Cys44 are involved
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
the multifunctional enzyme possesses both thioredoxin reductase activity, EC 1.8.1.9, glutathione reductase activity, EC 1.8.1.7, and glutaredoxin activity
-
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
the enzyme follows the Ping Pong mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
reduction
-
-
-
-
reduction
-
the enzyme shows also S-nitrosoglutathione reductase activity
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
glutathione:NADP+ oxidoreductase
A dimeric flavoprotein (FAD); activity is dependent on a redox-active disulfide in each of the active centres.
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CAS REGISTRY NUMBER
COMMENTARY
9001-48-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozymes from the cold-hardened strains GR-1H and GR-2H and noncold-hardened strains GR1NH and GR-2NH; red spruce
-
-
parasite isolated from mice, enzyme is a multifunctional thioredoxin-glutathione reductase TGR
-
-
-
394708, 394711, 394761, 394768, 394769, 659860, 660339, 688951, 699884, 701093, 712604, 723817, 726354
-
-
-
393993, 394708, 394712, 394714, 394718, 394723, 394724, 394725, 394726, 394727, 394728, 394729, 394730, 394761, 394763, 394775, 394779, 438075, 657878, 658250, 659592, 659860, 663260, 671910, 673194, 673458, 674175, 674440, 677215, 686259, 688050, 688172, 689306, 690134, 690144, 690147, 696556, 696681, 699224, 699241, 711008, 712066, 725616
-
-
chloroquine-resistant and chloroquine-sensitive strains, overview, intraerythrocytic parasite
-
-
-
394708, 394711, 394736, 394739, 394750, 658797, 659592, 659860, 673458, 673460, 677215, 700654, 713468
-
-
-
-
-
chromate-tolerant mutant chr1-663T displays a significantly decreased specific glutathione reductase activity coded by the pgr1 (+) gene compared with its parental strain
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
deletion of isoform GR1 prevents survival due to a pollen lethal phenotype
malfunction
-
in addition to a decrease in GSH and increase in GSSG, inhibition of glutathione reductase increases the ratios of NADH/NAD+ and NADPH/NADP+. Significant protein glutathionylation is observed. However, the inhibition does not affect the formation of reactive oxygen species or expression of antioxidant defense enzyme systems (glutathione reductase, glutathione peroxidase, catalase, and superoxide dismutase)
malfunction
-
glutathione reductase inhibition significantly enhances cancer sensitivity to X-ray irradiation through glutathione disulfide increase
malfunction
-
enzyme-deficient mice exhibit increased morbidity and mortality but do not exhibit a greater sensitivity to lipopolysaccharide than do wild type mice. Neutrophils of enzyme-deficient mice reveal impaired phagocytosis
malfunction
-
cells lacking the enzyme show decreased resistance to oxidative stress (H2O2) and 2fold higher levels of reactive oxygen species and catalase activity than the wild type strain
malfunction
-
cells lacking the enzyme show decreased resistance to oxidative stress (H2O2) and 2fold higher levels of reactive oxygen species and catalase activity than the wild type strain
-
physiological function
-
thioredoxin glutathione reductase binding to retinoic acid receptor is required for the retinoic acid-dependent retinoic acid receptor association with chromatin, retinoic acid receptor activity damaged by oxidative stress is restored by thioredoxin glutathione reductase
physiological function
-
the enzyme's physiological function is the reduction of glutathione disulfide or GSNO but not the opposite
physiological function
-
glutathione reductase is the crucial enzyme to maintain high glutathione/glutathione disulfide ratio and physiological redox status in cells
physiological function
-
glutathione reductase is essential for host defense against bacterial (group B Streptococcus) infection. The oxidative defense mechanism mediated by the enzyme is required for an effective innate immune response against bacteria, probably by preventing phagocyte dysfunction due to oxidative damage
physiological function
rice enzyme expression in yeast increases the ability of the cells to adapt and recover from H2O2-induced oxidative stress and various stimuli including heat shock and exposure to menadione, heavy metals (iron, zinc, copper, and cadmium), SDS, ethanol, and sulfuric acid
physiological function
the enzyme is involved in salt stress response and biotic stress tolerance
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays an essential central role in cell defense against reactive oxygen metabolites. The enzyme plays an important role in plant protection against various forms of stress
physiological function
-
the enzyme plays a crucial role in daylength-dependent redox signaling. The Arabidopsis glutathione reductase1 gene plays a crucial role in leaf responses to intracellular hydrogen peroxide and in ensuring appropriate gene expression through both salicylic acid and jasmonic acid signaling pathways
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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
2,5-bis(aziridin-1-yl)-3,6-dimethylcyclohexa-2,5-diene-1,4-dione + NADPH
?
-
-
-
-
?
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione + NADPH
?
-
-
-
-
?
2,5-bis(aziridin-1-yl)cyclohexa-2,5-diene-1,4-dione + NADPH
?
-
-
-
-
?
2,5-bis(ethylamino)-3,6-di(aziridinyl)-1,4-benzoquinone + NADPH
?
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
AuCl4- + NADPH + H+
?
-
formation of gold nanoparticles at the active site of glutathione reductase that are tightly bound through the catalytic cysteines. The nanoparticles can be removed from the glutathione reductase active site with thiol reagents such as 2-mercaptoethanol
-
-
?
bis-N-chloro-gamma-L-glutamyl derivative of GSSG + NADPH + H+
? + glutathione + NADP+
-
-
-
-
?
diethyl [2,5-bis(aziridin-1-yl)-3,6-dioxocyclohexa-1,4-diene-1,4-diyl]biscarbamate + NADPH
?
-
-
-
-
?
ajoene + NADPH
4,5,9-trithiadodeca-1,6,11-triene + NADP+
-
i.e. (E,Z)-4,5,9-trithiadodeca-1,6,11-triene-9-oxide, substrate and inhibitor
-
?
ajoene + NADPH
4,5,9-trithiadodeca-1,6,11-triene + NADP+
-
also formation of single-electron reduced product and concomitantly superoxide anion radicals
-
?
ajoene + NADPH
4,8,9,13-tetrathiahexadeca-1,6,1,15-tetraene + NADP+
-
i.e. (E,Z)-4,5,9-trithiadodeca-1,6,11-triene-9-oxide, substrate and inhibitor
-
?
ajoene + NADPH
4,8,9,13-tetrathiahexadeca-1,6,1,15-tetraene + NADP+
-
also formation of single-electron reduced product and concomitantly superoxide anion radicals
-
?
glutathione disulfide + NADH + H+
glutathione + NAD+
-
-
-
-
-
glutathione disulfide + NADH + H+
glutathione + NAD+
-
-
-
-
-
glutathione disulfide + NADH + H+
glutathione + NAD+
-
NADH is used as a coenzyme with a lower efficiency (32.7%) than NADPH
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
enzyme is required for disposal of peroxides and radicals especially in the brain
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
optimum ionic strength is 435 mM
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
key enzyme in maintaining the reducing environment in the cell, maintainance of sulfhydryl redox potential in the cytoplasm
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
optimum ionic strength is 0.75 M using Tris-HCl buffer in presence of EDTA
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
enzyme is required for disposal of peroxides and radicals especially in the brain
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
enzyme produces glutathione in spermatozoa which is required for reduction and antioxidant defense by glutathione peroxidase, enzyme is involved in protection of the cells against oxidative damage, regulatory of pentose phosphate pathway, pathway overview
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
enzyme contains an active site disulfide/dithiol depending on the redox status
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
enzyme contains an active site disulfide/dithiol depending on the redox status
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
antioxidant enzyme, protects the pancreatic cell against reactive oxygen species involved in the diabetogenic agent-induced dysfunction of pancreatic-beta-cells
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
671910, 673194, 673458, 674175, 674440, 677215, 690147, 696681, 699224, 699619, 711008, 712066, 725616
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
using levels up to 300 mM NADP+ and 1 mM glutathione, the enzyme does not catalyse the reverse reaction, indicating that its physiological function is the reduction of GSSG or GSNO but not the opposite
-
ir
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
-
?
GSSG + NADPH
glutathione + NADP+
Achromobacter starkeyi
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
?
GSSG + NADPH
glutathione + NADP+
-
methylene blue and L-cystine slowly
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
high intracellular concentration of glutathione is important for functionality of thiol groups of cellular proteins
-
-
ir
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
ferricyanide and 2,6-dichlorophenolindophenol as electron acceptors
-
r
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
r
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?, ir
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?, r
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?, r
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?
GSSG + NADPH
glutathione + NADP+
-
slight activity with D,L-lipoate
-
?, ir, r
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
?, ir, r
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
role in cell division cycle and in stress adaption on cellular level
-
-
?
GSSG + NADPH
glutathione + NADP+
-
probably major source of NADP+ for the pentose phosphate pathway in the lens
-
-
?
GSSG + NADPH
glutathione + NADP+
-
special role in cells that do no longer produce macromolecules
-
-
r
GSSG + NADPH
glutathione + NADP+
-
maintenance of high levels of GSH in cytoplasm
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
methylene blue as electron acceptor
-
?, r
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?, ir
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
?, ir, r
GSSG + NADPH
glutathione + NADP+
-
enzyme plays a key role in nutrient-induced increase in the thiol content of pancreatic-islet cells and this increase itself participates in the coupling of metabolic to secretory events
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?, ir
GSSG + NADPH
glutathione + NADP+
-
-
-
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
?
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
glutathione or other disulfides, e.g.: bis-L-gamma-glutamyl-L-cystinyl-bis-beta-alanine
-
r
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
?
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
-
?
GSSG + NADPH
glutathione + NADP+
-
mixed disulfide between coenzyme A and glutathione
-
r
GSSG + NADPH
glutathione + NADP+
-
slight activity with bis-N,N'-(gamma-glutamylcystine)
-
?, r
GSSG + NADPH
glutathione + NADP+
-
glutathione-S-sulfonate
-
?, r
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
reverse reaction only if very high concentration of NADP+ and glutathione present
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
S-sulfoglutathione and some mixed disulfides, with the exception of the mixed disulfide of coenzyme A and GSH, are poor substrates
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
trypanothione + NADPH
reduced trypanothione + NADP+
recombinant glutathione-trypanothione reductase-like enzyme
-
?
additional information
?
-
-
oxidized lipoamide and oxidized lipoic acid
-
-
-
additional information
?
-
-
enzyme is connected to neuronal loss during progression of neurodegenerative disorders
-
-
-
additional information
?
-
-
active with diverse FAD analogues, dependent on orientation of the cofactor
-
-
-
additional information
?
-
-
drug resistance to doxorubicin or selenite does not influence the enzyme activity in lung cancer cells
-
-
-
additional information
?
-
-
enzyme is connected to neuronal loss during progression of neurodegenerative disorders like Alzheimer's or Parkinson's disease
-
-
-
additional information
?
-
-
prior inhibition of glutathione reductase activity protects against the toxicity of Cr6+ to a significant extent, suggesting that it reduces Cr6+ to a toxic metabolite
-
-
-
additional information
?
-
-
enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4, selenium regulates the enzyme expression pattern
-
-
-
additional information
?
-
-
enzyme can catalyze isomerization of protein and interprotein disulfide bonds, the function is localized in the thiol domain
-
-
-
additional information
?
-
-
the enzyme is not effective to reduce cystine, lipoamide, nor trypanothione disulfide
-
-
-
additional information
?
-
-
the antioxidant enzyme is important in the parasite sensitive to oxidative stress
-
-
-
additional information
?
-
-
enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4
-
-
-
additional information
?
-
-
enzyme can catalyze isomerization of protein and interprotein disulfide bonds, the function is localized in the thiol domain
-
-
-
additional information
?
-
-
no substrates: dithiolethiones and dithiolones
-
-
-
additional information
?
-
-
modulation of the redox state of tubulin by an artificial glutathione/glutaredoxin reductase system, repair of peroxynitrite-induced disulfides in porcine brain tubulin, overview
-
-
-
additional information
?
-
-
no activity with L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide
-
-
-
additional information
?
-
-
low transhydrogenase activity with oxidized pyridine nucleotide analogs and diaphorase activity with 2,6-dichlorophenolindophenol as acceptor substrates, NADPH and NADH as donors
-
-
-
additional information
?
-
the enzyme has the ability to utilize both NADPH and NADH as electron donors
-
-
-
additional information
?
-
-
the enzyme has the ability to utilize both NADPH and NADH as electron donors
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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 disulfide + NADPH
glutathione + NADP+
-
enzyme is required for disposal of peroxides and radicals especially in the brain
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
key enzyme in maintaining the reducing environment in the cell, maintainance of sulfhydryl redox potential in the cytoplasm
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
enzyme is required for disposal of peroxides and radicals especially in the brain
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
enzyme produces glutathione in spermatozoa which is required for reduction and antioxidant defense by glutathione peroxidase, enzyme is involved in protection of the cells against oxidative damage, regulatory of pentose phosphate pathway, pathway overview
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
-
-
-
?
glutathione disulfide + NADPH
glutathione + NADP+
-
antioxidant enzyme, protects the pancreatic cell against reactive oxygen species involved in the diabetogenic agent-induced dysfunction of pancreatic-beta-cells
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
high intracellular concentration of glutathione is important for functionality of thiol groups of cellular proteins
-
-
ir
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
role in cell division cycle and in stress adaption on cellular level
-
-
?
GSSG + NADPH
glutathione + NADP+
-
probably major source of NADP+ for the pentose phosphate pathway in the lens
-
-
?
GSSG + NADPH
glutathione + NADP+
-
special role in cells that do no longer produce macromolecules
-
-
r
GSSG + NADPH
glutathione + NADP+
-
maintenance of high levels of GSH in cytoplasm
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
enzyme plays a key role in nutrient-induced increase in the thiol content of pancreatic-islet cells and this increase itself participates in the coupling of metabolic to secretory events
-
-
?
GSSG + NADPH
glutathione + NADP+
-
production of substrate for: glutathione peroxidase EC 1.11.1.9, glutathione-homocystine oxidoreductase EC 1.8.4.1, glutathione-protein disulfide oxidoreductase EC 1.8.4.2
-
-
?, ir
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
GSSG + NADPH
glutathione + NADP+
-
maintenance of glutathione/GSSG ratio is a protective mechanism for intracellular thiols during growth in atmospheric oxygen
-
-
?
additional information
?
-
-
enzyme is connected to neuronal loss during progression of neurodegenerative disorders
-
-
-
additional information
?
-
-
drug resistance to doxorubicin or selenite does not influence the enzyme activity in lung cancer cells
-
-
-
additional information
?
-
-
enzyme is connected to neuronal loss during progression of neurodegenerative disorders like Alzheimer's or Parkinson's disease
-
-
-
additional information
?
-
-
prior inhibition of glutathione reductase activity protects against the toxicity of Cr6+ to a significant extent, suggesting that it reduces Cr6+ to a toxic metabolite
-
-
-
additional information
?
-
-
enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4, selenium regulates the enzyme expression pattern
-
-
-
additional information
?
-
-
the antioxidant enzyme is important in the parasite sensitive to oxidative stress
-
-
-
additional information
?
-
-
enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4
-
-
-
additional information
?
-
-
modulation of the redox state of tubulin by an artificial glutathione/glutaredoxin reductase system, repair of peroxynitrite-induced disulfides in porcine brain tubulin, overview
-
-
-
additional information
?
-
-
no activity with L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
activity with diverse FAD analogues; FAD enzyme; properties of glutathione reductase reconstituted with FAD analogues
FAD
-
FAD enzyme; properties of glutathione reductase reconstituted with FAD analogues
FAD
-
FAD enzyme
FAD
-
flavoenzyme, interaction with Asp311 and Leu352, binding domain structure
FAD
-
-
NADH
-
NADH is used as a coenzyme by rat kidney glutathione reductase but with a lower efficiency (32.7%) than NADPH
NADPH
-
20times more activity than with NADH; can utilize both NADPH and NADH, more active with NADPH
NADPH
-
diphosphate group is bound at the C-terminal edge of a parallel stranded beta-sheet as is common in nucleotide-binding proteins
NADPH
-
5% of the activity with NADH, 3fold higher affinity of root enzyme compared to chloroplast enzyme
NADPH
-
-
NADPH
-
-
393993, 394712, 394714, 394718, 394723, 394724, 394726, 394728, 394729, 394730, 394776, 394779, 659182, 659592, 689306, 690147, 696556, 696681, 699224, 699241, 699619, 711008, 712066, 725616
NADPH
-
-
393993, 394708, 394709, 394718, 394723, 394746, 394764, 657763, 686077, 688032, 689967, 697449, 700654, 712997, 725618
NADPH
-
-
additional information
-
as malaria brings riboflavin deficiency, in effection regions a large portion of enzymes miss FAD, but are as well active
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
phosphate
selenium
-
regulates the enzyme expression pattern, enzyme contains a catalytic selenocysteine
Zn2+
-
glutathione reductase is non-competitively inhibited up to 2 mM and activated above this concentration
additional information
-
optimum ionic strength of enzyme is 50 mM Tris–HCl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R(S),2R(S),3S(R),4S(R))-2,3-dihydroxycyclo-hexane-1,4-diyl dinitrate
-
non-competitive inhibition
(1R(S),2R(S),4R(S),5R(S))-2,5-dihydroxycyclo-hexane-1,4-diyl dinitrate
-
non-competitive inhibition
(1S(R),2S(R),5R(S),6R(S))-5-bromo-9-oxabicyclo[4.2.1] nonan-2-yl nitrate
-
non-competitive inhibition
(1S(R),3S(R),4S(R),6S(R))-4,6-dihydroxycyclo-hexane-1,3-diyl dinitrate
-
non-competitive inhibition
(2R(S),7R(S))-7-hydroxybicyclo[2.2.1]heptan-2-yl nitrate
-
non-competitive inhibition
(2S(R),7R(S))-7-hydroxybicyclo[2.2.1] heptan-2-yl nitrate
-
non-competitive inhibition
(9R(S))-hydroxy-1,2,3,4-tetrahydro-1,4-methano-naphthalen-2R(S)-yl nitrate
-
non-competitive inhibition
1,2-bis[methylsulfonyl]-1-[2-[chloroethyl]-2-(methylamino)carbonyl]hydrazine
-
0.05 mM, 28% inhibition
1,3-Bis(2-chloroethyl)-1-nitrosourea
-
significant inhibition of recombinant isoform GR1 is observed at high concentrations of 1 mM and above
1-methyl-4-(2-methyl-1,3-dioxo-2,3,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-5(1H)-yl)pyridinium
-
poor inhibitor
2,5-bis(aziridin-1-yl)-3,6-bis[(2-hydroxyethyl)amino]cyclohexa-2,5-diene-1,4-dione
-
-
2-acetylamino-3-[4-(2-acetylamino-2-carboxy-ethylsulfanylthio carbonylamino)phenylthiocarbamoylsulfanyl]propionic acid
-
irreversible and selective glutathione reductase inhibitor, almost complete inhibition at 0.1 mM for 1 h, thereafter, the enzyme activity starts to return and reaches 63% of the control at the end of 8 h
2-acetylamino-3-[4-(2-acetylamino-2-carboxyethylsulfanylthiocarbonylamino)phenylthiocarbamoylsulfanyl]propionic acid
-
irreversible glutathione reductase inhibitor
3'-hydroxy-4'-O-methylisoscutellarein 7-O-[6'''-O-acetyl-beta-D-allopyranosyl-(1->2)]-beta-D-glucopyranoside
-
-
3-[5-[8-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)octyl]-1H-tetrazol-1-yl]propanenitrile
5-(3alpha,12alpha-dihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(4-chlorophenyl)-8-fluoro-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
8-azido-5-(4-chlorophenyl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
acylfulvene
-
reversible inhibition, less than 10% residual activity at 1.25 mM, inhibition by 1.0 or 1.25 mM acylfulvene is reduced by 30% in the presence of NDPH
ajoene
-
i.e. (E,Z)-4,5,9-trithiadodeca-1,6,11-triene-9-oxide, natural compound from garlic, Allium sativum, covalent inhibition, but also substrate; time- and temperature-dependent inhibition, mixed disulfide between cative site Cys58 and the inhibitor, modified enzyme shows a markedly increased oxidative activity
apigenin
-
flavonone, non-competitive with both NADPH and GSSG, influence on glutathione recognition
auranofin
-
complete inhibition of both enzyme reductase activities at 10 nM
Baicalin
-
slightly, flavone glycoside, non-competitive with both NADPH and GSSG, influence on glutathione recognition
catechin
-
slightly, catechin, non-competitive with both NADPH and GSSG, influence on glutathione recognition
chrysin
-
slightly, flavonone, non-competitive with both NADPH and GSSG, influence on glutathione recognition
diethyl dicarbonate
-
chloroplast enzyme, 100% inhibition at 4 mM, 23% inhibition at 1 mM
diethyl [2,5-bis(aziridin-1-yl)-3,6-dioxocyclohexa-1,4-diene-1,4-diyl]biscarbamate
-
-
Dinitrosated isomers of N,N'-bis[N(2-chloroethyl)-N-carbonyl]cysteamine
-
-
-
epicatechin
-
slightly, catechin, non-competitive with both NADPH and GSSG, influence on glutathione recognition
Epicatechin gallate
-
slightly, catechin, non-competitive with both NADPH and GSSG, influence on glutathione recognition
epigallocatechin
-
slightly, catechin, non-competitive with both NADPH and GSSG, influence on glutathione recognition
epigallocatechin gallate
-
catechin, non-competitive with both NADPH and GSSG, influence on glutathione recognition
ethyl [5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
ethyl [5-(3-chlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
-
-
fisetin
-
flavonol, non-competitive with both NADPH and GSSG, influence on glutathione recognition
GSH
-
With regard to GSSG as variable substrate at fixed NADPH concentration (0.1 mM), GSH is a non-competitive inhibitor. With regard to NADPH as variable substrate at fixed GSSG concentration, GSH is a non-competitive inhibitor
Haemin
-
mediates covalent cross-linking and degradation of the enzyme
hydroxymethylacylfulvene
-
irreversible inhibition, less than 10% residual activity at 1.25 mM, inhibition by 0.625 or 1.25 mM hydroxymethylacylfulvene is reduced by 45% in the presence of NDPH
hypolaetin 7-O-[6'''-O-acetyl-beta-D-allopyranosyl-(1->2)]-beta-D-glucopyranoside
-
-
isoscutellarein 7-O-[6'''-O-acetyl-beta-D-allopyranosyl-(1->2)]-beta-D-glucopyranoside
-
-
kaempferol
-
slightly, flavonol, non-competitive with both NADPH and GSSG, influence on glutathione recognition
L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide
-
competitive inhibitor
morin
-
slightly, flavonol, non-competitive with both NADPH and GSSG, influence on glutathione recognition
myricetin
-
flavonol, non-competitive with both NADPH and GSSG, influence on glutathione recognition
Nicotine
-
0.5 mg/kg, significant inhibition of enzymatic activity in liver (61.5%), lung (65%), heart (70.5%), stomach (72.5%), kidney (64%) and testicle (71.5%)
Phenylmethylsulfonylfluoride
-
i.e. PMSF, chloroplast enzyme, slight inhibition
putrescine
-
the early decrease of glutathione reductase activity in leaves treated with polyamines can be due to a direct interaction of these compounds with the enzyme
pyridoxal 5'-phosphate
-
70% inactivation, due to specific modification of an epsilon-amino group lysine residue
quercetin
-
flavonol, non-competitive with both NADPH and GSSG, influence on glutathione recognition
rutin
-
slightly, flavonol glycoside, non-competitive with both NADPH and GSSG, influence on glutathione recognition
spermidine
-
the early decrease of glutathione reductase activity in leaves treated with polyamines can be due to a direct interaction of these compounds with the enzyme
spermine
-
the early decrease of glutathione reductase activity in leaves treated with polyamines can be due to a direct interaction of these compounds with the enzyme
sulfhydryl reagents
-
in presence but not in absence of reduced coenzyme
TH-302
-
TH-302 at 300 mg/kg significantly inhibits glutathione reductase activity by 60% as compared with the controls, at 3 h after the injection
trans-(1S(R),6S(R))-6-hydroxycyclohex-3-enyl nitrate
-
non-competitive inhibition
trans-(1S(R),8S(R),Z)-8-hydroxycyclooct-4-enyl nitrate
-
non-competitive inhibition
[5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetic acid
[{1-phenyl-2,5-di(2-pyridyl)phosphole}AuCl]
-
gold-phosphole inhibitor, 1 nM, 50% inhibition, reversible
1,3-bis-(2-chloroethyl) 1-nitrosourea
-
physiological effects of enzyme inhibition in spermatozoa are increase of lipid peroxidation and impairment of sperm motility
1,3-Bis-(2-chloroethyl)-1-nitrosourea
-
time- and dose-dependent irreversible inhibition
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione
-
-
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione
-
-
2,5-bis(ethylamino)-3,6-di(aziridinyl)-1,4-benzoquinone
-
complete inhibition at 0.05 mM
2-methyl-5-(1-naphthyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
2-methyl-5-(1-naphthyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
2-methyl-5-pyridin-4-yl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
2-methyl-5-pyridin-4-yl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
3-[5-[8-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)octyl]-1H-tetrazol-1-yl]propanenitrile
-
-
3-[5-[8-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)octyl]-1H-tetrazol-1-yl]propanenitrile
-
-
5-(1-anthryl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
5-(1-anthryl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
poor inhibitor
5-(4-chlorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
5-(4-chlorophenyl)-8-fluoro-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
5-(4-chlorophenyl)-8-fluoro-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
5-(pentafluorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
5-(pentafluorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
6-[2-(3-fluoromethyl)-1,4-naphthoquinolyl]hexanoic acid
-
IC50: 0.0041 mM, irreversible inhibition
6-[2-(3-fluoromethyl)-1,4-naphthoquinolyl]hexanoic acid
-
IC50: 0.0064 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG, irreversible inhibition
6-[2-(3-methyl)-1,4-naphthoquinolyl]hexanoic acid
-
IC50: 0.0032 mM, uncompetitive inhibitor
6-[2-(3-methyl)-1,4-naphthoquinolyl]hexanoic acid
-
IC50: 0.0045 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG, uncompetitive inhibitor
8-azido-5-(4-chlorophenyl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
8-azido-5-(4-chlorophenyl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
-
acetaminophen-glutathione conjugate
-
the enzyme activity is inhibited to 48.1% after treatment with 2.96 mM acetaminophen-glutathione conjugate, the enzyme activity (from hepatocytes lysate) is decreased to 79%, 67%, and 397%, in 0.37, 1.48 and 3.7 mM concentration of the conjugate, respectively, at pH 7.6 at 25°C
acetaminophen-glutathione conjugate
-
the enzyme activity is inhibited to 52.7% after treatment with 2.96 mM acetaminophen-glutathione conjugate, at pH 7.6 at 25°C
Ca2+
-
inhibition is non-competitive with respect to GSSG and uncompetitive with respect to NADPH
carmustine
-
i.e. 1,3-bis(2-chloroethyl)-1-nitroso-urea, irreversible inhibitor, complete inhibition at 0.625 mM
Cd2+
-
noncompetitive inhibition with respect to both glutathione disulfide and NADPH
cefodizime
-
competitive, 21% inhibition in vivo, effect decreases with time
cefotaxime
-
noncompetitive, 46% inhibition in vivo, effect decreases with time
Cr6+
-
during the metabolism of Cr VI, glutathione reductase activity is inhibited
Cu2+
-
in the presence of 1 mM Cu2+, approximately 5% of residual activity is detected
ethyl [5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
-
-
ethyl [5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
-
-
Fe2+
-
addition of exogenous Fe2+ (but not Fe3+) potentiates NADPH-induced inactivation of glutathione reductase, after a 2 min incubation period, 0.05 mM Fe2+ plus 0.3 mM NADPH induce 57% loss of enzyme activity
glutathione
-
GSH functions as an inhibitor at relatively high concentrations (41 mM), and also only in the lower substrate concentration range
glutathione
-
inhibits the turtle liver GR only at high concentrations (6 mM), although this I50 value is within the physiological range of GSH concentrations in most cell types
Melarsen oxide
-
i.e. p-(4,6-diamono-s-triazin-2-yl)aminophenylarsenoxide; potent inhibitor, reversible by excess of thiols, more sensitive with NADPH
Melarsen oxide
-
i.e. p-(4,6-diamono-s-triazin-2-yl)aminophenylarsenoxide; potent inhibitor, reversible by excess of thiols, more sensitive with NADPH
menadione
-
IC50: 0.042 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG
N-(2-cyanoethyl)-9-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)nonanamide
-
-
N-(2-cyanoethyl)-9-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)nonanamide
-
-
N-ethylmaleimide
-
root enzyme is slightly more sensitive than chloroplast enzyme
N-ethylmaleimide
-
chloroplast enzyme, 90% inhibition at 1 mM, partially reversible by GSSG 0.5 mM
NADP+
-
With regard to GSSG as variable substrate at fixed NADPH concentration, NADP+ is an uncompetitive inhibitor. With regard to NADPH as variable substrate at fixed GSSG concentration, NADP+ is a competitive inhibitor
NADP+
-
competitive product inhibition regarding NADPH and non-competitive product inhibition regarding glutathione disulfide, however, NADP+ (up to 1m M) is not inhibitor when assays are performed at 1 mM glutathione disulfide and 300 mM NADPH
NADPH
-
promotes formation of aggregates, reversible by thiols, e.g. glutathione or 2-mercaptoethanol
NADPH
-
slow inactivation in vitro due to inter- or intramolecular disulfide formation
NADPH
-
reversible reductive inactivation with isozyme GR-1H and slightly with GR-2H
NADPH
-
58% inhibition at 0.3 mM after 60 min incubation, exogenously added antioxidants including ethanol, dimethylsulfoxide and 2-deoxyribose do not protect glutathione reductase against NADPH-induced inactivation, whilst addition of exogenous Fe2+ (but not Fe3+) potentiates the inactivation, removal of oxygen from the medium leads to increased inhibition of glutathione reductase, whereas pre-incubation of the Fe2+-containing medium for 30 min under normoxic conditions prior to the addition of GR abolishes the enzyme inactivation by NADPH
Ni2+
-
non-competitive inhibition with respect to GSSG and uncompetitive inhibition with respect to NADPH
Ni2+
-
noncompetitive inhibition with respect to glutathione disulfide and uncompetitive with respect to NADPH
Ni2+
-
inhibition is competitive with respect to GSSG and uncompetitive with respect to NADPH
p-hydroxymercuribenzoate
-
chloroplast enzyme is slightly more sensitive than root enzyme
peroxynitrite
-
inactivation of enzyme by formation of nitrotyrosine near the catalytic center, 2.5fold increased Km-value and 1.7fold decreased Vmax, molecular modeling
peroxynitrite
-
40% inhibition of activity with 0.1 mM, 72% inhibition of activity with 0.2 mM
Zn2+
-
noncompetitive inhibition with respect to both glutathione disulfide and NADPH
Zn2+
-
in the presence of 1 mM Zn2+, approximately 55% of residual activity is detected
Zn2+
-
Zn acetate at concentrations of 0.1 mM or greater inactivate glutathione reductase via an NADPH-dependent mechanism. Zn2+ is a highly effective inhibitor of glutathione reductase activity in astrocytes. This inhibition impairs their capacity to detoxify H2O2
Zn2+
-
glutathione reductase is non-competitively inhibited up to 2 mM and activated above this concentration
Zn2+
-
chloroplast enzyme, 94% inhibition at 0.5 mM, reversible and competitive to GSSG
[4-(3-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)phenyl]acetic acid
-
IC50: 0.0014 mM
[4-(3-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)phenyl]acetic acid
-
IC50: 0.0077 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG
[4-[3-(fluoromethyl)-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl]phenyl]acetic acid
-
IC50: 0.0035 mM
[4-[3-(fluoromethyl)-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl]phenyl]acetic acid
-
IC50: 0.002 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG
[5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetic acid
-
binds to the large helices-containing cavity at the dimer interface
[5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetic acid
-
-
additional information
-
glutathione reductase is not influenced by Al3+, Ba2+, Mn2+, and Li+ at 0.01-0.1 mM, and by Ca2+ and Mo6+ at 0.005-0.125 mM
-
additional information
-
regulation by inactivation in vivo, e.g. by disulfide bridging
-
additional information
-
cytotoxic effect of selenite on drug-sensitive and drug-resistant cancer cell lines, overview
-
additional information
-
bis-nitro-enzyme form is impaired in peptide substrate binding with a 20fold increased Km for glutathione disulfide, overview
-
additional information
-
no inhibition by 1,2-bis[methylsulfonyl]-1-[2-[chloroethyl]-2 ](methylamino)carbonyl hydrazine
-
additional information
-
not inhibited by Ca2+, addition of imidazole up to 0.8 M has no significant effect on the activity
-
additional information
-
regulation by inactivation in vivo, e.g. by disulfide bridging
-
additional information
-
ethyl [5-(3-chlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate and 1-methyl-4-(2-methyl-1,3-dioxo-2,3,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-5(1H)-yl)pyridinium are no inhibitors for the parasite enzyme, numerous noncompetitive inhibitors bind to the large helices-containing cavity at the dimer interface which therefore is a target for selective drugs
-
additional information
-
IC50 for quinoline-5,8-dione is above 0.13 mM
-
additional information
-
glutathione reductase activity is not inhibited by up to 1 mM sodium arsenate
-
additional information
-
glutathione reductase activity is not inhibited by up to 1 mM sodium arsenate
-
additional information
-
vitamin E restores the inhibition of glutathione reductase due to nicotine administration in liver, lung, heart, stomach and kidney tissue, but not in testicle tissue
-
additional information
-
regulation by inactivation in vivo, e.g. by disulfide bridging
-
additional information
-
no inhibition by chlorambucil, melphalan, busulfan and carboplatin
-
additional information
-
up to 2 mM, illudin S does not inhibit glutathione reductase activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
abscisic acid
-
0.1 mM, significant enhancement of activity 24 h after treatment
alpha-crystallin
-
2 mg/ml causes 37% increase in activity, 1 mg/ml causes 20% enhancement
-
cadmium
-
100 mM, 111% and 100% enhancement of enzyme activity in root tissue after 7 and 14 days, respectively
DL-dithiothreitol
-
0.25-4 mM, the best enhancement of activity (96.6%) is obtained by a concentration of 1 mM
doxorubicin
-
differences between drug-sensitive and drug-resistant cells, overview
phenanthrene
-
exposure to 0.5 microM phenanthrene results in significant increases in the levels of both enzymatic and non-enzymatic antioxidants, with the levels of total glutathione and ascorbate doubling, and the activities of GR increasing by 20fold after 72 h of exposure to PHEN
Selenite
-
4fold increase in activity in U-1256 cells, less pronounced in presence of doxorubicin, differences between drug-sensitive and drug-resistant cells, overview
FAD analogues
-
properties of glutathione reductase reconstituted with FAD analogues
-
FAD analogues
-
properties of glutathione reductase reconstituted with FAD analogues
-
additional information
-
oxidative agents, e.g. cumene hydroperoxide or xanthine, increase the flux through the pentose phosphate pathway and enzyme activity
-
additional information
-
glutathione reductase activity is not activated by up to 1 mM sodium arsenate
-
additional information
-
glutathione reductase activity is not activated by up to 1 mM sodium arsenate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.114
5,5'-dithiobis(2-nitrobenzoic acid)
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
0.71
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C
0.0123
glutathione disulfide
-
in 50 mM potassium phosphate buffer (pH 7.0)
0.045
glutathione disulfide
-
chloroquine-sensitive strain D10, pH 6.9, 25°C
0.0531
glutathione disulfide
-
in 100 mM potassium phosphate buffer, pH 7.4, 4 mM EDTA, at 37°C
0.065
glutathione disulfide
-
chloroquine-resistant strain FCR3, pH 6.9, 25°C
0.071
glutathione disulfide
-
chloroquine-sensitive strain 3D7, pH 6.9, 25°C
0.073
glutathione disulfide
-
chloroquine-sensitive strain S106, pH 6.9, 25°C
0.074
glutathione disulfide
-
chloroquine-resistant strain Dd2, pH 6.9, 25°C
0.076
glutathione disulfide
-
chloroquine-sensitive strain HB3, pH 6.9, 25°C
0.08
glutathione disulfide
-
chloroquine-resistant strain 7G8, pH 6.9, 25°C
0.088
glutathione disulfide
-
chloroquine-resistant strain K1, pH 6.9, 25°C
0.114
glutathione disulfide
-
in 100 mM potassium phosphate buffer (pH 8.0), at 25°C
0.59
glutathione disulfide
-
in 50 mM potassium phosphate buffer pH 7.0, at 37°C
0.00446
GSSG
-
anoxic enzyme in 50 mM potassium phosphate, pH 7.4, 1 mM EDTA, 0.1 mM GSSG and 0.2 mM NADPH
0.0715
GSSG
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 150 mM potassium phosphate pH 7.0, at 37°C
0.205
GSSG
-
full length enzyme, in 150 mM potassium phosphate pH 7.0, at 37°C
0.00682
NADPH
-
anoxic enzyme in 50 mM potassium phosphate, pH 7.4, 1 mM EDTA, 0.1 mM GSSG and 0.2 mM NADPH
0.0153
NADPH
-
in 100 mM potassium phosphate buffer, pH 7.4, 4 mM EDTA, at 37°C
additional information
additional information
-
thermal dependency of Km
-
additional information
additional information
-
different isozymes, temperature-dependent, homo-glutathione
-
additional information
additional information
-
kinetics, hysteretic behaviour
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
1,4-dihydroxy-9,10-anthraquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.1
1,8-dihydroxy-9,10-anthraquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
5
2,5-bis(aziridin-1-yl)cyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°CpH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
1.1
2,6-dimethyl-1,4-benzoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.14
2-methyl-1,4-naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
7
5,8-Dihydroxy-1,4-naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
5.5
5-hydroxy-1,4-naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.22
9,10-phenanthrene quinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.1
diethyl [2,5-bis(aziridin-1-yl)-3,6-dioxocyclohexa-1,4-diene-1,4-diyl]biscarbamate
Plasmodium falciparum
-
kcat_Km above 0.8 1/sec*mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°Ckcat above 0.1 1/sec, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.3
tetramethyl-1,4-benzoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.2
trimethyl-1,4-benzoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
1
1,4-Naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
1.2
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C
16
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
50.14
glutathione disulfide
Ipomoea batatas
-
in 100 mM potassium phosphate buffer (pH 8.0), at 25°C
0.19
GSSG
Schistosoma mansoni
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 150 mM potassium phosphate pH 7.0, at 37°C
20.8
trypanothione
Homo sapiens
-
recombinant glutathione-trypanothione reductase-like enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
1,4-dihydroxy-9,10-anthraquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
11244
5.2
1,4-Naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
1083
0.4
1,8-dihydroxy-9,10-anthraquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
7508
0.1
2,5-bis(aziridin-1-yl)-3,6-dimethylcyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
kcat_Km above 0.1 1/sec*mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
18751
0.25
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
kcat_Km above 0.25 1/sec*mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
15103
40
2,5-bis(aziridin-1-yl)cyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
19328
6.5
2,6-dimethyl-1,4-benzoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
3260
1.8
2-methyl-1,4-naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
1950
430
5,8-Dihydroxy-1,4-naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
5918
360
5-hydroxy-1,4-naphthoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
1344
4.2
9,10-phenanthrene quinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
6474
0.8
diethyl [2,5-bis(aziridin-1-yl)-3,6-dioxocyclohexa-1,4-diene-1,4-diyl]biscarbamate
Plasmodium falciparum
-
kcat_Km above 0.8 1/sec*mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
14415
1
tetramethyl-1,4-benzoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
7640
0.7
trimethyl-1,4-benzoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
13710
0.65
trimethyl-aziridinyl-1,4-benzoquinone
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
19377
439.8
glutathione disulfide
Ipomoea batatas
-
in 100 mM potassium phosphate buffer (pH 8.0), at 25°C
973
4850
glutathione disulfide
Rattus norvegicus
-
in 100 mM potassium phosphate buffer, pH 7.4, 4 mM EDTA, at 37°C
973
16800
NADPH
Rattus norvegicus
-
in 100 mM potassium phosphate buffer, pH 7.4, 4 mM EDTA, at 37°C
5
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0174
(1R(S),2R(S),3S(R),4S(R))-2,3-dihydroxycyclo-hexane-1,4-diyl dinitrate
-
-
0.0184
(1R(S),2R(S),4R(S),5R(S))-2,5-dihydroxycyclo-hexane-1,4-diyl dinitrate
-
-
0.0215
(1S(R),2S(R),5R(S),6R(S))-5-bromo-9-oxabicyclo[4.2.1] nonan-2-yl nitrate
-
-
0.0179
(1S(R),3S(R),4S(R),6S(R))-4,6-dihydroxycyclo-hexane-1,3-diyl dinitrate
-
-
0.0188
(9R(S))-hydroxy-1,2,3,4-tetrahydro-1,4-methano-naphthalen-2R(S)-yl nitrate
-
-
0.2
1-methyl-4-(2-methyl-1,3-dioxo-2,3,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-5(1H)-yl)pyridinium
-
pH 6.9, 25°C
0.0005
2,4,6-trinitrobenzene-sulfonate
-
below, at 50% inhibition value, leading to oxidase activity
0.5
2,5-bis(aziridin-1-yl)-3,6-bis[(2-hydroxyethyl)amino]cyclohexa-2,5-diene-1,4-dione
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.03
2,5-bis(aziridin-1-yl)-3,6-dimethylcyclohexa-2,5-diene-1,4-dione
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0025 - 0.012
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione
0.002
2,5-bis(aziridin-1-yl)cyclohexa-2,5-diene-1,4-dione
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0028
2,6-dimethyl-1,4-benzoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.5
2-hydroxy-3-methyl-1,4-naphthoquinone
-
Ki above 0.5 mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0005 - 0.011
2-methyl-5-(1-naphthyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
0.0025 - 0.015
2-methyl-5-pyridin-4-yl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
0.016 - 0.16
3-[5-[8-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)octyl]-1H-tetrazol-1-yl]propanenitrile
0.0006
5,8-Dihydroxy-1,4-naphthoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0025 - 0.2
5-(1-anthryl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
0.0061
5-(3alpha,12alpha-dihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
0.0723
5-(3alpha-hydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
0.0004 - 0.0059
5-(4-chlorophenyl)-8-fluoro-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
0.0019 - 0.0025
5-(pentafluorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
0.00015
5-hydroxy-1,4-naphthoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0014 - 0.0062
8-azido-5-(4-chlorophenyl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
0.3
diethyl [2,5-bis(aziridin-1-yl)-3,6-dioxocyclohexa-1,4-diene-1,4-diyl]biscarbamate
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0066 - 0.013
ethyl [5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
0.0093
ethyl [5-(3-chlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
-
pH 6.9, 25°C
0.18
hydroxymethylacylfulvene
-
at 25°C, pH not specified in the publication
0.01464
L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide
-
in 100mM in potassium phosphate, pH 7.5, temperature not specified in the publication
0.0108 - 0.0227
N-(2-cyanoethyl)-9-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)nonanamide
0.0162
trimethyl-1,4-benzoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0072 - 0.014
[5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetic acid
0.15
1,4-dihydroxy-9,10-anthraquinone
-
Ki above 0.15 mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.15
1,4-dihydroxy-9,10-anthraquinone
-
Ki above 0.15 mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0025
1,4-Naphthoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.035
1,8-dihydroxy-9,10-anthraquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.09
1,8-dihydroxy-9,10-anthraquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0032
11-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)undecanoic acid
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.057
11-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)undecanoic acid
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0025
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.012
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.5
2,5-bis(ethylamino)-3,6-di(aziridinyl)-1,4-benzoquinone
-
Ki above 0.5 mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.5
2,5-bis(ethylamino)-3,6-di(aziridinyl)-1,4-benzoquinone
-
Ki above 0.5 mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.5
2-Hydroxy-1,4-naphthoquinone
-
Ki above 0.5 mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.5
2-Hydroxy-1,4-naphthoquinone
-
Ki above 0.5 mM, pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.028
2-methyl-1,4-naphthoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.039
2-methyl-1,4-naphthoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0005
2-methyl-5-(1-naphthyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.011
2-methyl-5-(1-naphthyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0025
2-methyl-5-pyridin-4-yl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.015
2-methyl-5-pyridin-4-yl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.016
3-[5-[8-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)octyl]-1H-tetrazol-1-yl]propanenitrile
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.16
3-[5-[8-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)octyl]-1H-tetrazol-1-yl]propanenitrile
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0025
5-(1-anthryl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.2
5-(1-anthryl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0006
5-(4-chlorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0054
5-(4-chlorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0004
5-(4-chlorophenyl)-8-fluoro-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0059
5-(4-chlorophenyl)-8-fluoro-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0019
5-(pentafluorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0025
5-(pentafluorophenyl)-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0014
8-azido-5-(4-chlorophenyl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0062
8-azido-5-(4-chlorophenyl)-2-methyl-5a,9a-dihydropyrido[3,4-b]quinoxaline-1,3(2H,5H)-dione
-
pH 6.9, 25°C
0.0025
9,10-phenanthrene quinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.012
9,10-phenanthrene quinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0066
ethyl [5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
-
pH 6.9, 25°C
0.013
ethyl [5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetate
-
pH 6.9, 25°C
5
glutathione
-
competitive product inhibition regarding glutathione disulfide, at 30°C and pH 7.5
10
glutathione
-
non-competitive product inhibition regarding NADPH, at 30°C and pH 7.5
7.985
GSH
-
pH 7.4, 37°C, GSSG as variable substrate at fixed NADPH concentration (0.1 mM)
0.0108
N-(2-cyanoethyl)-9-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)nonanamide
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0227
N-(2-cyanoethyl)-9-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)nonanamide
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.043
NADP+
-
pH 7.4, 37°C, NADPH as variable substrate at fixed GSSG concentration
0.052
NADP+
-
competitive product inhibition regarding NADPH, at 30°C and pH 7.5
0.219
NADP+
-
pH 7.4, 37°C, GSSG as variable substrate at fixed NADPH concentration (0.1 mM)
1
NADP+
-
non-competitive product inhibition regarding glutathione disulfide, at 30°C and pH 7.5
0.001
Nitrofurantoin
-
at 50% inhibition value, enzyme partially purified from platelets
0.16
tetramethyl-1,4-benzoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.25
tetramethyl-1,4-benzoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.009
trimethyl-aziridinyl-1,4-benzoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.01
trimethyl-aziridinyl-1,4-benzoquinone
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0072
[5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetic acid
-
pH 6.9, 25°C
0.014
[5-(3,5-dichlorophenyl)-1,3-dioxo-3,5,5a,9a-tetrahydropyrido[3,4-b]quinoxalin-2(1H)-yl]acetic acid
-
pH 6.9, 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00717
(1R(S),2R(S),3S(R),4S(R))-2,3-dihydroxycyclo-hexane-1,4-diyl dinitrate
Homo sapiens
-
-
0.00871
(1R(S),2R(S),4R(S),5R(S))-2,5-dihydroxycyclo-hexane-1,4-diyl dinitrate
Homo sapiens
-
-
0.011
(1S(R),2S(R),5R(S),6R(S))-5-bromo-9-oxabicyclo[4.2.1] nonan-2-yl nitrate
Homo sapiens
-
-
0.0081
(1S(R),3S(R),4S(R),6S(R))-4,6-dihydroxycyclo-hexane-1,3-diyl dinitrate
Homo sapiens
-
-
0.0103
(9R(S))-hydroxy-1,2,3,4-tetrahydro-1,4-methano-naphthalen-2R(S)-yl nitrate
Homo sapiens
-
-
0.0035
11-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)undecanoic acid
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0024
2,5-bis(aziridin-1-yl)-3,6-bis[(2-hydroxyethyl)amino]cyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.00004
2,5-bis(aziridin-1-yl)-3,6-dimethylcyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.00001
2,5-bis(aziridin-1-yl)-3-(hydroxymethyl)-6-methylcyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.00043
2,5-bis(aziridin-1-yl)cyclohexa-2,5-diene-1,4-dione
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.295
3'-hydroxy-4'-O-methylisoscutellarein 7-O-[6'''-O-acetyl-beta-D-allopyranosyl-(1->2)]-beta-D-glucopyranoside
Bos taurus
-
in 100 mM sodium phosphate buffer, pH 7.4, at 37°C
0.0014
3-[5-[8-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)octyl]-1H-tetrazol-1-yl]propanenitrile
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0045
5-(3alpha,12alpha-dihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
-
-
0.0471
5-(3alpha-hydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
-
-
0.0018
diethyl [2,5-bis(aziridin-1-yl)-3,6-dioxocyclohexa-1,4-diene-1,4-diyl]biscarbamate
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.216
hydroxymethylacylfulvene
Saccharomyces cerevisiae
-
at 25°C, pH not specified in the publication
0.177
hypolaetin 7-O-[6'''-O-acetyl-beta-D-allopyranosyl-(1->2)]-beta-D-glucopyranoside
Bos taurus
-
in 100 mM sodium phosphate buffer, pH 7.4, at 37°C
0.372
isoscutellarein 7-O-[6'''-O-acetyl-beta-D-allopyranosyl-(1->2)]-beta-D-glucopyranoside
Bos taurus
-
in 100 mM sodium phosphate buffer, pH 7.4, at 37°C
0.0015
N-(2-cyanoethyl)-9-(3-methyl-1,4-dioxo-1,4-dihydronaphthalen-2-yl)nonanamide
Plasmodium falciparum
-
pH 7.0, 0.1 M potassium phosphate, 1 mM EDTA, 25°C
0.0014 - 0.0077
[4-(3-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)phenyl]acetic acid
0.002 - 0.0035
[4-[3-(fluoromethyl)-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl]phenyl]acetic acid
0.0041
6-[2-(3-fluoromethyl)-1,4-naphthoquinolyl]hexanoic acid
Homo sapiens
-
IC50: 0.0041 mM, irreversible inhibition
0.0064
6-[2-(3-fluoromethyl)-1,4-naphthoquinolyl]hexanoic acid
Plasmodium falciparum
-
IC50: 0.0064 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG, irreversible inhibition
0.0032
6-[2-(3-methyl)-1,4-naphthoquinolyl]hexanoic acid
Homo sapiens
-
IC50: 0.0032 mM, uncompetitive inhibitor
0.0045
6-[2-(3-methyl)-1,4-naphthoquinolyl]hexanoic acid
Plasmodium falciparum
-
IC50: 0.0045 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG, uncompetitive inhibitor
0.042
menadione
Plasmodium falciparum
-
IC50: 0.042 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG
0.0014
[4-(3-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)phenyl]acetic acid
Homo sapiens
-
IC50: 0.0014 mM
0.0077
[4-(3-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)phenyl]acetic acid
Plasmodium falciparum
-
IC50: 0.0077 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG
0.002
[4-[3-(fluoromethyl)-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl]phenyl]acetic acid
Plasmodium falciparum
-
IC50: 0.002 mM, at pH 6.9 and 25°C in the presence of 1 mM GSSG
0.0035
[4-[3-(fluoromethyl)-1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl]phenyl]acetic acid
Homo sapiens
-
IC50: 0.0035 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.009
0.11
-
crude liver homogenate, in 100 mM potassium phosphate buffer, pH 7.4, 4 mM EDTA, at 37°C
1.07
-
in C6 glioma cells, pH and temperature not specified in the publication
114
120
180
204
207
240
246
248
250
269
643
-
89.8fold purified enzyme, in 50 mM potassium phosphate buffer pH 7.0, at 25°C
additional information
250
-
after 2356fold purification, in 100 mM potassium phosphate buffer, pH 7.4, 4 mM EDTA, at 37°C
additional information
-
relative activity and reaction velocity with diverse FAD analogues
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.8
6.9
7.4
7.5
7.8 - 8.6
8.1
8.2
8
-
enzyme activity in 50 mM Tris-HCl buffer (pH 8.0) is higher than in 50 mM phosphate buffer (pH 8.0)
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
50% activity at pH 6.5 and pH 9.0, 10% activity at pH 5.0 and pH10.0
6.6 - 10.8
6.9 - 9.2
-
pH 6.9: about 50% of activity maximum, pH 9.2: about 83% of activity maximum
7 - 11
-
pH 7: about 13% of activity maximum, pH 11: 36% of activity maximum
7 - 9.5
-
pH 7: about 40% of activity maximum, pH 9.5: about 55% of activity maximum
7.3 - 8.8
-
pH 7.3: about 65% of activity maximum, pH 8.6: about 90% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
27
30
35
37
50
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 40
Achromobacter starkeyi
-
15°C: about 25% of activity maximum, 40°C: about 50% of activity maximum
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
glutathione reductase activity is significantly lower in leprosy as compared to the control group
-
mature kernel endosperm, 2 isoforms belonging to different developmental stages
-
doxorubicin-insensitive lung cancer cell line expressing the MRP multi-drug resistant protein
-
doxorubicin-insensitive leukemic cell line HL-60-R, a subclone of HL-60
-
i.e. cysticeri, recovered from peritoneal cavity of 6-8 months before inoculated female Balb/c mice
-
pancreas, lower expression level than in islet cells
-
doxorubicin-insensitive lung cancer cell line expressing the MRP multi-drug resistant protein
additional information
-
-
394708, 394714, 394723, 394724, 394725, 394726, 394727, 394728, 394729, 394761, 394776, 438075, 659592, 659698, 659860, 671910, 673458, 688050, 696556, 696681, 699224, 699241, 699619, 711008, 725616
-
tubule and cortex, developmental changes in enzyme activity from fetal prenatal over neonatal to adult stage, overview, gradual increase with maximum at adult age
-
the early decrease of glutathione reductase activity in leaves treated with polyamines can be due to a direct interaction of these compounds with the enzyme
-
glutathione reductase plays a key role in maintaining thiol groups in the lens, and its activity decreases with aging and cataract formation. The glutathione reductase activity in the cortex and nucleus of the cataractous lenses is significantly lower than that of the aged clear lenses. The highest activity in the cortex is observed in the clear aged lenses. The combination of thioredoxin and thioredoxin reductase revives the activity of glutathione reductase from both the cortex and nucleus of aged clear lenses. In cataract lenses (grade II and grade IV), there is a statistically significant recovery of glutathione reductase activity in the cortex, but not in the nucleus. No recovery is observed when thioredoxin or thioredoxin reductase are used separately. alpha-Crystallin successfully revives glutathione reductase activity in the cortex of cataract grade II lenses, but not in the nucleus. The combination of alpha-crystallin and thioredoxin/thioredoxin reductase gives a further increase of activity. Thioltransferase alone revives some of the glutathione reductase activity but together with the thioredoxin/thioredoxin reductase system gives no statistically significant enhancement of glutathione reductase activity; the combination of thioredioxin and thioredoxin reductase revives the activity of glutathione reductase from both the cortex and nucleus of aged clear lenses. In cataract lenses (grade II and grade IV) there is a statistically significant recovery of glutathione reductase activity in the cortex, but not in the nucleus. alpha-Crystallin successfully revives glutathione reductase activity in the cortex of cataract grade II lenses, but not in the nucleus. the combination of alpha-crystallin and thioredoxin/thioredoxin reductase gives a further increase in activity. Both disulfide bond formation and protein unfolding are responsible for glutathione inactivation
-
mainly in epithelium, low content in alveoli, developmental changes in enzyme activity from fetal prenatal over neonatal to adult stage, overview, substantially constant
HvGR2 is mainly expressed in root tissue. HvGR2 is upregulated in response to Fe-deficiency. Glutathione reductase is not post-transcriptionally regulated
-
TaGR2 is mainly expressed in root tissue. TaGR2 is upregulated in response to Fe-deficiency. Glutathione reductase is not post-transcriptionally regulated
HvGR1 is mainly expressed in shoot tissue. HvGR1 is upregulated in response to Fe-deficiency. Glutathione reductase is not post-transcriptionally regulated
-
TaGR1 is mainly expressed in shoot tissue. Expression of TaGR1 is not elevated in response to Fe-deficiency
-
at the site of mitochondrial sheath formation in elongating spermatids, absent in mature sperm
-
at the site of mitochondrial sheath formation in elongating spermatids, absent in mature sperm
additional information
-
stage-specific expression of the enzyme in life-cycle stages with different oxidation-reduction levels, glutathione levels, overview
additional information
stage-specific expression of the enzyme in life-cycle stages with different oxidation-reduction levels, glutathione levels, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
analysis of the overlapping targeting signals of dual-targeted enzyme, in vitro and in vivo import analysis, overview
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
47000
49300
2 * 50000, SDS-PAGE, 2 * 49300, MALDI-TOF mass spectrometry
50000
52000
53000
55000
56000
57000
58000
59000
60000
63000
64000
79000
90000
99800
-
Spirulina maxima, pore gradient gel electrophoresis, dimer, enzyme exists predominantly as tetrameric species in equilibrium with a minor dimer fraction
100000
104000
105000
107000
108000
-
ultracentrifugation in glycerol density gradient, dimer, enzyme can also be active also as monomer
110000
118000
120000
125000
177000
-
sedimentation equilibrium, tetramer, enzyme exists predominantly as a tetrameric species in equilibrium with a minor dimer fraction
40000
-
composed of two major proteins of 58000 and 40000 Da, SDS-PAGE
47000
-
2 * 47000, SDS-PAGE, enzyme exists predominantly as a tetrameric species in equilibrium with a minor dimer fraction; 4 * 47000, SDS-PAGE, enzyme exists predominantly as a tetrameric species in equilibrium with a minor dimer fraction
47000
one of two minor protein bands at 50000 and 47000 Da, SDS-PAGE
50000
2 * 50000, SDS-PAGE, 2 * 49300, MALDI-TOF mass spectrometry
50000
one of two minor protein bands at 50000 and 47000 Da, SDS-PAGE
56000
-
SDS-PAGE, gel filtration, monomer, enzyme can also be active as dimer
58000
-
composed of two major proteins of 58000 and 40000 Da, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
oligomer
tetramer
additional information
dimer
-
2 * 47000, SDS-PAGE, enzyme exists predominantly as a tetrameric species in equilibrium with a minor dimer fraction
dimer
2 * 50000, SDS-PAGE, 2 * 49300, MALDI-TOF mass spectrometry
dimer
-
determination of shape and electrostatics of the large helices-containing cavity at the dimer interface
homodimer
-
2 * 57100, calculated for GR1 including the N-terminal His-tag; 2 * 60000, SDS-PAGE
monomer
-
1 * 55000, bovine brain enzyme, SDS-PAGE, 1 * 52000, bovine erythrocyte and liver enzyme, SDS-PAGE
tetramer
-
4 * 47000, SDS-PAGE, enzyme exists predominantly as a tetrameric species in equilibrium with a minor dimer fraction
additional information
-
in absence of thiols the enzyme shows tendency to form aggregates
additional information
-
in absence of thiols, glutathione reductase shows a tendency to form tetramers and larger aggregates, catalytically active
additional information
-
human enzyme structure comparison with the enzyme from Plasmodium falciparum, human parasite, active site structure
additional information
-
enzyme is a fusion protein consisting of an N-terminal glutaredoxin domain and the thioredoxin reductase module
additional information
-
enzyme structure comparison with the human enzyme, active site structure
additional information
-
enzyme is a fusion protein consisting of an N-terminal glutaredoxin domain and the thioredoxin reductase module
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
glutathione reductase is not post-transcriptionally regulated; glutathione reductase is not post-transcriptionally regulated
additional information
glutathione reductase is not post-transcriptionally regulated; glutathione reductase is not post-transcriptionally regulated
additional information
-
dual-targeted enzyme contains overlapping targeting signals for import into mitochondria and chloroplasts
additional information
-
glutathione reductase is not post-transcriptionally regulated
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop method, form-S grown crystals from salt and form-P grown crystals from PEG-8000, X-ray analysis
-
molecular asymmetry of crystals from deionized water and from 2 M ammonium sulfate, exact 2fold molecular axis in the dimer, form A-D, three-dimensional structure
-
peroxynitrite inactivated enzyme, hanging drop vapour dffusion method, 10 mg/ml protein in 120 mM ammonium sulfate, 100 mM potassium phosphate, pH 7.5, against reservoir solution containing 720 mM ammonium sulfate, 100 mM potassium phosphate, pH 8.0, 30-37°C, 5 days, storage and handling in stabilization solution containing 1 M ammonium sulfate, 100 mM potassium phosphate, pH 8.0, X-ray structure determination and analysis at 1.9 A resolution
-
purified recombinant strain K1 wild-type enzyme, enzyme is dialyzed against EDTA for 3 h, hanging drop vapour diffusion method, protein solution contains 10 mg/ml protein, mixed with an equal volume of reservoir solution containing 14% w/v PEG monomethylether 550, 70 mM NaCl, 70 mM bicine, pH 8.7-9.0, 20°C, one week, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement
-
hanging drop method, crystal structure is determined at 2.40 A resolution
hanging drop vapor diffusion method, using 22% (w/v) PEG 3350, 0.1 M HEPES pH 7.2, 0.2 M NaNO3, 5 mM dithiothreitol, or beta-mercaptoethanol
-
hanging-drop method at 22°C, size of crystals varies with ammonium sulfate concentration
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
-
the enzyme remains stable in 100 mM Tris-HCl buffer between pH 6.5 and 10.0, the activity remains practically unchanged between pH 6.5-7.5 and decreases significantly only above pH 8.5
701146
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 4
-
there is no appreciable effect of freezing and thawing on enzyme activity for approximately 1 month
30 - 35
-
the abrupt decrease in activity observed at temperatures higher than 35°C, can be associated with loss of enzyme stability beyond 30°C
42.5
-
complete loss of activity above 42°C, 10 min in presence of NADPH
45
50
55
60
65
70
75
80
-
NADP+, GSSG, glutathione and dichloroindophenol protect against thermal inactivation at 80°C
additional information
45
-
irreversible denaturation above, complete loss of activity after 40 min
additional information
-
root enzyme more stable than chloroplast enzyme, oxidized form more stable than reduced form
additional information
-
resistant to high temperatures and very resistant to low temperatures
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
active in the presence of imidazole up to 0.8 M, the native enzyme is resistant to digestion by trypsin or chymotrypsin
-
complete inactivation after incubation with NADH, reversible by addition of GSSG
-
complete inactivation after incubation with NADPH, reversible by addition of GSSG
concentrated solution, stable for years
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
freezing denaturates
NADP+ stabilizes
pure enzyme heated in presence of bovine serum albumin and 0.020 mM NADPH: loss of activity beyond 30°C, significant reduction even at 0°C
-
repeated freezing and thawing, inactivation
repeated freezing and thawing, stable
urea, quite stable to
complete inactivation after incubation with NADPH, reversible by addition of GSSG
-
complete inactivation after incubation with NADPH, reversible by addition of GSSG
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
crystals and amorphous protein obtained by precipitation with ammonium sulfate are stable
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen promotes enzyme aggregation by oxidation of thiols, that prevent oxidation of the enzyme
-
394725
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 6.8, 0.05 M potassium phosphate buffer, indefinitely stable
-
0-4°C, 1 month, no appreciable effect of freezing and thawing on enzyme activity
-
4°C, 50 mM potassium phosphate, pH 7.4, 50% loss of activity after 10 days
-
4°C, activation after storage over days, months or years
4°C, concentrated purified enzyme, 0.05% NaN3, 50 mM potassium phosphate, pH 7.4, 2 mM EDTA, 150 mM NaCl, 2 mM glutathione, quite stable
-
4°C, pH 7.5, 50 mM sodium phosphate buffer, 1 mM 2-mercaptoethanol, 1 mM EDTA
-
4°C, pure enzyme without stabilizers such as glycerol, 8 days, 25% loss of activity
-
concentrated solution, years
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1714fold from liver homogenate, by ammonium sulfate fractionation, affinity chromatography, and gel filtration
-
2',5'-ADP Sepharose 4B affinity chromatography and DEAE Sepharose column chromatography
-
31250fold from erythrocyte hemolysate, by ammonium sulfate fractionation, affinity chromatography, and gel filtration
-
5342fold to homogeneity from erythrocytes by hemolysis, ammonium sulfate fractionation, affinity chromatography, and gel filtration
-
647fold to homogeneity from metacystodes by ammonium sulfate fractionation, ion exchange chromatography, affinity chromatography, and gel filtration
-
ammonium sulfate fractionation, 2',5'-ADP Sepharose 4B affinity chromatography and Sephadex G-200 gel filtration
ammonium sulfate precipitation, 2 ',5'-ADP Sepharose-4B affinity column chromatography and Sephadex G-200 gel filtration
-
ammonium sulfate precipitation, 2',5'-ADP Sepharose 4B column chromatography and Sephadex G-200 gel filtration
-
ammonium sulfate precipitation, 2‘‘,5‘-ADP Sepharose 4B affinity column chromatography, and Sephadex G-200 gel filtration
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Blue-A Sepharose column chromatography, and 2',5'-ADP-Sepharose column chromatography
-
ammonium sulfate precipitation, ultrafiltration, CM-Sepharose column chromatography, DEAE-Sepharose column chromatography, GSH–Sepharose affinity column chromatography, and ADP-Sepharose affinity chromatography
-
heat-denaturation and Sephadex G25 gel filtration, 2',5'-ADP agarose 4B column chromatography, and PBE94 column chromatography
-
ion exchange chromatography on hydroxylapatite, LKB 8101 isoelectrofocusing column chromatography, Sephacryl S-300 column gel filtration and Matrix Red dye ligand chromatography
-
Mono Q HR 5/5 column chromatography and 2'5'-ADP Sepharose 4B affinity chromatography
-
native enzyme from microplasmodia, 968fold in a multistep procedure
nickel affinity column chromatography
partially
recombinant His-tagged enzyme from in-vitro expression by nickel chelate affinity chromatography
-
ammonium sulfate fractionation, 2',5'-ADP Sepharose 4B affinity chromatography and Sephadex G-200 gel filtration
-
ammonium sulfate fractionation, 2',5'-ADP Sepharose 4B affinity chromatography and Sephadex G-200 gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of a genetic library, DNA and amino acid sequence determination and analysis of the enzyme encoding gene, expression in Escherichia coli
DNA sequence determination, genomic structure
expressed in Escherichia coli BL21(DE3) cells
expression of strain K1 wild-type and mutant enzymes in Escherichia coli
-
mutant enzyme glutathione reductase-trypanothine reductase, expression in Escherichia coli
-
overexpression of Saccharomyces cerevisiae Glr1 in Pichia pastoris GS115
transient expression of the enzyme's targeting signal sequence fused to the green fluorescent protein, as well as GFP-holoenzyme fusion protein, targets to the chloroplasts only
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after treatment with methyl viologen for two weeks, there is a significant increase in the glutathione reductase activity in both wild type and transgenic plants and such an increase is greater in transgenic plants than in wild type plants
expression of isoform GR3 is induced by salt stress (35fold in shoots at 200 mM NaCl, 6fold in roots by 100 mM NaCl). In addition, the transcript level of isoform GR3 is greatly increased with salicylic acid treatment (0.1-0.2 mM)
glutathione reductase activity is generally higher in the rag2 mutant than in the wild type strain, either under hypoxic or aerobic conditions; the treatment with menadione, H2O2, or tert-butyl hydroperoxide does not increase significantly glutathione reductase activity in the wild type strain
hepatic glutathione reductase activity is significantly increased on days 4 and 10 after injection of DL-ethionine (12.5 mg/kg)
-
the expression of isoforms GR2 and GR3 but not GR1 is increased in rice roots treated with NaCl, Na+ but not Cl- or osmotic stress is involved in NaCl-induced expression of glutathione reductase in roots of rice seedlings, after 8 h treatment with NaCl (150, 200, and 300 mM), isoform GR3 expression is specifically increased, the expression of isofomr GR2 is also increased by 150 and 200 mM NaCl but not 300 mM NaCl, no significant increase due to NaCl (150, 200, and 300 mM) can be detected in the expression of isoform GR1
-
the transcript level of isoform GR3 is not significantly affected by methyl jasmonate, dehydration or heat shock stress
zinc exposure (0.01, 0.03, and 0.1 mM Zn2+ for a period of 48 h) causes a concentration-dependent reduction in glutathione reductase activity in gills, liver and brain
-
glutathione reductase activity is generally higher in the rag2 mutant than in the wild type strain, either under hypoxic or aerobic conditions; the treatment with menadione, H2O2, or tert-butyl hydroperoxide does not increase significantly glutathione reductase activity in the wild type strain
-
glutathione reductase activity is generally higher in the rag2 mutant than in the wild type strain, either under hypoxic or aerobic conditions; the treatment with menadione, H2O2, or tert-butyl hydroperoxide does not increase significantly glutathione reductase activity in the wild type strain
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A18E//N21W/R22N/N101D/K105D/R319A
-
mutant enzyme shows very little activity with GSSG in micromolar range but, on increasing the GSSG concentration to 20 mM some activity with GSSG can be detected. 1.5fold decrease in turnover-number for trypanothione, 9.5fold decrease in KM-value for trypanothione
A18E/N21W/R22N
-
mutant enzyme shows very little activity with GSSG in micromolar range but, on increasing the GSSG concentration to 20 mM some activity with GSSG can be detected. 1.6fold increase in turnover-number for trypanothione, 3fold decrease in KM-value for trypanothione
A18E/N21W/R22N/N101D/K105D
-
mutant enzyme shows very little activity with GSSG in micromolar range but, on increasing the GSSG concentration to 20 mM some activity with GSSG can be detected. 1.5fold increase in turnover-number for trypanothione, 6.7fold decrease in KM-value for trypanothione
N101D/K105D
-
about 2fold increase in KM-value for GSSG, 1.2fold decrease in turnover-number. 1.6fold decrease in turnover-number for trypanothione, 1.15fold increase in KM-value for trypanothione
N21R
-
1.6fold increase in KM-value for GSSG, 1.4fold decrease in turnover-number for GSSG, 1.2fold decrease in turnover-number for trypanothione, 2.3fold increase in turnover number for trypanothione
A34E/R37W
-
glutathione reductase mutant, activity switches to trypanothione reductase, termed GRTR, 700fold more activity with trypanothione than with glutathione
Y114L
additional information
Y114L
-
site-directed mutagenesis, mutant is insensitive to inactivation by peroxynitrite in contrast to the wild-type enzyme
Y114L
-
site-directed mutagenesis, mutant is insensitive to inactivation by peroxynitrite in contratst to the wild-type enzyme
additional information
-
introduction of silent random mutations in 5'-region to generate a His-tagged high-level expression clone
additional information
-
a mutant lacking a loop involved in ligand binding, showing reduced activity, and a mutant with a modified loop, which is more efficient with NADPH and NADH
additional information
-
cell-free enzyme synthesis, 71% of which is soluble, the enzyme is dimeric, requires FAD as a cofactor, and is more active than the native enzyme
additional information
-
analysis of enzyme import rates into chloroplasts of diverse point mutated pea strains, overview
additional information
-
construction of a deletion mutant lacking residues 317-349 forms a dimeric FAD-free apoenzyme
additional information
N278 at the vicinity of NADP-binding pocket is artificially glycosylated when heterogeneously overexpressed in Pichia pastoris. The highly motile oligosaccharide chain linked to N278 of the recombinant Glr1 interferes with the entry of NADPH, wich results in a dramatic increase of Km for NAPDH and a significant decrease of turnover number, when compared with the native protein
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding after treatment with 6 M urea, recovering of full activity
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
-
enzyme is a target for enzyme inhibitor and antimalarial drug development
medicine
-
mimicking of favism by inhibiting the enzyme with specific inhibitors to protect against malaria; potential target of antimalarial and cytostatic agents
medicine
-
antimalarial dual drugs based on potent inhibitors of glutathione reductase from Plasmodium falciparum
LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.7)
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