1.8.1.7: glutathione-disulfide reductase
This is an abbreviated version!
For detailed information about glutathione-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.7
-
1.8.1.7
-
dismutase
-
catalase
-
sod
-
malondialdehyde
-
ascorbate
-
s-transferase
-
gst
-
glutathione-s-transferase
-
erythrocyte
-
glucose-6-phosphate
-
wistar
-
thiobarbituric
-
gsh-px
-
tbars
-
necrosis
-
selenium
-
dehydroascorbate
-
anti-oxidant
-
hydroperoxide
-
cadmium
-
albino
-
hepatoprotective
-
hepatotoxicity
-
riboflavin
-
non-enzymatic
-
seedling
-
gill
-
chlorophyll
-
dt-diaphorase
-
cumene
-
medicine
-
selenium-dependent
-
lipoperoxidation
-
sulfoximine
-
glyoxalase
-
gamma-glutamyl
-
alpha-tocopherol
-
transpeptidase
-
pro-oxidant
-
cuznsod
-
dienes
-
trypanothione
-
glutaredoxins
-
glutathione-dependent
-
guaiacol
-
buthionine
-
1.15.1.1
-
acid-reactive
-
mn-sod
-
pharmacology
-
lipoamide
-
gamma-glutamylcysteine
- 1.8.1.7
- dismutase
- catalase
- sod
- malondialdehyde
- ascorbate
- s-transferase
- gst
- glutathione-s-transferase
- erythrocyte
- glucose-6-phosphate
- wistar
-
thiobarbituric
- gsh-px
-
tbars
- necrosis
- selenium
- dehydroascorbate
-
anti-oxidant
- hydroperoxide
- cadmium
-
albino
-
hepatoprotective
-
hepatotoxicity
- riboflavin
-
non-enzymatic
- seedling
- gill
- chlorophyll
- dt-diaphorase
- cumene
- medicine
-
selenium-dependent
-
lipoperoxidation
- sulfoximine
- glyoxalase
-
gamma-glutamyl
- alpha-tocopherol
- transpeptidase
-
pro-oxidant
-
cuznsod
-
dienes
- trypanothione
- glutaredoxins
-
glutathione-dependent
- guaiacol
-
buthionine
-
1.15.1.1
-
acid-reactive
- mn-sod
- pharmacology
- lipoamide
- gamma-glutamylcysteine
Reaction
2 glutathione
+
Synonyms
At3g54660, EC 1.6.4.2, GLR, glutahione reductase, glutathione disulfide reductase, glutathione reductase, glutathione reductase (NADPH), glutathione reductase 3, glutathione reductase Glr1, glutathione S-reductase, glutathione: NADP(+) oxidoreductase, glutathione: NADP+ oxidoreductase, glutathione:NADP+ oxidoreductase, Gor, GOR1, GOR2, GR, GR1, GR2, Gr3, GRase, GRase-1, GRd, GSH reductase, GSHR, Gsr, GSR-1, GSSG reductase, HCOI_01258400, hGR, HvGR1, HvGR2, multifunctional thioredoxin-glutathione reductase, NADPH-glutathione reductase, NADPH-GSSG reductase, NADPH-reduced GR, NADPH: oxidized glutathione oxidoreductase, NADPH:oxidized glutathione oxidoreductase, NADPH:oxidized-glutathione oxidoreductase, OBP29, PfGR, psgr, PtGR1.1, PtGR1.2, PtGR2, reductase, glutathione, SpGR, TaGR1, TaGR2, TGR, thioredoxin glutathione reductase, thioredoxin/glutathione reductase, TrxR3
ECTree
1.8.1.7 glutathione-disulfide reductaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 1.8.1.7 - glutathione-disulfide reductase
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INHIBITOR 
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
bis[1,3,5-triazino[1,2-a]benzimidazole-2-amine,3,4-dihydro-4-(2-imidazole)]copper(II) bromide
-
bis[1,3,5-triazino[1,2-a]benzimidazole-2-amine,3,4-dihydro-4-(2-thiophene)]copper(II) bromide
-
catechin
-
slightly, catechin, non-competitive with both NADPH and GSSG, influence on glutathione recognition
chloro[N(4)-ortho-chlorophenyl-2-acetylpyridinethiosemicarbazonato]gold(III)dichloroaurate(I)
-
in addition, the complex is highly cytotoxic to MCF-7 and HT29 cells
chrysin
-
slightly, flavonone, non-competitive with both NADPH and GSSG, influence on glutathione recognition
Cu+
-
presence of Cu+ inhibits noncompetitively with respect to the substrate GSSG and NADPH and inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase
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
H2O2
-
inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase
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
hypericin
when is glutathione disulfide is the variable substrate, hypericin inhibits the enzyme competitively
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
methylene blue
impairs the activity of recombinant form of the enzyme
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
N,N-dimethyl-3-[2-(trifluoromethyl)-10H-phenothiazin-10-yl]propan-1-aminium
-
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)-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
Cu2+
-
presence of Cu2+ inhibits noncompetitively with respect to the substrate GSSG and NADPH and inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase. Copper binds to sites apart from the substrate sites, causing the peptide cleavage by hydroxyl radical
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
-
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
-
