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1,4-naphthoquinone + NADPH + H+
?
-
-
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
2-Cys peroxiredoxin + NADH
?
-
NADH is a poor electron donor for NTRC activity
-
-
?
2-Cys peroxiredoxin + NADPH
?
-
NTRC is able to conjugate NADPH thioredoxin reductase and thioredoxin activities for the efficient reduction of 2-Cys peroxiredoxin
-
-
?
2-Cys peroxiredoxin A + NADPH
?
-
-
-
-
?
2-Cys peroxiredoxin A + NADPH + H+
2-Cys peroxiredoxin A disulfide + NADP+
-
-
-
-
?
2-Cys peroxiredoxin B + NADPH
?
-
-
-
-
?
2-Cys peroxiredoxin B + NADPH + H+
2-Cys peroxiredoxin B disulfide + NADP+
-
-
-
-
?
4,4'-bischloro-diphenyl diselenide + NADPH + H+
?
-
-
-
-
?
4,4'-bismethoxy-diphenyl diselenide + NADPH + H+
?
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol
2-nitro-5-thiobenzoate + oxidized dithiothreitol
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoicacid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
?
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
?
-
-
-
?
alloxan + NADPH + H+
? + NADP+
-
-
-
-
?
Arabidopsis thaliana thioredoxin 3 + NADP+
Arabidopsis thaliana thioredoxin 3 disulfide + NADPH + H+
Babesia bovis thioredoxin + NADP+
Babesia bovis thioredoxin disulfide + NADPH + H+
-
-
-
?
BAS1 + hydrogen peroxide
?
-
-
-
?
benzyl viologen + NADH + H+
?
benzyl viologen + NADPH + H+
?
-
-
-
-
?
bis-gamma-glutamyl cystine + NADPH + H+
gamma-glutamyl cystine + NADP+
BrxA bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxA + NADP+
BrxB bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxB + NADP+
BrxC bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxC + NADP+
chaetocin + NADPH + H+
?
-
competitive and selective substrate for TrxR1
-
-
?
chetomin + NADPH + H+
?
-
-
-
-
?
CHLI-1 ATPase + NADPH + H+
CHLI-1 ATPase disulfide + NADP+
-
-
-
?
cystine + NADPH + H+
2 cysteine + NADP+
-
-
-
?
cytochrome c + NADPH
reduced cytochrome c + NADP+
-
-
-
?
diphenyl diselenide + NADPH + H+
?
-
-
-
-
?
disulfide oxidase + NADPH + H+
?
-
-
-
?
dithionitrobenzene + NADPH + H+
?
-
-
-
-
?
ebselen + NADPH + H+
? + NADP+
-
-
-
-
?
ebsulfur + NADP+
ebsulfur disulfide + NADPH + H+
-
-
-
-
?
ebsulfur disulfide + NADPH + H+
ebsulfur + NADP+
-
-
-
-
r
Entamoeba histolytica thioredoxin disulfide 41 + NADPH + H+
Entamoeba histolytica thioredoxin 41 + NADP+
-
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
Escherichia coli thioredoxin disulfide + NADPH + H+
Escherichia coli thioredoxin + NADP+
-
-
-
-
?
gliotoxin + NADPH + H+
?
-
-
-
-
?
glutaredoxin 4 + NADPH
?
-
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
Hordeum vulgare thioredoxin 1 + NADP+
Hordeum vulgare thioredoxin 1 disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 + NADP+
Hordeum vulgare thioredoxin 2 disulfide + NADPH + H+
Hordeum vulgare thioredoxin 2 mutant E86A + NADP+
Hordeum vulgare thioredoxin 2 mutant E86A disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant G47P + NADP+
Hordeum vulgare thioredoxin 2 mutant G47P disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant G57P + NADP+
Hordeum vulgare thioredoxin 2 mutant G57P disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant I51G + NADP+
Hordeum vulgare thioredoxin 2 mutant I51G disulfide + NADPH + H+
Hordeum vulgare thioredoxin disulfide h1 + NADPH + H+
Hordeum vulgare thioredoxin h1 + NADP+
-
-
-
-
r
Hordeum vulgare thioredoxin disulfide h2 + NADPH + H+
Hordeum vulgare thioredoxin h2 + NADP+
-
-
-
-
r
human thioredoxin + NADP+
human thioredoxin disulfide + NADPH + H+
-
-
-
-
r
insulin + NADPH + H+
? + NADP+
L-cysteine + NADPH
L-cystine + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(2-amino-2-oxoethyl)carbamoyl]-6-oxo-1,2,5-dithiazocan-7-] + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-L-cysteinylglycinamide + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(2-amino-2-oxoethyl)carbamoyl]-6-oxo-1,2,5-thiaselenazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-3-selanyl-L-alanylglycinamide + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(carboxymethyl)carbamoyl]-6-oxo-1,2,5-dithiazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-L-cysteinylglycine + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(carboxymethyl)carbamoyl]-6-oxo-1,2,5-thiaselenazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-3-selanyl-L-alanylglycine + NADP+
-
-
-
-
?
lipoamide + NADPH + H+
?
-
isoform TrxR2 displays strikingly lower activity with lipoamide compared to isoform TrxR1
-
-
?
lipoamide + NADPH + H+
dihydrolipoamide + NADP+
-
-
-
?
lipoamide disulfide + NADPH + H+
lipoamide + NADP+
-
-
-
?
lipoic acid + NADPH + H+
?
methaneseleninic acid + NADP+
? + NADPH + H+
-
-
-
-
?
methylseleninate + H2O2
?
methylseleninate + NADPH
CH3SeH + NADP+
-
also utilizes glutathione instead of NADPH
-
ir
NADH + ubiquinone-10
NAD+ + ubiquinol-10
NADPH + H+ + ubiquinone-10
NADP+ + ubiquinol-10
NADPH + thioredoxin disulfide
NADP+ + thioredoxin
-
mechanism, Cys57 attacks Cys490 in the interchange reaction between the N-terminal dithiol and the C-terminal disulfide
-
-
?
oxidized bacillithiol disulfide + NADH + H+
reduced bacillithiol disulfide + NAD+
oxidized bacillithiol disulfide + NADPH + H+
reduced bacillithiol disulfide + NADP+
oxidized lipoamide + NADPH
lipoamide disulfide + NADP+
-
-
-
-
?
oxidized lipoate + NADPH
?
paraquat + NAD(P)H
paraquat radical + NAD(P)+
-
-
-
-
r
paraquat radical + O2
paraquat + O2-
-
-
-
-
r
peroxiredoxin + NADPH + H+
peroxiredoxin disulfide + NADP+
-
-
-
?
Pro-Thr-Val-Thr-Gly-Cys-S-S-Cys-Gly + NADPH + H+
Pro-Thr-Val-Thr-Gly-Cys + Cys-Gly + NADP+
-
-
-
-
?
Pro-Thr-Val-Thr-Gly-Cys-S-S-selenoCys-Gly + NADPH + H+
Pro-Thr-Val-Thr-Gly-Cys + selenoCys-Gly + NADP+
-
-
-
-
?
protein disulfide isomerase + NADPH
protein disulfide isomerase + NADP+
-
-
protein disulfide isomerase with reduced disulfides
r
protein disulfide isomerase + NADPH + H+
?
-
-
-
-
r
protein disulfide isomerase like protein 1 + NADPH
protein disulfide isomerase like protein 1 + NADP+
-
protein disulfide isomerase like protein 1 from rat liver containing a thioredoxin domain
protein disulfide isomerase like protein 1 with reduced disulfides, coupled assay with insulin
?
protein disulfide isomerase like protein 2 + NADPH
protein disulfide isomerase like protein 2 + NADP+
-
protein disulfide isomerase like protein 2 from rat liver containing a thioredoxin domain
protein disulfide isomerase like protein 2 with reduced disulfides, coupled assay with insulin
?
protein-disulfide + NADH + H+
protein-dithiol + NAD+
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
rat thioredoxin + NADP+
rat thioredoxin disulfide + NADPH + H+
-
-
-
-
r
reduced tissue factor + NADP+
tissue factor + NADPH + H+
-
-
-
r
S-nitrosoglutathione + NADPH + H+
? + NADP+
-
-
-
-
?
seleninate + NADPH
?
-
-
-
-
?
selenite + NADPH
? + NADP+
-
-
-
?
selenite + NADPH + H+
? + NADP+
selenite + NADPH + H2O
Se2- + NADP+ + ?
-
-
-
-
?
selenocysteine + NADPH
selenocystine + NADP+
sodium selenite + NADPH + H+
? + NADP+
-
-
-
-
?
thioredoxin + 3-acetylpyridine adenine dinucleotide
thioredoxin disulfide + reduced 3-acetylpyridine adenine dinucleotide
-
wild-type enzyme, mutant enzyme C135S and thioredoxin in subunit complex C135-C32S with the enzyme
-
?
thioredoxin + insulin disulfide
thioredoxin disulfide + insulin
thioredixin is the native principal substrate of TrxR1
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
thioredoxin + tert-butyl-hydroperoxide
?
-
in presence of methylseleninate, coupled assay
-
-
?
thioredoxin 1 + NADP+
thioredoxin 1 disulfide + NADPH + H+
-
TrxR2 prefers its endogenous substrate thioredocin 2 over thioredoxin 1 (10fold), whereas isoform TrxR1 efficiently reduces both thioredoxin 1 and thioredoxin 2
-
-
?
thioredoxin 1 + NADP+ +
thioredoxin 1 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin 2 + NADP+
thioredoxin 2 disulfide + NADPH + H+
thioredoxin 3 + NADP+
thioredoxin 3 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin 41 + NADP+
thioredoxin 41 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin 8 + NADP+
thioredoxin 8 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin C-2 + NADP+
thioredoxin C-2 disulfide + NADPH + H+
-
-
-
-
r
thioredoxin disulfide + H2
thioredoxin
-
-
-
?
thioredoxin disulfide + insulin
thioredoxin + insulin disulfide
thioredoxin disulfide + NADH + H+
thioredoxin + NAD+
thioredoxin disulfide + NADPH
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
thioredoxin disulfide 41 + NADPH + H+
thioredoxin 41 + NADP+
-
-
-
-
?
thioredoxin disulfide 8 + NADPH + H+
thioredoxin 8 + NADP+
-
-
-
-
?
thioredoxin disulfide h + NADH
thioredoxin + NAD+
-
-
-
?
thioredoxin disulfide h + NADPH
thioredoxin + NADP+
-
-
-
?
thioredoxin K36E + NADP+
thioredoxin K36E disulfide + NADPH + H+
-
-
-
-
r
thioredoxin K36R + NADP+
thioredoxin K36R disulfide + NADPH + H+
-
-
-
-
r
thioredoxin P34S + NADP+
thioredoxin P34S disulfide + NADPH + H+
-
-
-
-
r
thioredoxin-1 disulfide + NADPH
NADP+ + thioredoxin-1
-
-
-
-
?
thioredoxin-1 disulfide + NADPH + H+
thioredoxin-1 + NADP+
-
-
-
-
r
thioredoxin-CAC + NADP+
thioredoxin-CAC disulfide + NADPH + H+
-
-
-
-
r
thioredoxin-II + NADP+
thioredoxin-II disulfide + NADPH + H+
-
-
-
-
r
thioredoxin-R + NADP+
thioredoxin-R disulfide + NADPH + H+
-
-
-
-
r
tissue factor + NADPH + H+
reduced tissue factor + NADP+
-
-
-
r
[redox protein PhRP]-disulfide + NADH + H+
[redox protein PhRP]-dithiol + NAD+
[redox protein PhRP]-disulfide + NADPH + H+
[redox protein PhRP]-dithiol + NADP+
[thioredoxin reductase from Escherichia coli]-disulfide + NADH + H+
[thioredoxin reductase from Escherichia coli]-dithiol + NAD+
-
-
-
?
[thioredoxin reductase from Escherichia coli]-disulfide + NADPH + H+
[thioredoxin reductase from Escherichia coli]-dithiol + NADP+
-
-
-
?
additional information
?
-
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol
2-nitro-5-thiobenzoate + oxidized dithiothreitol
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol
2-nitro-5-thiobenzoate + oxidized dithiothreitol
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
native thioredoxin-thioredoxin reductase fusion protein
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
C-terminal tetrapeptide sequences is Gly-Cys-Sec-Gly. Changing the C-terminal carboxylate of mTR3 to a carboxamide increases the activity of the enzyme. If the selenium content is normalized for both samples, the carboxamide mutant has nearly twice the activity as the semisynthetic wild-type carboxylate enzyme
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
isoform TrxR2 displays strikingly lower activity with 5,5'-dithiobis(2-nitrobenzoic acid) compared to isoform TrxR1
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
alloxan + NADPH
?
-
-
-
-
?
alloxan + NADPH
?
-
-
-
-
?
alloxan + NADPH
?
-
-
-
-
?
alloxan + NADPH
?
-
-
-
-
?
Arabidopsis thaliana thioredoxin 3 + NADP+
Arabidopsis thaliana thioredoxin 3 disulfide + NADPH + H+
-
-
-
?
Arabidopsis thaliana thioredoxin 3 + NADP+
Arabidopsis thaliana thioredoxin 3 disulfide + NADPH + H+
-
-
-
?
benzyl viologen + NADH + H+
?
-
-
-
-
?
benzyl viologen + NADH + H+
?
-
-
-
-
?
bis-gamma-glutamyl cystine + NADPH + H+
gamma-glutamyl cystine + NADP+
-
-
-
?
bis-gamma-glutamyl cystine + NADPH + H+
gamma-glutamyl cystine + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
BrxA bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxA + NADP+
-
-
-
?
BrxA bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxA + NADP+
-
-
-
?
BrxB bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxB + NADP+
-
-
-
?
BrxB bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxB + NADP+
-
-
-
?
BrxC bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxC + NADP+
-
-
-
?
BrxC bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxC + NADP+
-
-
-
?
dithiothreitol + NADPH
?
-
no activity
-
-
?
dithiothreitol + NADPH
?
-
-
-
-
?
dithiothreitol + NADPH
?
-
-
-
-
?
dithiothreitol + NADPH
?
-
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
GSSG + NADPH
GSH + NADP+
-
no activity
-
-
?
GSSG + NADPH
GSH + NADP+
-
-
-
-
?
GSSG + NADPH
GSH + NADP+
-
in presence of methylselenol
-
-
r
GSSG + NADPH
GSH + NADP+
-
-
-
-
?
Hordeum vulgare thioredoxin 2 + NADP+
Hordeum vulgare thioredoxin 2 disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 + NADP+
Hordeum vulgare thioredoxin 2 disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant I51G + NADP+
Hordeum vulgare thioredoxin 2 mutant I51G disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant I51G + NADP+
Hordeum vulgare thioredoxin 2 mutant I51G disulfide + NADPH + H+
-
-
-
?
insulin + NADPH + H+
? + NADP+
-
-
-
-
?
insulin + NADPH + H+
? + NADP+
-
-
-
-
?
juglone + NADPH + H+
?
-
-
-
-
?
juglone + NADPH + H+
?
-
isoform TrxR2 displays strikingly lower activity with juglone compared to isoform TrxR1
-
-
?
juglone + NADPH + H+
?
-
-
-
-
?
lipoic acid + NADPH + H+
?
-
substrate for isoform TrxR1
-
-
?
lipoic acid + NADPH + H+
?
-
-
-
-
?
menadione + NADPH
?
-
-
-
-
?
menadione + NADPH
?
-
-
-
-
?
methylseleninate + H2O2
?
-
-
-
-
?
methylseleninate + H2O2
?
-
in presence of methylseleninate
-
-
?
methylseleninate + H2O2
?
-
-
-
-
?
methylseleninate + H2O2
?
-
-
-
-
?
methylseleninate + H2O2
?
-
addition of selenocysteine increases the activity by 20%
-
-
?
methylseleninate + H2O2
?
-
only wild-type enzyme
-
-
?
NADH + ubiquinone-10
NAD+ + ubiquinol-10
-
-
-
-
?
NADH + ubiquinone-10
NAD+ + ubiquinol-10
-
-
-
-
?
NADH + ubiquinone-10
NAD+ + ubiquinol-10
-
-
-
-
?
NADPH + H+ + ubiquinone-10
NADP+ + ubiquinol-10
-
-
-
-
?
NADPH + H+ + ubiquinone-10
NADP+ + ubiquinol-10
-
-
-
-
?
NADPH + H+ + ubiquinone-10
NADP+ + ubiquinol-10
-
HEK cells overexpressing TrxR1 reduce ubiquinone-10
-
-
?
NADPH + H+ + ubiquinone-10
NADP+ + ubiquinol-10
-
-
-
-
?
oxidized bacillithiol disulfide + NADH + H+
reduced bacillithiol disulfide + NAD+
-
-
-
r
oxidized bacillithiol disulfide + NADH + H+
reduced bacillithiol disulfide + NAD+
-
-
-
r
oxidized bacillithiol disulfide + NADH + H+
reduced bacillithiol disulfide + NAD+
-
-
-
r
oxidized bacillithiol disulfide + NADPH + H+
reduced bacillithiol disulfide + NADP+
-
-
-
r
oxidized bacillithiol disulfide + NADPH + H+
reduced bacillithiol disulfide + NADP+
-
-
-
r
oxidized bacillithiol disulfide + NADPH + H+
reduced bacillithiol disulfide + NADP+
-
-
-
r
oxidized lipoate + NADPH
?
-
no activity with DL-alpha-lipoate
-
-
?
oxidized lipoate + NADPH
?
-
-
-
-
?
protein-disulfide + NADH + H+
protein-dithiol + NAD+
reduction activity for the disulfides in bovine insulin
-
-
?
protein-disulfide + NADH + H+
protein-dithiol + NAD+
reduction activity for the disulfides in bovine insulin
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
the enzyme is involved in a thioredoxin like system with thioredoxin reductase (PH1426). The redox potential of the redox protein is similar to that of thioredoxin from Escherichia coli and lower than that of glutathione
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
reduction activity for the disulfides in bovine insulin
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
the enzyme is involved in a thioredoxin like system with thioredoxin reductase (PH1426). The redox potential of the redox protein is similar to that of thioredoxin from Escherichia coli and lower than that of glutathione
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
reduction activity for the disulfides in bovine insulin
-
-
?
selenite + NADPH + H+
? + NADP+
-
-
-
-
?
selenite + NADPH + H+
? + NADP+
-
-
-
-
?
selenocysteine + NADPH
selenocystine + NADP+
-
-
-
-
?
selenocysteine + NADPH
selenocystine + NADP+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
radical reduction, prevention of cells from UV-generated free radical caused damage on the skin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with ribonucleotide reductase or methionine sulfoxide reductase from E. coli, thioredoxin-2
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
defense against oxidative stress
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
wide variety of electron acceptors
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
NADH in the standard assay, wild-type and chimeric mutants with and without amino acid exchanges
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
substrate e.g. thioredoxin disulfide from phage T4
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
metabolic function of thioredoxin reductase-thioredoxin system: supplies reducing equivalents for a wide variety of acceptors, e.g. : ribonucleotide reductase, nonspecific protein disulfide reductase, methionine sulfoxide reductase, D-proline reductase
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with nitroxide reductase
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with adenosine 3'-phosphate 5'-phosphosulfate reductase
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
radical reduction, prevention of cells from UV-generated free radical caused damage on the skin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
major anti-oxidant in keratinocytes, melanocytes, melanoma cells
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
reduction of free radicals at the surface of the epidermis, enzyme may play a role in physiology of pancreatic beta-cells
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
native thioredoxin-thioredoxin reductase fusion protein
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
detoxification of hydrogen peroxide, protection of the cell against oxidative damage
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with dithiothreitol
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
no activity
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
the enzyme forms a redox system with protein-disulfide oxidoreductase PhRP (PH0178)
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
the enzyme forms a redox system with protein-disulfide oxidoreductase PhRP (PH0178)
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
Thermosynechococcus vestitus
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
in presence of NADPH, coupled assay
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
i.e. DTNB
-
-
?
thioredoxin 2 + NADP+
thioredoxin 2 disulfide + NADPH + H+
-
TrxR2 prefers its endogenous substrate thioredocin 2 over thioredoxin 1 (10fold), whereas isoform TrxR1 efficiently reduces both thioredoxin 1 and thioredoxin 2
-
-
?
thioredoxin 2 + NADP+
thioredoxin 2 disulfide + NADPH + H+
-
-
-
-
?
thioredoxin disulfide + insulin
thioredoxin + insulin disulfide
-
-
-
?
thioredoxin disulfide + insulin
thioredoxin + insulin disulfide
-
-
-
-
?
thioredoxin disulfide + NADH + H+
thioredoxin + NAD+
-
-
-
-
?
thioredoxin disulfide + NADH + H+
thioredoxin + NAD+
-
-
-
-
?
thioredoxin disulfide + NADH + H+
thioredoxin + NAD+
-
-
-
r
thioredoxin disulfide + NADH + H+
thioredoxin + NAD+
MtNTRC can use either NADPH or NADH as cofactors
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
thioredoxin-1 from Anopheles gambiae or Plasmodium falciparum, thioredoxin-2 from Drosophila melanogaster
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
?
-
-
-
?
thioredoxin disulfide + NADPH + H+
?
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
?
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
?
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
?
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
r
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2. This process is consistent with the corresponding redox potentials and is essential for GSSG/GSH cycling in Drosophila melanogaster, which is deficient in glutathione reductase
-
-
r
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
DmTrxR catalyzes the reversible transfer of reducing equivalents from NADPH to DmTrx-2
-
-
r
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
the tandem system involving thioredoxin reductase and thioredoxin proves to be operative for reducing low molecular weight disulfides, including putative physiological substrates as cystine and oxidized trypanothione
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
the active site of Escherichia coli thioredoxin reductase contains a CATC motif without any selenocysteine and it specifically reduces oxidized Escherichia coli thioredoxin
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
r
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
the enzyme (TrxR) can use NADPH to reduce thioredoxin disulfide which passes the reducing equivalent to its downstream substrates involved in various biomedical events, such as ribonucleotide reductase for deoxyribonucleotide and DNA synthesis, or peroxiredoxins for counteracting oxidative stress
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
ebselen is an excellent substrate for mammalian Trx system
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
recombinant HvNTR1 and HvNTR2 exhibit virtually the same affinity toward HvTrxh1 and HvTrxh2, whereas HvNTR2 has slightly higher catalytic activity than HvNTR1 with both Trx h isoforms, and HvNTR1 has slightly higher catalytic activity toward HvTrxh1 than HvTrxh2
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
MtNTRC can use either NADPH or NADH as cofactors
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
the enzyme is specific for Methanosarcina acetivorans thioredoxin 7, no activity with Methanosarcina acetivorans thioredoxin 2 or Methanosarcina acetivorans thioredoxin 6
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
C-terminal tetrapeptide sequences is Gly-Cys-Sec-Gly. Changing the C-terminal carboxylate of mTR3 to a carboxamide increases the activity of the enzyme. If the selenium content is normalized for both samples, the carboxamide mutant has nearly twice the activity as the semisynthetic wild-type carboxylate enzyme
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
[redox protein PhRP]-disulfide + NADH + H+
[redox protein PhRP]-dithiol + NAD+
redox protein PhRP from PH0178
-
-
?
[redox protein PhRP]-disulfide + NADH + H+
[redox protein PhRP]-dithiol + NAD+
redox protein PhRP from PH0178
-
-
?
[redox protein PhRP]-disulfide + NADPH + H+
[redox protein PhRP]-dithiol + NADP+
redox protein PhRP from PH0178
-
-
?
[redox protein PhRP]-disulfide + NADPH + H+
[redox protein PhRP]-dithiol + NADP+
redox protein PhRP from PH0178
-
-
?
additional information
?
-
-
NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxin system is suggested to be important for scavenging H2O2 independent of light-driven generation of reducing equivalents
-
-
?
additional information
?
-
-
plants of the ntra ntrb knockout mutant are viable and fertile, although with a wrinkled seed phenotype, slower plant growth, and pollen with reduced fitness. Neither cytosolic nor mitochondrial NADPH-dependent thioredoxin reductases are essential in plants
-
-
?
additional information
?
-
the thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione
-
-
?
additional information
?
-
-
the thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione
-
-
?
additional information
?
-
the enzyme (TrxR) shows a weak ferredoxin/flavodoxin NADP+ oxidoreductase activity toward the flavodoxin-like protein NrdI
-
-
-
additional information
?
-
-
the enzyme (TrxR) shows a weak ferredoxin/flavodoxin NADP+ oxidoreductase activity toward the flavodoxin-like protein NrdI
-
-
-
additional information
?
-
the enzyme (TrxR) shows a weak ferredoxin/flavodoxin NADP+ oxidoreductase activity toward the flavodoxin-like protein NrdI
-
-
-
additional information
?
-
Bdr and BrxB function cooperatively to debacillithiolate OhrR
-
-
-
additional information
?
-
-
Bdr and BrxB function cooperatively to debacillithiolate OhrR
-
-
-
additional information
?
-
incubation of Bdr with BSH under aerobic conditions reveals formation of an S-bacillithiolated species (Bdr-SSB). BrxC is a monothiol bacilliredoxin and Bdr is a bacilliredoxin reductase. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. The two bacilliredoxin (Brx) proteins, BrxA and BrxB, are substrates of Bdr. BrxC de-bacillithiolates enzyme Bdr in vitro. Bdr substrate specificity, overview
-
-
-
additional information
?
-
-
incubation of Bdr with BSH under aerobic conditions reveals formation of an S-bacillithiolated species (Bdr-SSB). BrxC is a monothiol bacilliredoxin and Bdr is a bacilliredoxin reductase. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. The two bacilliredoxin (Brx) proteins, BrxA and BrxB, are substrates of Bdr. BrxC de-bacillithiolates enzyme Bdr in vitro. Bdr substrate specificity, overview
-
-
-
additional information
?
-
Bdr and BrxB function cooperatively to debacillithiolate OhrR
-
-
-
additional information
?
-
incubation of Bdr with BSH under aerobic conditions reveals formation of an S-bacillithiolated species (Bdr-SSB). BrxC is a monothiol bacilliredoxin and Bdr is a bacilliredoxin reductase. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. The two bacilliredoxin (Brx) proteins, BrxA and BrxB, are substrates of Bdr. BrxC de-bacillithiolates enzyme Bdr in vitro. Bdr substrate specificity, overview
-
-
-
additional information
?
-
-
thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
specific for NADPH, B side of nicotinamide ring
-
-
?
additional information
?
-
-
the enzyme does not reduce hydrogen peroxide or insulin
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
NTRC shows both NADPH-dependent thioredoxin reductase and thioredoxin-like dithiol-disulfide oxidoreductase activities
-
-
?
additional information
?
-
-
NTRC shows both NADPH-dependent thioredoxin reductase and thioredoxin-like dithiol-disulfide oxidoreductase activities
-
-
?
additional information
?
-
NTRC shows both NADPH-dependent thioredoxin reductase and thioredoxin-like dithiol-disulfide oxidoreductase activities
-
-
?
additional information
?
-
-
EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediates the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo
-
-
?
additional information
?
-
-
in addition, the enzyme exhibits NAD(P)H dependent oxidase activity, which generates hydrogen peroxide from molecular oxygen
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
-
-
?
additional information
?
-
-
slowly reduces other proteins, e.g. insulin, lipoate and ribonuclease
-
-
?
additional information
?
-
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
additional information
?
-
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
additional information
?
-
-
enzyme does not reduce ubiquinone-10
-
-
?
additional information
?
-
-
thioredoxin reductase is essential for formate dehydrogenase H production and for labelling the formate dehydrogenase H polypeptide with 75Se-selenite
-
-
?
additional information
?
-
R73G, R73D, and K36A site-directed mutants of thioredoxin are impaired to different extents in their ability to be reduced by TrxR
-
-
?
additional information
?
-
-
R73G, R73D, and K36A site-directed mutants of thioredoxin are impaired to different extents in their ability to be reduced by TrxR
-
-
?
additional information
?
-
-
reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
-
-
?
additional information
?
-
-
reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
-
-
?
additional information
?
-
-
reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
-
-
?
additional information
?
-
-
isoform TrxR1 shows broad activity with thioredoxins from Escherichia coli, sheep, and Haemonchus contortus, while isoform TrxR2 has high activity only with the mitochondrial Haemonchus contortus thioredoxin
-
-
?
additional information
?
-
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
additional information
?
-
HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
-
-
?
additional information
?
-
HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
-
-
?
additional information
?
-
-
HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
-
-
?
additional information
?
-
function of TRXR1 in the self-defense mechanism against self-generated oxidative stress
-
-
?
additional information
?
-
-
function of TRXR1 in the self-defense mechanism against self-generated oxidative stress
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
after successful cloning, overexpression and purification of PrxIII,18 Trx2 and TRR2, the PrxIII pathway is reconstituted and studied in vitro
-
-
?
additional information
?
-
-
sulforaphane is an inducer for thioredoxin reductase. The dietary isothiocyanate, sulforaphane, is important in the regulation of thioredoxin reductase/thioredoxin redox system in cells
-
-
?
additional information
?
-
-
isoform TrxR2 cannot reduce lipoic acid
-
-
?
additional information
?
-
binding of NADP+ enhances the ability of Ntr2 to bind thioredoxin
-
-
?
additional information
?
-
no substrates: ferredoxin, flavodoxin
-
-
?
additional information
?
-
no substrates: ferredoxin, flavodoxin
-
-
?
additional information
?
-
no substrates: ferredoxin, flavodoxin
-
-
?
additional information
?
-
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
no substrates: ferredoxin, flavodoxin
-
-
?
additional information
?
-
-
TR3 does not have catalytic preferences for mitochondrial thioredoxin versus cytosolic thioredoxin
-
-
?
additional information
?
-
homozygous (-/-) knockout of Txnrd1 is embryonically lethal. No major effect of Txnrd1 hemizygosity and/or Se on male fertility and the viability of offspring
-
-
?
additional information
?
-
homozygous (-/-) knockout of Txnrd1 is embryonically lethal. No major effect of Txnrd1 hemizygosity and/or Se on male fertility and the viability of offspring
-
-
?
additional information
?
-
homozygous (-/-) knockout of Txnrd2 is embryonically lethal. No major effect of Txnrd2 hemizygosity and/or Se on male fertility and the viability of offspring
-
-
?
additional information
?
-
homozygous (-/-) knockout of Txnrd2 is embryonically lethal. No major effect of Txnrd2 hemizygosity and/or Se on male fertility and the viability of offspring
-
-
?
additional information
?
-
-
the enzyme can promote oxidative stress by redox cycling of paraquat: paraquat + O2 + NADPH + H+ --> paraquat radical + O2- radical + NADP+
-
-
?
additional information
?
-
-
no substrate: chloroplastic thioredoxin x
-
-
?
additional information
?
-
the enzyme has protein disulfide reductase activity with a thioredoxin domain at the C-terminus, able to conjugate both activities for 2-Cys peroxiredoxin reduction
-
-
?
additional information
?
-
-
the enzyme has protein disulfide reductase activity with a thioredoxin domain at the C-terminus, able to conjugate both activities for 2-Cys peroxiredoxin reduction
-
-
?
additional information
?
-
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
additional information
?
-
the enzyme catalyzes the reduction of protein-disulfide oxidoreductase PhRP (PH0178)
-
-
?
additional information
?
-
-
the enzyme catalyzes the reduction of protein-disulfide oxidoreductase PhRP (PH0178)
-
-
?
additional information
?
-
the enzyme catalyzes the reduction of protein-disulfide oxidoreductase PhRP (PH0178)
-
-
?
additional information
?
-
-
specific for NADPH, B side of nicotinamide ring
-
-
?
additional information
?
-
-
ribonucleotide reductase, thioredoxin and thioredoxin reductase constitute a system necessary for the biosynthesis of deesoxyribonucleotides
-
-
?
additional information
?
-
mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity
-
-
?
additional information
?
-
-
the internal disulfide bond (CD7D5) of human neuroglobin can be reduced by thioredoxin reductase
-
-
?
additional information
?
-
-
ebselen, 4,4'-bistrifluoromethyl-diphenyl diselenide, 2,4,6,2',4',6-hexamethyldiphenyl diselenide, and 4,4'-biscarboxydiphenyl diselenide are no substrates
-
-
?
additional information
?
-
enzyme shows additionally NADH oxidase activity
-
-
?
additional information
?
-
-
enzyme shows additionally NADH oxidase activity
-
-
?
additional information
?
-
TrxRB3 also displays NADH oxidase activity
-
-
?
additional information
?
-
-
TrxRB3 also displays NADH oxidase activity
-
-
?
additional information
?
-
TrxRB3 is endowed with an additional NADH oxidase activity
-
-
?
additional information
?
-
-
TrxRB3 is endowed with an additional NADH oxidase activity
-
-
?
additional information
?
-
-
the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin
-
-
?
additional information
?
-
a redox couple consiting of protein disulfide oxidoreductase Ton_0319 and thioredoxin reductase has intracellular cystine-reducing activity, permitting recycling of cysteine. Cysteine or cystine is essentially required for DMSO reduction by whole cells and cell extracts
-
-
?
additional information
?
-
TrxR from Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H
-
-
-
additional information
?
-
Thermosynechococcus vestitus
-
NADPH thioredoxin reductase C functions as an electron donor to 2-Cys peroxiredoxin and transfers the reducing power from NADPH to the peroxiredoxin, which reduces peroxides in the cyanobacterium under oxidative stress
-
-
?
additional information
?
-
-
the enzyme cannot use thioredoxin from Spirulina as an electron acceptor
-
-
?
additional information
?
-
-
the enzyme cannot use thioredoxin from Spirulina as an electron acceptor
-
-
?
additional information
?
-
-
slowly reduces other proteins, e.g. insulin, lipoate and ribonuclease
-
-
?
additional information
?
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
additional information
?
-
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
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(1E,4E)-1,5-bis(3,4-dihydroxyphenyl)penta-1,4-dien-3-one
-
-
(1E,4E)-1,5-bis(3,5-di-tert-butyl-4-hydroxyphenyl)penta-1,4-dien-3-one
-
-
(1E,4E)-1,5-bis(3-bromo-4-hydroxy-5-methoxyphenyl)penta-1,4-dien-3-one
-
-
(1E,4E)-1,5-bis(4-hydroxy-3,5-dimethoxyphenyl)penta-1,4-dien-3-one
-
-
(1E,4E)-1,5-bis(4-hydroxyphenyl)penta-1,4-dien-3-one
-
-
(1E,4Z,6E)-1,7-di-2-furyl-5-hydroxyhepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-1-(2-bromophenyl)-5-hydroxy-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-1-[4-(dimethylamino)phenyl]-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-1,7-bis(5-methyl-2-furyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(5-methyl-2-furyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-[5-(hydroxymethyl)-2-furyl]hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-1-(4-hydroxyphenyl)-7-(2-thienyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxy-3-methoxyphenyl)-1-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxy-3-methoxyphenyl)-1-phenylhepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxyphenyl)-1-(3,4,5-trimethoxyphenyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxyphenyl)-1-phenylhepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]-1-(3,4,5-trimethoxyphenyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]-1-(4-methoxyphenyl)hepta-1,4,6-trien-3-one
-
-
(1E,4Z,6E)-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]-1-phenylhepta-1,4,6-trien-3-one
-
-
(2E,5E)-2,5-bis(3,4-dihydroxybenzylidene)cyclopentanone
-
-
(2E,5E)-2,5-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)cyclopentanone
-
-
(2E,5E)-2,5-bis(4-hydroxybenzylidene)cyclopentanone
-
-
(2E,5E)-2,5-bis[(3,5-di-tert-butyl-4-hydroxyphenyl)methylidene]cyclopentanone
-
-
(2E,5E)-2,5-bis[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]cyclopentanone
-
-
(2E,6E)-2,6-bis(3,4-dihydroxybenzylidene)cyclohexanone
-
-
(2E,6E)-2,6-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)cyclohexanone
-
-
(2E,6E)-2,6-bis(4-hydroxybenzylidene)cyclohexanone
-
-
(2E,6E)-2,6-bis[(3,4-dimethoxyphenyl)methylidene]cyclohexanone
-
-
(2E,6E)-2,6-bis[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]cyclohexanone
-
-
(2E,6E)-2-(4-hydroxybenzylidene)-6-(4-hydroxy-3-methoxybenzylidene)cyclohexanone
-
-
(2E,6E)-2-[(4-hydroxyphenyl)methylidene]-6-[(3,4,5-trimethoxyphenyl)methylidene]cyclohexanone
-
-
(3E,5E)-3,5-bis(3,4-dihydroxybenzylidene)piperidin-4-one
-
-
(3E,5E)-3,5-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)piperidin-4-one
-
-
(3E,5E)-3,5-bis(4-hydroxybenzylidene)-4-oxopiperidinium
-
-
(3E,5E)-3,5-bis[(3,4-dimethoxyphenyl)methylidene]piperidin-4-one
-
-
(3E,5E)-3,5-bis[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]piperidin-4-one
-
-
(3E,5E)-3-[(2,5-di-tert-butyl-4-hydroxyphenyl)methylidene]-5-[(3,5-di-tert-butyl-4-hydroxyphenyl)methylidene]piperidin-4-one
-
-
(4-ammoniothiophenolato)(2,2':6',2''-terpyridine)platinum(II) chloride
-
-
(4-ammoniothiophenolato)(4'-toyl-2,2':6',2''-terpyridine)platinum(II) nitrate
-
-
(4-hydroxylthiophenolato)(2,2':6',2''-terpyridine)platinum(II) chloride
-
-
(4-hydroxylthiophenolato)(4'-toyl-2,2':6',2''-terpyridine)platinum(II) chloride
-
-
(4-methylpyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
-
-
(4-methylpyrimidine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
-
-
(N-acetyl-4-aminothiophenolato)(2,2':6',2''-terpyridine)platinum(II) chloride
-
-
(N-acetyl-4-aminothiophenolato)(4'-toyl-2,2':6',2''-terpyridine)platinum(II) nitrate
-
-
(pyridine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
-
-
(pyridine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
-
-
(pyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
-
-
1,1'-sulfanediylbis(2,4-dinitrobenzene)
1,1'-sulfanediylbis[2-nitro-4-(trifluoromethyl)benzene]
1,2-[bis(1,2-benzisoselenazolone-3(2H)-ketone)]ethane
-
apoptosis induced by the inhibitor is through Bcl-2/Bax and caspase-3 pathways
1,3-dinitro-5-(trifluoromethyl)benzene
1,4-dihydroxyanthroquinone
-
1,8-dihydroxyanthroquinone
-
1-chloro-2,4-dinitrobenzene
1-Fluoro-2,4-dinitrobenzene
1-methyl-1-propyl-2-imidazolyl disulfide
15-deoxy-D-12,14-PGJ2
-
0.06 mM, IC50: 0.00036 mM
2,2'-(ethane-1,2-diyl)di(1,2-benzoselenazol-3(2H)-one)
-
IC50 value for HEK-293T cells 3.4 microg/ml
2,2'-(hexane-1,6-diyl)di(1,2-benzoselenazol-3(2H)-one)
-
IC50 value for HEK-293T cells 2.5 microg/ml
2-aminothiazolium [trans-tetrachlorobis(2-aminothiazole)ruthenate(III)]
-
2-benzoyloxycinnamaldehyde
2-benzyloxycinnamaldehyde
2-chloro-1,3-dinitro-5-(trifluoromethyl)benzene
2-hydroxymethyl-5-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
2-hydroxymethyl-5-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
2-hydroxymethyl-6-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
3,4-estronequinone
-
0.032 mM, IC50: 0.02 mM
3-(4-[[2-(1-hydroxy-4-oxocyclohexa-2,5-dien-1-yl)-1H-indol-1-yl]sulfonyl]phenyl)propanoic acid
-
-
3-(4-[[6-fluoro-2-(1-hydroxy-4-oxocyclohexa-2,5-dien-1-yl)-1H-indol-1-yl]sulfonyl]phenyl)propanoic acid
-
-
4,5-dinitro-1,3-benzodioxole
4,6-dinitro-2,1,3-benzothiadiazole
4-(1,3-benzothiazol-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
-
-
4-(1,3-benzoxazol-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
-
-
4-(1-benzothien-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
-
-
4-(5-fluoro-1,3-benzothiazol-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
-
-
4-azobenzene sulfonic acid
-
63% residual activity at 5 mM
4-hydroxy-2-nonenal
-
0.005-0.025 mM, IC50: 0.0038 mM, irreversible inhibition; 0.05 mM, remarkable lost inhibition
4-hydroxy-4-[1-(phenylsulfonyl)-1H-indol-2-yl]cyclohexa-2,5-dien-1-one
-
-
4-hydroxynonenal
-
0.06 mM, IC50: 0.012 mM
4-nitro-2,1,3-benzothiadiazole
4-[6-fluoro-1-(phenylsulfonyl)-1H-indol-2-yl]-4-hydroxycyclohexa-2,5-dien-1-one
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
above 0.1 mM
5-fluoro-2-hydroxycinnamaldehyde
5-methoxy-1,2-dimethyl-3-[1-oxo-2-(2,4,6-trifluorophenyl)ethyl]indole-4,7-dione
5-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
5-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
5-nitro-2,1,3-benzothiadiazole
6-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
6-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
allyl isothiocyanate
-
0.0205 mM, 50% inhibition after 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
arsenic trioxide
-
irreversible. Both the N-terminal redox-active dithiol and the C-terminal selenothiol-active site of reduced TrxR may participate in the reaction with the inhibitor. The inhibition of MCF-7 cell growth by arsenic trioxide is correlated with irreversible inactivation of thioredoxin reductase, which subsequently led to thioredoxin oxidation
Benzyl isothiocyanate
-
0.0033 mM, 50% inhibition after 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
bis-demethoxy curcumin
-
-
chaetocin
-
competitive inhibitor with anticancer effects, complete inhibition at 0.015 mM
chloro[N(4)-ortho-chlorophenyl-2-acetylpyridinethiosemicarbazonato]gold(III)dichloroaurate(I)
-
in addition, the complex is highly cytotoxic to MCF-7 and HT29 cells
Cr6+
-
hexavalent chromium causes pronounced inhibition of TrxR, the inhibition of TrxR is not reversed by removal of residual Cr6+ or by NADPH. In cells treated with 0.025 or 0.050 mM Cr6+ for 90 min, TrxR activity is inhibited by 71 and 77%, respectively, while after 180 min of the same treatments, TrxR is inhibited by 97 and 85%, respectively
cyclophosphamide
-
250 mg/kg reduces activity reversibly to 25% at 3h after treatment
diallyl disulfide
-
0.38 mM, 50% inhibition after 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
dichloro[N(4)-ortho-chlorophenyl-2-acetylpyridinethiosemicarbazonato]antimony(III)
-
in addition, the complex is highly cytotoxic to MCF-7 and HT29 cells
diphenylene iodonium
-
IC50: 0.001 mM
Glyoxal
-
93% residual activity at 5 mM
gold acetate
-
500 nM, 50% inhibition
gold sodium thiomalate
-
500 nM, 50% inhibition
ifosfamide
-
inhibition of thioredoxin reductase activity in malignant cells by ifosfamide is highly associated with its anticancer effect and the mechanism of ifosfamide systemic toxicity may be related to multi-organ inhibition of thioredoxin reductase activity
Iodine
-
86% residual activity at 5 mM
leukotriene A4 methyl ester
-
0.06 mM, IC50: 0.513 mM
metronidazole
-
metronidazole-modified recombinant enzyme displays considerably reduced thioredoxin reductase activity. By reducing metronidazole, the enzyme renders itself and associated thiol-containing proteins vulnerable to adduct formation
myricetin
-
0.05 mM, strong inhibitory effect, IC50: 0.62 mM
NAD+
-
NAD+ acts as poor competitive inhibitor respect to both NADPH and NADH
p-chloromercuribenzoate
-
with NADPH
palmarumycin CP1
-
0.001 mM, the naphthoquinone spiroketal fungal metabolite palmarumycin CP1 is a potent inhibitor of thioredoxin reductase-1, IC50: 0.00035 mM
palmitoyl-CoA
covalent inhibition of TrxR1/hTrx1 by palmitoyl-CoA. The palmitoyl-CoA/TrxR1 reaction is NADPH-dependent and produces palmitoylated TrxR1 at an active site selenocysteine residue
phenethyl isothiocyanate
-
0.075 mM, 50% inhibition after 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
phenyl mercuric acetate
-
stabilizes enzyme in one of two possible conformations
Prostaglandin A2
-
0.06 mM, IC50: 0.068 mM
pseudohypericin
strong inhibitor of isoform TrxR1
PX-911
-
0.001 mM, a water-soluble prodrug of a palmarumycin CP1 analogue, IC50: 0.0032 mM
PX-916
-
0.001 mM, a water-soluble prodrug of a palmarumycin CP1 analogue, potent inhibitor of purified human thioredoxin reductase-1, IC50: 0.00028 mM
PX-960
-
0.001 mM, a water-soluble prodrug of a palmarumycin CP1 analogue, IC50: 0.00027 mM
quercetin
-
0.05 mM, strong inhibitory effect, IC50: 0.97 mM
reactive oxygen species
-
0.1 mM, ROS generated by xanthine/xanthine oxidase enhance the inhibitory effect of flavonoids
-
sodium aurothiomalate
-
0.1 mM
sodium aurothiosulfate
-
100 nM, 50% inhibition
sulforaphane
-
0.04 mM, 50% inhibition after 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
theaflavin-3'-monogallate
-
theaflavin-3,3'-digallate
-
theaflavin-3-monogallate
-
trans-[bis(2-amino-5-methylthiazole)tetrachlororuthenate(III)]
selective inhibition of TrxR1
triphenyl phosphine gold chloride
-
75 nM, 50% inhibition
trisodium (4,5-dihydro-1,3-thiazole-2-thiolato-kappaS2)[3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)]aurate(3-)
-
-
trisodium [3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)](pyrimidine-2-thiolato-kappaS)aurate(3-)
-
-
Zinc
-
0.05 mM, 50% inhibition
[(iPr2Im)2Au]Cl
-
mainly inhibits isoform TrxR2, about 30% residual activity after 8 h at 0.005 mM or 0.05 mM
[Au(d2pype)2]Cl
-
mainly inhibits isoform TrxR1, about 30% residual activity after 8 h at 0.005 mM, about 10% residual activity after 8 h at 0.05 mM
[Au(d2pypp)2]Cl
-
about 30% residual activity after 8 h at 0.005 mM, about 10% residual activity after 8 h at 0.05 mM
[Pt(2,2'-bipyridine)(ethylenediamine)]Cl2
-
the platinum(II) complex acts as an inhibitor by binding with the active site of the enzyme
1,1'-sulfanediylbis(2,4-dinitrobenzene)
-
IC50: 0.004 mM
1,1'-sulfanediylbis(2,4-dinitrobenzene)
-
IC50: 0.0005 mM
1,1'-sulfanediylbis[2-nitro-4-(trifluoromethyl)benzene]
-
IC50: 0.15 mM
1,1'-sulfanediylbis[2-nitro-4-(trifluoromethyl)benzene]
-
IC50: 0.02 mM
1,3-dinitro-5-(trifluoromethyl)benzene
-
IC50: 0.2 mM
1,3-dinitro-5-(trifluoromethyl)benzene
-
IC50: 0.03 mM
1-chloro-2,4-dinitrobenzene
-
i.e. DNCB; irreversible, with NADPH, alkylation of the active site cysteine disulfide, strong increase in oxidation activity of the enzyme against NADPH
1-chloro-2,4-dinitrobenzene
-
i.e. DNCB; mitochondrial isoform
1-chloro-2,4-dinitrobenzene
-
0.01 mM, irreversible inhibition
1-chloro-2,4-dinitrobenzene
-
-
1-chloro-2,4-dinitrobenzene
-
i.e. DNCB; irreversible, with NADPH, alkylation of the active site cysteine disulfide, strong increase in oxidation activity of the enzyme against NADPH
1-chloro-2,4-dinitrobenzene
-
1-chloro-2,4-dinitrobenzene
-
0.1 mM
1-chloro-2,4-dinitrobenzene
-
uncompetitive inhibition
1-chloro-2,4-dinitrobenzene
-
TrxR inhibition by 1-chloro-2,4-dinitrobenzene results in generation of reactive oxygen species and subsequent activation of stress-inducible kinases without impairment of the cellular antioxidant status or mitochondrial function
1-chloro-2,4-dinitrobenzene
-
1-chloro-2,4-dinitrobenzene
-
-
1-Fluoro-2,4-dinitrobenzene
-
irreversible, with NADPH, alkylation of the active site cysteine disulfide, strong increase in oxidation activity of the enzyme against NADPH
1-Fluoro-2,4-dinitrobenzene
-
irreversible, with NADPH, alkylation of the active site cysteine disulfide, strong increase in oxidation activity of the enzyme against NADPH
1-methyl-1-propyl-2-imidazolyl disulfide
-
1-methyl-1-propyl-2-imidazolyl disulfide
-
2-benzoyloxycinnamaldehyde
-
-
2-benzoyloxycinnamaldehyde
-
-
2-benzoyloxycinnamaldehyde
-
-
2-benzyloxycinnamaldehyde
-
-
2-benzyloxycinnamaldehyde
-
-
2-chloro-1,3-dinitro-5-(trifluoromethyl)benzene
-
IC50: 0.1 mM
2-chloro-1,3-dinitro-5-(trifluoromethyl)benzene
-
IC50: 0.008 mM
2-hydroxycinnamaldehyde
-
-
2-hydroxycinnamaldehyde
-
-
2-hydroxymethyl-5-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
-
maximum inhibition is achieved 5 min after addition of 0.003 mM
2-hydroxymethyl-5-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
-
maximum inhibition is achieved 5 min after addition of 0.003 mM
2-hydroxymethyl-5-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
2-hydroxymethyl-5-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
2-hydroxymethyl-6-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
2-hydroxymethyl-6-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
2-pentoxycinnamaldehyde
-
-
2-pentoxycinnamaldehyde
-
-
4,5-dinitro-1,3-benzodioxole
-
IC50: 0.08 mM
4,5-dinitro-1,3-benzodioxole
-
IC50: 0.01 mM
4,6-dinitro-2,1,3-benzothiadiazole
-
IC50: 0.002 mM
4,6-dinitro-2,1,3-benzothiadiazole
-
IC50: 0.01 mM
4-nitro-2,1,3-benzothiadiazole
-
IC50: 0.05 mM
4-nitro-2,1,3-benzothiadiazole
-
IC50: 0.002 mM
4-Vinylpyridine
-
irreversible
4-Vinylpyridine
-
irreversible
5-fluoro-2-hydroxycinnamaldehyde
-
-
5-fluoro-2-hydroxycinnamaldehyde
-
-
5-fluoro-2-hydroxycinnamaldehyde
-
-
5-methoxy-1,2-dimethyl-3-[1-oxo-2-(2,4,6-trifluorophenyl)ethyl]indole-4,7-dione
-
-
5-methoxy-1,2-dimethyl-3-[1-oxo-2-(2,4,6-trifluorophenyl)ethyl]indole-4,7-dione
-
-
5-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
-
-
5-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
-
-
5-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
5-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
5-nitro-1,3-benzodioxole
-
IC50: 0.2 mM
5-nitro-1,3-benzodioxole
-
0.1 mM, 10% inhibition
5-nitro-2,1,3-benzothiadiazole
-
IC50: 0.09 mM
5-nitro-2,1,3-benzothiadiazole
-
IC50: 0.01 mM
6,7-dinitroquinoxaline
-
IC50: 0.14 mM
6,7-dinitroquinoxaline
-
IC50: 0.002 mM
6-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
-
-
6-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
-
-
6-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
6-methoxy-1-methyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione
-
-
6-nitroquinoxaline
-
IC50: 0.2 mM
6-nitroquinoxaline
-
IC50: 0.04 mM
Ag+
-
enzyme activity is moderately reduced (50%) by 1 mM
Ag+
-
silver ions bind to the active sites of thioredoxin reductase with dissociation constants of 0.0014 mM and stoichiometries of 1 Ag+ ion per protein
arsenite
-
-
auranofin
-
-
auranofin
-
15 nM, complete inhibition
auranofin
-
inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells
auranofin
-
about 10% residual activity at 400 nM in the presence of NADPH, less than 5% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 80% residual activity at 400 nM for juglone reduction
auranofin
-
efficient inhibition, about 20% residual activity after 8 h at 0.005 mM, about 7% residual activity after 8 h at 0.05 mM
auranofin
-
irreversibe inhibition
auranofin
-
5-10 nM, 50% inhibition, complete inhibition above 15 nM
auranofin
-
about 10% residual activity at 400 nM in the presence of NADPH, less than 5% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 80% residual activity at 400 nM for juglone reduction
auranofin
-
protects cerebellar granular neurons from the action of different doses of tetanus neurotoxin, about 1 microM auranofinF confers a full protection against tetnus neurotoxin intoxication. Auranofin protects cerebellar granular neurons from the cleavage of VAMP-2 induced by botulinum neurotoxi B and the cleavage of syntaxin 1A induced by botulinum neurotoxin C
aurothioglucose
-
IC50: 120 nM
aurothioglucose
-
0.02 mM
aurothioglucose
-
about 90% residual activity after 8 h at 0.005 mM, about 80% residual activity after 8 h at 0.05 mM
Ca2+
-
-
Ca2+
-
non-reversible by EDTA
calveolin
overexpression of caveolin 1 inhibits TrxR activity by about 50% whereas a lack of caveolin 1 activates TrxR, both in vitro and in vivo
-
calveolin
-
overexpression of caveolin 1 inhibits TrxR activity by about 50% whereas a lack of caveolin 1 activates TrxR, both in vitro and in vivo
-
Cd2+
-
enzyme activity is drastically reduced (70%) by 1 mM
cisplatin
-
cisplatin
-
i.e. cis-diamminedichloroplatinum(II), about 3% residual activity at 400 nM in the presence of NADPH, about 10% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 90% residual activity at 400 nM for juglone reduction
cisplatin
-
about 40% residual activity after 8 h at 0.005 mM or 0.05 mM
cisplatin
-
at pharmacological doses inhibits TrxR activity in both ascitic hepatoma 22 cells and kidney, leading to suppression of H22 cells proliferation along with nephrotoxicity. Amifostine, a clinical used cytoprotective agent, protected against CDDP-induced TrxR inactivation in kidney but not in H22 cells
cisplatin
-
heat shock protein 27 protects L929 cells from cisplatin-induced apoptosis by enhancing Akt activation and abating suppression of thioredoxin reductase activity
cisplatin
complete inhibition after 1 h at 0.5 mM
cisplatin
-
i.e. cis-diamminedichloroplatinum(II), about 3% residual activity at 400 nM in the presence of NADPH, about 10% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 90% residual activity at 400 nM for juglone reduction
Cu2+
-
strong inhibition
Cu2+
-
enzyme activity is drastically reduced (70%) by 1 mM
curcumin
-
curcumin
-
IC50: 0.0036 mM
curcumin
-
irreversible inhibition
ebselen
-
competitive, inhibitor reacts with the active site dithiol
ebselen
-
reversible competitive inhibitor of the enzyme from Escherichia coli. Ebselen can form a stable selenosulfide bond with the attacking cysteine in Escherichia coli thioredoxin reductase which cannot easily be resolved by the other cysteine in the active site. The binding blocks the electron transfer from Escherichia coli TrxR to Trx, and ultimately to the downstream substrates of thioredoxin. Ebselen is an excellent substrate for mammalian thioredoxin system
ES936
-
i.e. 5-methoxy-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione, potent inhibitor
ES936
-
i.e. 5-methoxy-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione, potent inhibitor
gold
-
potent inhibitor, the inhibition of TrxR1 by the metal compound is not markedly influenced by the presence of EDTA
gold
-
potent inhibitor, the inhibition of TrxR1 by the metal compound is not markedly influenced by the presence of EDTA
Hg2+
-
Hg2+
-
enzyme activity is drastically reduced (70%) by 1 mM
Hg2+
potently inhibits (at concentrations of 5-50 nM) TrxR1 activity in both cell-free and intracellular assays
Hg2+
-
in the presence of NADPH, a ratio of 2 HgCl2 molecules to 1 TrxR dimer leads to a virtually inactive enzyme. On treatment with 0.005 mM selenite and NADPH, TrxR inactivated by HgCl2 displays almost full recovery of activity
Hg2+
-
in the presence of NADPH, a ratio of 2 HgCl2 molecules to 1 TrxR dimer leads to a virtually inactive enzyme. On treatment with 0.005 mM selenite and NADPH, TrxR inactivated by HgCl2 displays almost full recovery of activity
iodoacetate
-
irreversible
iodoacetate
-
irreversible
juglone
-
K2PdCl4
-
strong and irreversible inhibition, about 30% residual activity at 400 nM in the presence of NADPH, less than 10% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 90% residual activity at 400 nM for juglone reduction
K2PdCl4
-
strong and irreversible inhibition, about 30% residual activity at 400 nM in the presence of NADPH, less than 10% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 90% residual activity at 400 nM for juglone reduction
K2PdCl6
-
irreversible inhibition
K2PdCl6
-
irreversible inhibition
K2PtCl4
-
irreversible inhibition, about 5% residual activity at 400 nM in the presence of NADPH, complete inhibition of 5,5'-dithiobis(2-nitrobenzoic acid) reduction at 400 nM, about 90% residual activity at 400 nM for juglone reduction
K2PtCl4
-
irreversible inhibition, about 5% residual activity at 400 nM in the presence of NADPH, complete inhibition of 5,5'-dithiobis(2-nitrobenzoic acid) reduction at 400 nM, about 90% residual activity at 400 nM for juglone reduction
K2PtCl6
-
irreversible inhibition
K2PtCl6
-
irreversible inhibition
KAuCl4
-
irreversible inhibition, about 10% residual activity at 400 nM in the presence of NADPH, less than 5% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 70% residual activity at 400 nM for juglone reduction
KAuCl4
-
irreversible inhibition, about 10% residual activity at 400 nM in the presence of NADPH, less than 5% residual activity at 400 nM for 5,5'-dithiobis(2-nitrobenzoic acid) reduction, about 70% residual activity at 400 nM for juglone reduction
menadione
-
methylmercury
-
in the case of methylmercury, a ratio of 16 molecules per dimer leads to a virtually inactive enzyme
methylmercury
-
a single administration of methylmercury (1, 5, and 10 mg/kg) causes a marked inhibition of kidney TrxR activity, while significant inhibition is observed in the liver 24 h after exposure to 5 and 10 mg/kg. In the brain, methylmercury does not inhibit TrxR activity. Methylmercury can bind to selenocysteine residues present in the catalytic site of TrxR, in turn causing enzyme inhibition that can compromise the redox state of cells
methylmercury
-
in the case of methylmercury, a ratio of 16 molecules per dimer leads to a virtually inactive enzyme
N-ethylmaleimide
-
46% residual activity at 5 mM
N-ethylmaleimide
-
reaction only with the reduced enzyme
NADP+
-
better competitive inhibitor than NAD+
NADP+
-
product inhibition
oxaliplatin
-
palladium
-
potent inhibitor, the inhibition of TrxR1 by the metal compound is not markedly influenced by the presence of EDTA
palladium
-
potent inhibitor, the inhibition of TrxR1 by the metal compound is not markedly influenced by the presence of EDTA
platinum
-
the inhibition of TrxR1 by the metal compound is not markedly influenced by the presence of EDTA
platinum
-
the inhibition of TrxR1 by the metal compound is not markedly influenced by the presence of EDTA
theaflavin
-
trans,trans-curcumin
-
0.01-0.05 mM, IC50: 0.0015 mM, irreversible inhibition
trans,trans-curcumin
-
IC50: 0.0036 mM, irreversible inhibition after incubation at room temperature for 2 h in vitro
trans-cinnamaldehyde
-
-
Zn2+
-
strong inhibition
Zn2+
-
enzyme activity is drastically reduced (70%) by 1 mM
Zn2+
-
0.1-0.2 mM and above
Zn2+
-
0.1-0.2 mM and above
additional information
-
no inhibition with dinitrohalobenzene analogues: 1,4-dichlorobenzene, 1-chloro-4-nitrobenzene, 1-chloro-3,4-dinitrobenzene, 1-chloro-2,5-dinitrobenzene
-
additional information
-
not inhibited by 1-chloro-2,4-dinitrobenzene
-
additional information
-
not inhibited by trans-cinnamaldehyde and 2-hydroxycinnamaldehyde after 1 h of incubation
-
additional information
-
no inhibition with dinitrohalobenzene analogues: 1,4-dichlorobenzene, 1-chloro-4-nitrobenzene, 1-chloro-3,4-dinitrobenzene, 1-chloro-2,5-dinitrobenzene
-
additional information
-
no inhibition by Ca2+ or Co2+
-
additional information
transfection of HeLa cells with siRNA targeted against TrxR1 effectively decreases TrxR1 protein levels and activity relative to control cells. Trx1 oxidation is not an inevitable consequence of TrxR1 inhibition
-
additional information
-
hypoxanthine/xanthine oxidase system and H2O2 in rheumatoid arthritis cells decrease thioredoxin reductase activity, which is found to be unchanged in osteoarthritis cells. H2O2 and superoxide anion cause a time-dependent accumulation of oxidized thioredoxin reductase and induces the formation of carbonyl groups in thioredoxin reductase protein in rheumatoid arthritis cells rather than osteoarthritis cells, and oxidizes the selenocysteine of the active site. The oxidation in thioredoxin reductase protein is irreversible in rheumatoid arthritis cells but not in osteoarthritis cells
-
additional information
-
2-[(1-methylpropyl)dithio]-1H-imidazole (IV-2) causes the oxidation of cysteine residues from both thioredoxin reductase and thioredoxin, with only the latter leading to irreversible inhibition of protein function
-
additional information
-
SecTRAPs (selenium compromised thioredoxin reductase-derived apoptotic proteins) can be formed from the selenoprotein thioredoxin reductase by targeting of its selenocysteine residue with electrophiles, or by its removal through C-terminal truncation. SecTRAPs are devoid of thioredoxin reductase activity but can induce rapid cell death in cultured cancer cell lines by a gain of function. Human and rat SecTRAPs induce cell death in human A549 and HeLa cells
-
additional information
black tea extract and theaflavins (mixture of theaflavin, theaflavin-3-monogallate, theaflavin-3'-monogallate and theaflavin-3,3'-digallate) inhibit the purified TrxR1 with IC50 44 mg/ml and 21 mg/ml, respectively. Kinetics of theaflavins exhibit a mixed type of competitive and non-competitive inhibition, with Kis 4 mg/ml and Kii 26 mg/ml against coenzyme NADPH, and with Kis 12 mg/ml and Kii 27 mg/ml against substrate 5,5'-dithiobis(2-nitrobenzoic acid)
-
additional information
-
not inhibited by 2-methoxycinnamaldehyde and cinnamic acid
-
additional information
-
tetrahydrocurcumin has no significant effect on TxnRd activity at doses of up to 0.05 mM
-
additional information
-
no inhibition by Ca2+ or Co2+
-
additional information
-
the enzyme is not inhibited by dimedone even at 150fold excess
-
additional information
-
quinols irreversible inhibit mammalian TrxR by targeting the penultimate C-terminal selenocysteine residue
-
additional information
SecTRAPs (selenium compromised thioredoxin reductase-derived apoptotic proteins) can be formed from the selenoprotein thioredoxin reductase by targeting of its selenocysteine residue with electrophiles, or by its removal through C-terminal truncation. SecTRAPs are devoid of thioredoxin reductase activity but can induce rapid cell death in cultured cancer cell lines by a gain of function. Human and rat SecTRAPs induce cell death in human A549 and HeLa cells
-
additional information
-
not inhibited by 2-methoxycinnamaldehyde and cinnamic acid after 1 h of incubation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.032 - 11.9
5,5'-dithio-bis(2-nitrobenzoic acid)
0.0186 - 172.4
5,5'-dithiobis(2-nitrobenzoic acid)
0.00227 - 0.02374
5-hydroxy-1,4-naphthoquinone
0.00048 - 0.0543
Arabidopsis thaliana thioredoxin 3
-
0.0042
Babesia bovis thioredoxin
pH 8.0, 30°C
-
0.089
benzyl viologen
-
at pH 9.5 and 80°C
0.0046
chaetocin
-
in 100 mM potassium phosphate (pH 7.0), at 22°C
0.0161
chetomin
-
in 100 mM potassium phosphate (pH 7.0), at 22°C
1.25
dithionitrobenzene
-
pH and temperature not specified in the publication
0.0025
ebsulfur
-
pH 7.5, temperature not specified in the publication
0.0275
ebsulfur disulfide
-
pH 7.5, temperature not specified in the publication
0.0036
Entamoeba histolytica thioredoxin disulfide 41
-
pH 7.0, 25°C
-
0.007 - 0.149
Escherichia coli thioredoxin
-
0.0046
Escherichia coli thioredoxin disulfide
-
pH 7.0, 25°C
-
0.0169
gliotoxin
-
in 100 mM potassium phosphate (pH 7.0), at 22°C
0.0333
glutaredoxin 4
-
-
-
2.5
H2O2
-
wild-type enzyme, Km-value can be reduced by addition of selenocysteine
0.00123
Hordeum vulgare thioredoxin 1
wild-type, pH 7.5, temperature not specified in the publication
-
0.00068 - 0.06
Hordeum vulgare thioredoxin 2
-
0.00041 - 0.0016
Hordeum vulgare thioredoxin 2 mutant E86A
-
0.0014
Hordeum vulgare thioredoxin 2 mutant G57P
wild-type, pH 7.5, temperature not specified in the publication
-
0.0155
Hordeum vulgare thioredoxin 2 mutant I51G
wild-type, pH 7.5, temperature not specified in the publication
-
0.00112 - 0.00118
Hordeum vulgare thioredoxin disulfide h1
-
0.0009 - 0.00179
Hordeum vulgare thioredoxin disulfide h2
-
0.0033
human thioredoxin
-
wild-type enzyme
6.6
hydrogen peroxide
semisynthetic enzyme with 91% content of selenium
0.0027
lipoic acid
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
0.134
methaneseleninic acid
-
at pH 6.1 and 37°C
0.018
methylseleninate
-
-
0.035
protein disulfide-isomerase
-
-
-
0.0025 - 0.0033
reductase
-
0.00031 - 67.6
thioredoxin
0.0013
thioredoxin 1
-
wild type enzyme, pH and temperature not specified in the publication
0.0006 - 0.0009
thioredoxin 2
-
0.0011
thioredoxin 3
-
wild type enzyme, pH and temperature not specified in the publication
-
0.0023 - 0.0036
thioredoxin 41
-
0.0028 - 0.0029
thioredoxin 8
-
0.00047
thioredoxin C-2
-
-
-
0.00099 - 0.173
thioredoxin disulfide
0.0036
thioredoxin disulfide 41
-
pH 7, 30°C
-
0.0028
thioredoxin disulfide 8
-
pH 7, 30°C
-
0.0076
thioredoxin disulfide h
-
-
0.0067
thioredoxin K36R
-
substrate mutant, pH 8.0
-
0.007 - 0.019
thioredoxin-1 disulfide
-
0.0044
thioredoxin-II
-
-
-
0.125
thioredoxin-R
-
substrate mutant, thioredoxin-CAC, pH 8.0
-
additional information
additional information
-
0.032
5,5'-dithio-bis(2-nitrobenzoic acid)
-
pH 7.5, 50°C
0.238
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 8.0, 30°C
0.28
5,5'-dithio-bis(2-nitrobenzoic acid)
-
pH 7.8, 37°C
2.4
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 7.2, temperature not specified in the publication
2.5
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 7.2, temperature not specified in the publication
11.9
5,5'-dithio-bis(2-nitrobenzoic acid)
truncated mutant, pH 7.2, temperature not specified in the publication
0.0186
5,5'-dithiobis(2-nitrobenzoic acid)
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.049
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
0.088
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme
0.09
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C
0.0906
5,5'-dithiobis(2-nitrobenzoic acid)
mutant enzyme Y116T, in TE buffer, at 20°C
0.094
5,5'-dithiobis(2-nitrobenzoic acid)
wild type enzyme, in TE buffer, at 20°C
0.0971
5,5'-dithiobis(2-nitrobenzoic acid)
mutant enzyme Y116I, in TE buffer, at 20°C
0.105
5,5'-dithiobis(2-nitrobenzoic acid)
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
0.114
5,5'-dithiobis(2-nitrobenzoic acid)
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
0.139
5,5'-dithiobis(2-nitrobenzoic acid)
purified, recombinant, tetrameric enzyme
0.17
5,5'-dithiobis(2-nitrobenzoic acid)
full-length Drosophila enzyme with C-terminal sequence SCCS
0.2156
5,5'-dithiobis(2-nitrobenzoic acid)
purified, recombinant, dimeric enzyme
0.22
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
0.39
5,5'-dithiobis(2-nitrobenzoic acid)
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
0.41
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
0.42
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme
0.45
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
0.463
5,5'-dithiobis(2-nitrobenzoic acid)
-
in 50 mM potassium phosphate buffer (pH 7.0), at 22°C
0.47
5,5'-dithiobis(2-nitrobenzoic acid)
full-length mouse enzyme with C-terminal sequence GCUG
0.53
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
0.7
5,5'-dithiobis(2-nitrobenzoic acid)
-
pH 7.4
0.7
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant U498C
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
0.75
5,5'-dithiobis(2-nitrobenzoic acid)
-
pH 7, 25°C
0.83
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
0.92
5,5'-dithiobis(2-nitrobenzoic acid)
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid
1.1
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16 mutant K29R/H108Y/A119N/V478E
1.1
5,5'-dithiobis(2-nitrobenzoic acid)
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.4
5,5'-dithiobis(2-nitrobenzoic acid)
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.7
5,5'-dithiobis(2-nitrobenzoic acid)
-
pH 7.0, 25°C
2.4
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16, TrxR lacking the last 16 C-terminal amino acids
2.72
5,5'-dithiobis(2-nitrobenzoic acid)
truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid
3.3
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16 mutant K29R
4.1
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
4.5
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16 mutant K29R/H108Y
172.4
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
0.00227
5-hydroxy-1,4-naphthoquinone
wild type enzyme, in TE buffer, at 20°C
0.00698
5-hydroxy-1,4-naphthoquinone
mutant enzyme Y116T, in TE buffer, at 20°C
0.02374
5-hydroxy-1,4-naphthoquinone
mutant enzyme Y116I, in TE buffer, at 20°C
0.00048
Arabidopsis thaliana thioredoxin 3
pH 7.5, temperature not specified in the publication
-
0.00052
Arabidopsis thaliana thioredoxin 3
mutant G222D/A223G/G224E, pH 7.5, temperature not specified in the publication
-
0.00067
Arabidopsis thaliana thioredoxin 3
mutant G225R/G226D, pH 7.5, temperature not specified in the publication
-
0.00073
Arabidopsis thaliana thioredoxin 3
mutant G225R/G226D/P227V, pH 7.5, temperature not specified in the publication
-
0.0008
Arabidopsis thaliana thioredoxin 3
wild-type, pH 7.5, temperature not specified in the publication
-
0.0024
Arabidopsis thaliana thioredoxin 3
mutant W42A, pH 7.5, temperature not specified in the publication
-
0.0042
Arabidopsis thaliana thioredoxin 3
mutant N45A/D46A, pH 7.5, temperature not specified in the publication
-
0.0141
Arabidopsis thaliana thioredoxin 3
mutant M43A, pH 7.5, temperature not specified in the publication
-
0.0305
Arabidopsis thaliana thioredoxin 3
mutant W42A/M43A, pH 7.5, temperature not specified in the publication
-
0.0543
Arabidopsis thaliana thioredoxin 3
mutant Delta42-47, pH 7.5, temperature not specified in the publication
-
0.05
DTNB
-
mutant enzyme H509Q
0.147
DTNB
-
mutant enzyme H509A
0.212
DTNB
-
wild-type enzyme
0.38
DTNB
-
cytosolic TrxR1 isoform
0.41
DTNB
-
mitochondrial TrxR1 isoform
0.007
Escherichia coli thioredoxin
pH 8.0, 30°C
-
0.149
Escherichia coli thioredoxin
wild-type, pH 7.5, temperature not specified in the publication
-
0.00068
Hordeum vulgare thioredoxin 2
mutant N139A, pH 7.5, temperature not specified in the publication
-
0.00105
Hordeum vulgare thioredoxin 2
mutant G225R/G226D/P227V, pH 7.5, temperature not specified in the publication
-
0.00117
Hordeum vulgare thioredoxin 2
wild-type, pH 7.5, temperature not specified in the publication
-
0.00128
Hordeum vulgare thioredoxin 2
mutant G225R/G226D, pH 7.5, temperature not specified in the publication
-
0.00146
Hordeum vulgare thioredoxin 2
mutant G222D/A223G/G224E, pH 7.5, temperature not specified in the publication
-
0.0022
Hordeum vulgare thioredoxin 2
mutant N45A/D46A, pH 7.5, temperature not specified in the publication
-
0.00343
Hordeum vulgare thioredoxin 2
mutant R140A, pH 7.5, temperature not specified in the publication
-
0.016
Hordeum vulgare thioredoxin 2
mutant M43A, pH 7.5, temperature not specified in the publication
-
0.0457
Hordeum vulgare thioredoxin 2
mutant W42A, pH 7.5, temperature not specified in the publication
-
0.06
Hordeum vulgare thioredoxin 2
pH 7.5, temperature not specified in the publication
-
0.00041
Hordeum vulgare thioredoxin 2 mutant E86A
mutant N139A, pH 7.5, temperature not specified in the publication
-
0.00057
Hordeum vulgare thioredoxin 2 mutant E86A
wild-type, pH 7.5, temperature not specified in the publication
-
0.0016
Hordeum vulgare thioredoxin 2 mutant E86A
mutant R140A, pH 7.5, temperature not specified in the publication
-
0.00112
Hordeum vulgare thioredoxin disulfide h1
-
pH 7.4, HvNTR2
-
0.00118
Hordeum vulgare thioredoxin disulfide h1
-
pH 7.4, HvNTR1
-
0.0009
Hordeum vulgare thioredoxin disulfide h2
-
pH 5.7, HvNTR2
-
0.00129
Hordeum vulgare thioredoxin disulfide h2
-
pH 7.4, HvNTR2
-
0.00145
Hordeum vulgare thioredoxin disulfide h2
-
pH 5.7, HvNTR1
-
0.00179
Hordeum vulgare thioredoxin disulfide h2
-
pH 7.4, HvNTR1
-
0.0019
Lipoamide
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
0.0043
Lipoamide
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
2.89
Lipoamide
wild type enzyme, in TE buffer, at 20°C
3.68
Lipoamide
mutant enzyme Y116I, in TE buffer, at 20°C
5.59
Lipoamide
mutant enzyme Y116T, in TE buffer, at 20°C
0.011
NADH
-
0.023
NADH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.0302
NADH
-
in 50 mM potassium phosphate buffer (pH 7.0), at 22°C
0.073
NADH
-
at pH 9.5 and 80°C
0.0806
NADH
truncated mutant, pH 7.2, temperature not specified in the publication
0.1
NADH
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.736
NADH
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
0.0004
NADPH
-
0.001
NADPH
-
cytosolic and mitochondrial TrxR1 isoform
0.0013
NADPH
pH 8.0, 30°C
0.0014
NADPH
-
pH 7.5, 50°C
0.0017
NADPH
pH 5.5, 60°C
0.0018
NADPH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.0022
NADPH
pH 7.0, 30°C
0.00235
NADPH
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.0045
NADPH
-
pH 7.0, 25°C, cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid)
0.0056
NADPH
pH 7.2, temperature not specified in the publication
0.006
NADPH
-
pH 7.8, 37°C
0.0063
NADPH
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
0.0125
NADPH
-
in 50 mM potassium phosphate buffer (pH 7.0), at 22°C
0.0224
NADPH
pH 7.2, temperature not specified in the publication
0.0247
NADPH
truncated mutant, pH 7.2, temperature not specified in the publication
0.088
NADPH
-
wild type enzyme
0.78
NADPH
-
at pH 6.5 and 80°C
1.1
NADPH
-
TrxR-16 mutant K29R/H108Y/A119N/V478E
2.4
NADPH
-
TrxR-16, TrxR lacking the last 16 C-terminal amino acids
3.3
NADPH
-
TrxR-16 mutant K29R
4.5
NADPH
-
TrxR-16 mutant K29R/H108Y
0.0025
reductase
-
thioredoxin from rat, bovine substrate
-
0.00031
thioredoxin
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.0004
thioredoxin
-
SeC498C mutant, human thioredoxin
0.00076
thioredoxin
assay with DTNB instead of NADPH
0.00076
thioredoxin
-
substrate: thioredoxin from E. coli
0.00088
thioredoxin
-
mutant C136S
0.0011
thioredoxin
-
recombinant enzyme
0.00125
thioredoxin
-
wild-type
0.00141
thioredoxin
-
rat thioredoxin as substrate
0.00157
thioredoxin
-
Escherichia coli thioredoxin as substrate
0.0017
thioredoxin
-
at 4°C
0.0017
thioredoxin
-
mutant C139S
0.00183
thioredoxin
-
human thioredoxin as substrate
0.002
thioredoxin
-
substrate wild-type, thioredoxin P34S, pH 8.0
0.00236
thioredoxin
-
human thioredoxin as substrate
0.0025
thioredoxin
-
substrate: thioredoxin from calf and rat
0.00256
thioredoxin
-
Escherichia coli thioredoxin as substrate
0.0028
thioredoxin
-
at 25°C
0.0037
thioredoxin
-
thioredoxin from rat
0.0047
thioredoxin
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.0051
thioredoxin
-
rat thioredoxin as substrate
0.006
thioredoxin
-
human thioredoxin
0.0062
thioredoxin
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.007
thioredoxin
-
cytosolic TrxR1 isoform
0.0085
thioredoxin
-
thioredoxin-1 from Anopheles gambiae, pH 7.4
0.009
thioredoxin
-
thioredoxin-2 from Drosophila melanogaster, pH 7.4
0.0144
thioredoxin
-
substrate: thioredoxin from E. coli
0.019
thioredoxin
-
mitochondrial TrxR1 isoform
0.033
thioredoxin
-
thioredoxin-1 from Plasmodium falciparum, pH 7.4
0.034
thioredoxin
-
thioredoxin from E. coli
0.036
thioredoxin
wild-type, thioredoxin from E. coli
0.0441
thioredoxin
pH 5.5, 60°C
0.045
thioredoxin
-
substrate: thioredoxin from E. coli
0.07
thioredoxin
-
E. coli thioredoxin
0.077
thioredoxin
-
thioredoxin from Escherichia coli, mutant TR-GCCS
0.1047
thioredoxin
-
in 100 mM potassium phosphate (pH 7.0), at 22°C
0.219
thioredoxin
-
thioredoxin from Escherichia coli, mutant TR-SCCS
0.61
thioredoxin
-
thioredoxin from Escherichia coli, wild type enzyme
6.6
thioredoxin
mutant enzyme U489C
35
thioredoxin
semisynthetic enzyme with 63% content of selenium
67.6
thioredoxin
semisynthetic enzyme with 91% content of selenium
0.0006
thioredoxin 2
-
wild type enzyme, pH and temperature not specified in the publication
-
0.0009
thioredoxin 2
-
mutant enzyme K137A, pH and temperature not specified in the publication
-
0.0023
thioredoxin 41
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
0.0036
thioredoxin 41
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
0.0028
thioredoxin 8
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
0.0029
thioredoxin 8
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
0.00099
thioredoxin disulfide
mutant enzyme Y116I, in TE buffer, at 20°C
0.00106
thioredoxin disulfide
mutant enzyme Y116T, in TE buffer, at 20°C
0.00143
thioredoxin disulfide
wild type enzyme, in TE buffer, at 20°C
0.0021
thioredoxin disulfide
pH 7.0, 30°C
0.0032
thioredoxin disulfide
purified, recombinant, tetrameric enzyme
0.0036
thioredoxin disulfide
purified, recombinant, dimeric enzyme
0.00637
thioredoxin disulfide
-
full length enzyme, in 50 mM potassium phosphate pH 7.0, at 25°C
0.0067
thioredoxin disulfide
pH 7.0, 30°C
0.017
thioredoxin disulfide
-
-
0.032
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence SCCS
0.0676
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCUG
0.086
thioredoxin disulfide
-
Methanosarcina acetivorans thioredoxin 7, cosubstrate: NADPH, pH and temperature not specified in the publication
0.123
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCCG
0.141
thioredoxin disulfide
full-length Drosophila enzyme with C-terminal sequence SCCS
0.173
thioredoxin disulfide
-
pH 7, 25°C
0.007
thioredoxin-1 disulfide
-
TrxR(cyto)
-
0.019
thioredoxin-1 disulfide
-
TRxR(mito)
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
additionally to the Arabidopsis thaliana thioredoxin, several other thioredoxins have been tested, Km-values
-
additional information
additional information
-
Km-values are pH-dependent
-
additional information
additional information
-
effects of paraquat on reaction kinetics of NADH and NADPH in lung cell extracts
-
additional information
additional information
KM-values of semisynthetic truncated mTR3 enzymes
-
additional information
additional information
-
KM-values of semisynthetic truncated mTR3 enzymes
-
additional information
additional information
-
KM-values of truncated enzymes forms
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.88 - 87.8
5,5'-dithio-bis(2-nitrobenzoic acid)
0.012 - 106.3
5,5'-dithiobis(2-nitrobenzoic acid)
24.1 - 174.3
5-hydroxy-1,4-naphthoquinone
3.9 - 15.3
Arabidopsis thaliana thioredoxin 3
-
20
Babesia bovis thioredoxin
pH 8.0, 30°C
-
11.7
ebsulfur
-
pH 7.5, temperature not specified in the publication
1.7
ebsulfur disulfide
-
pH 7.5, temperature not specified in the publication
4.1 - 9.4
Escherichia coli thioredoxin
-
12.1
Hordeum vulgare thioredoxin 1
wild-type, pH 7.5, temperature not specified in the publication
-
1.8 - 11.4
Hordeum vulgare thioredoxin 2
-
2.6 - 5.3
Hordeum vulgare thioredoxin 2 mutant E86A
-
7.9
Hordeum vulgare thioredoxin 2 mutant G57P
wild-type, pH 7.5, temperature not specified in the publication
-
15.9
Hordeum vulgare thioredoxin 2 mutant I51G
wild-type, pH 7.5, temperature not specified in the publication
-
2.25 - 3.26
Hordeum vulgare thioredoxin disulfide h1
-
0.43 - 2.98
Hordeum vulgare thioredoxin disulfide h2
-
1.183 - 6.08
hydrogen peroxide
1.8
lipoic acid
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
16.05
methaneseleninic acid
-
at pH 6.1 and 37°C
500
protein disulfide-isomerase
-
-
-
1.83
rat thioredoxin
-
insulin coupled assay
-
43.7
thioredoxin 1
-
wild type enzyme, pH and temperature not specified in the publication
42.9 - 47.1
thioredoxin 2
-
34
thioredoxin 3
-
wild type enzyme, pH and temperature not specified in the publication
-
2.6 - 2.7
thioredoxin 8
-
0.083 - 114.1
thioredoxin disulfide
2.2
thioredoxin disulfide 41
-
pH 7, 30°C
-
1.43
thioredoxin disulfide 8
-
pH 7, 30°C
-
22.7
thioredoxin K36E, thioredoxin P34S
-
mutant, pH 8.0
-
10.3
thioredoxin-CAC, thioredoxin-R
-
mutant, pH 8.0
-
additional information
additional information
-
0.88
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 7.2, temperature not specified in the publication
1.23
5,5'-dithio-bis(2-nitrobenzoic acid)
truncated mutant, pH 7.2, temperature not specified in the publication
10.7
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 7.2, temperature not specified in the publication
10.8
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 8.0, 30°C
11.96
5,5'-dithio-bis(2-nitrobenzoic acid)
-
pH 7.8, 37°C
87.8
5,5'-dithio-bis(2-nitrobenzoic acid)
-
pH 7.5, 50°C
0.012
5,5'-dithiobis(2-nitrobenzoic acid)
-
mutant U498C
0.018
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16 mutant K29R/H108Y/A119N/V478E
0.075
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16 mutant K29R/H108Y
0.23
5,5'-dithiobis(2-nitrobenzoic acid)
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.25
5,5'-dithiobis(2-nitrobenzoic acid)
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.52
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16 mutant K29R
0.55
5,5'-dithiobis(2-nitrobenzoic acid)
-
TrxR-16, TrxR lacking the last 16 C-terminal amino acids
0.62
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.62
5,5'-dithiobis(2-nitrobenzoic acid)
pH 7.5
1.2
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
1.6
5,5'-dithiobis(2-nitrobenzoic acid)
full-length Drosophila enzyme with C-terminal sequence SCCS
1.77
5,5'-dithiobis(2-nitrobenzoic acid)
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
2.23
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme
2.23
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
2.4
5,5'-dithiobis(2-nitrobenzoic acid)
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid
2.53
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
2.62
5,5'-dithiobis(2-nitrobenzoic acid)
-
pH 7, 25°C
2.62
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
5.5
5,5'-dithiobis(2-nitrobenzoic acid)
-
pH 7.4
8.28
5,5'-dithiobis(2-nitrobenzoic acid)
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
9
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
15.6
5,5'-dithiobis(2-nitrobenzoic acid)
truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid
16
5,5'-dithiobis(2-nitrobenzoic acid)
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
18.73
5,5'-dithiobis(2-nitrobenzoic acid)
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
20.83
5,5'-dithiobis(2-nitrobenzoic acid)
full-length mouse enzyme with C-terminal sequence GCUG
20.85
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
21.6
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
30.02
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C
33.08
5,5'-dithiobis(2-nitrobenzoic acid)
purified, recombinant, tetrameric enzyme
33.33
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme
47.72
5,5'-dithiobis(2-nitrobenzoic acid)
mutant enzyme Y116T, in TE buffer, at 20°C
48.42
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
49.87
5,5'-dithiobis(2-nitrobenzoic acid)
mutant enzyme Y116I, in TE buffer, at 20°C
70.3
5,5'-dithiobis(2-nitrobenzoic acid)
wild type enzyme, in TE buffer, at 20°C
106.3
5,5'-dithiobis(2-nitrobenzoic acid)
purified, recombinant, dimeric enzyme
24.1
5-hydroxy-1,4-naphthoquinone
wild type enzyme, in TE buffer, at 20°C
52.75
5-hydroxy-1,4-naphthoquinone
mutant enzyme Y116T, in TE buffer, at 20°C
174.3
5-hydroxy-1,4-naphthoquinone
mutant enzyme Y116I, in TE buffer, at 20°C
3.9
Arabidopsis thaliana thioredoxin 3
mutant G225R/G226D/P227V, pH 7.5, temperature not specified in the publication
-
4.8
Arabidopsis thaliana thioredoxin 3
wild-type, pH 7.5, temperature not specified in the publication
-
5
Arabidopsis thaliana thioredoxin 3
mutant G222D/A223G/G224E, pH 7.5, temperature not specified in the publication
-
5
Arabidopsis thaliana thioredoxin 3
mutant G225R/G226D, pH 7.5, temperature not specified in the publication
-
5.9
Arabidopsis thaliana thioredoxin 3
pH 7.5, temperature not specified in the publication
-
10.4
Arabidopsis thaliana thioredoxin 3
mutant W42A, pH 7.5, temperature not specified in the publication
-
10.7
Arabidopsis thaliana thioredoxin 3
mutant N45A/D46A, pH 7.5, temperature not specified in the publication
-
11
Arabidopsis thaliana thioredoxin 3
mutant W42A/M43A, pH 7.5, temperature not specified in the publication
-
14.8
Arabidopsis thaliana thioredoxin 3
mutant M43A, pH 7.5, temperature not specified in the publication
-
15.3
Arabidopsis thaliana thioredoxin 3
mutant Delta42-47, pH 7.5, temperature not specified in the publication
-
0.16
DTNB
-
mutant enzyme H509A
0.233
DTNB
-
mutant enzyme H509Q
4.58
DTNB
-
wild-type enzyme
50.3
DTNB
-
chimeric enzyme mutant, partly from Salmonella typhimurium AhpF protein
4.1
Escherichia coli thioredoxin
pH 8.0, 30°C
-
9.4
Escherichia coli thioredoxin
wild-type, pH 7.5, temperature not specified in the publication
-
1.8
Hordeum vulgare thioredoxin 2
mutant G225R/G226D/P227V, pH 7.5, temperature not specified in the publication
-
4.2
Hordeum vulgare thioredoxin 2
mutant N139A, pH 7.5, temperature not specified in the publication
-
5.1
Hordeum vulgare thioredoxin 2
mutant R140A, pH 7.5, temperature not specified in the publication
-
7.3
Hordeum vulgare thioredoxin 2
mutant N45A/D46A, pH 7.5, temperature not specified in the publication
-
7.9
Hordeum vulgare thioredoxin 2
mutant G222D/A223G/G224E, pH 7.5, temperature not specified in the publication
-
8
Hordeum vulgare thioredoxin 2
wild-type, pH 7.5, temperature not specified in the publication
-
8.1
Hordeum vulgare thioredoxin 2
mutant G225R/G226D, pH 7.5, temperature not specified in the publication
-
8.5
Hordeum vulgare thioredoxin 2
pH 7.5, temperature not specified in the publication
-
10.4
Hordeum vulgare thioredoxin 2
mutant W42A, pH 7.5, temperature not specified in the publication
-
11.4
Hordeum vulgare thioredoxin 2
mutant M43A, pH 7.5, temperature not specified in the publication
-
2.6
Hordeum vulgare thioredoxin 2 mutant E86A
mutant R140A, pH 7.5, temperature not specified in the publication
-
4.2
Hordeum vulgare thioredoxin 2 mutant E86A
mutant N139A, pH 7.5, temperature not specified in the publication
-
5.3
Hordeum vulgare thioredoxin 2 mutant E86A
wild-type, pH 7.5, temperature not specified in the publication
-
2.25
Hordeum vulgare thioredoxin disulfide h1
-
pH 7.4, HvNTR1
-
3.26
Hordeum vulgare thioredoxin disulfide h1
-
pH 7.4, HvNTR2
-
0.43
Hordeum vulgare thioredoxin disulfide h2
-
pH 5.7, HvNTR1
-
0.8
Hordeum vulgare thioredoxin disulfide h2
-
pH 5.7, HvNTR2
-
1.31
Hordeum vulgare thioredoxin disulfide h2
-
pH 7.4, HvNTR1
-
2.98
Hordeum vulgare thioredoxin disulfide h2
-
pH 7.4, HvNTR2
-
1.183
hydrogen peroxide
semisynthetic enzyme with 91% content of selenium
6.08
hydrogen peroxide
semisynthetic enzyme with 91% content of selenium
1.6
Lipoamide
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
2 - 3.7
Lipoamide
wild type enzyme, in TE buffer, at 20°C
3.3
Lipoamide
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
27.6
Lipoamide
mutant enzyme Y116I, in TE buffer, at 20°C
31.2
Lipoamide
mutant enzyme Y116T, in TE buffer, at 20°C
12
methylseleninate
-
recombinant protein
0.06
NADH
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.2
NADH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.2
NADH
truncated mutant, pH 7.2, temperature not specified in the publication
0.817
NADH
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
0.25
NADPH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.35
NADPH
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.59
NADPH
pH 7.2, temperature not specified in the publication
0.65
NADPH
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
0.97
NADPH
truncated mutant, pH 7.2, temperature not specified in the publication
6.4
NADPH
pH 7.2, temperature not specified in the publication
109.8
NADPH
-
pH 7.5, 50°C
0.016
thioredoxin
-
Escherichia coli thioredoxin as substrate
0.02
thioredoxin
mutant enzyme U489C
0.052 - 2.1
thioredoxin
-
thioredoxin from Escherichia coli, wild type enzyme
0.243
thioredoxin
-
SeC498C mutant enzyme, human thioredoxin
0.38
thioredoxin
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.5
thioredoxin
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.25
thioredoxin
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.3
thioredoxin
pH 5.5, 60°C
2.38
thioredoxin
-
mutant C136S
3.5
thioredoxin
-
human thioredoxin as substrate
4.03
thioredoxin
-
thioredoxin from Escherichia coli, mutant TR-SCCS
5.3
thioredoxin
-
thioredoxin from Escherichia coli, mutant TR-GCCS
5.58
thioredoxin
-
insulin coupled assay method
8.1
thioredoxin
-
human thioredoxin as substrate
10.17
thioredoxin
-
thioredoxin from Escherichia coli, wild type enzyme
13.2
thioredoxin
-
mutant C139S
14.3
thioredoxin
-
thioredoxin-2 from Drosophila melanogaster, pH 7.4
15.4
thioredoxin
-
thioredoxin-1 from Anopheles gambiae, pH 7.4
15.7
thioredoxin
-
thioredoxin-1 from Plasmodium falciparum, pH 7.4
19.97
thioredoxin
-
human thioredoxin as substrate
22
thioredoxin
-
wild-type
22.8
thioredoxin
-
wild-type, pH 8.0
25
thioredoxin
semisynthetic enzyme with 63% content of selenium
25.78
thioredoxin
-
human thioredoxin as substrate
27.4
thioredoxin
-
rat thioredoxin as substrate
29.5
thioredoxin
-
Escherichia coli thioredoxin as substrate
37
thioredoxin
semisynthetic enzyme with 91% content of selenium
37.88
thioredoxin
-
rat thioredoxin as substrate
41.7
thioredoxin
-
wild-type enzyme, human thioredoxin
46.57
thioredoxin
-
Escherichia coli thioredoxin as substrate
1030
thioredoxin
-
human thioredoxin
1300
thioredoxin
-
thioredoxin from E. coli
42.9
thioredoxin 2
-
wild type enzyme, pH and temperature not specified in the publication
-
47.1
thioredoxin 2
-
mutant enzyme K137A, pH and temperature not specified in the publication
-
2
thioredoxin 41
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
2.2
thioredoxin 41
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
2.6
thioredoxin 8
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
2.7
thioredoxin 8
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
0.083
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence SCCS
0.13
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCCG
1.175
thioredoxin disulfide
-
Methanosarcina acetivorans thioredoxin 7, cosubstrate: NADPH, pH and temperature not specified in the publication
4.99
thioredoxin disulfide
-
pH 7, 25°C
5.8
thioredoxin disulfide
full-length Drosophila enzyme with C-terminal sequence SCCS
7.7
thioredoxin disulfide
pH 7.0, 30°C
13.3
thioredoxin disulfide
pH 7.0, 30°C
19.2
thioredoxin disulfide
-
-
30
thioredoxin disulfide
-
full length enzyme, in 50 mM potassium phosphate pH 7.0, at 25°C
37
thioredoxin disulfide
full-length mouse enzyme with C-terminal sequence GCUG
40.98
thioredoxin disulfide
mutant enzyme Y116I, in TE buffer, at 20°C
44.85
thioredoxin disulfide
mutant enzyme Y116T, in TE buffer, at 20°C
47 - 73
thioredoxin disulfide
purified, recombinant, tetrameric enzyme
94.17
thioredoxin disulfide
wild type enzyme, in TE buffer, at 20°C
114.1
thioredoxin disulfide
purified, recombinant, dimeric enzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
wild-type and recombinant chimeric mutants in a coupled assay
-
additional information
additional information
-
transhydrogenase activity of mutants and wild-type enzyme with thioredoxin and FAD
-
additional information
additional information
turnover number of semisynthetic truncated mTR3 enzymes
-
additional information
additional information
-
turnover number of semisynthetic truncated mTR3 enzymes
-
additional information
additional information
-
turnover number of truncated enzyme forms
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.075 - 42
5,5'-dithio-bis(2-nitrobenzoic acid)
0.17 - 748.3
5,5'-dithiobis(2-nitrobenzoic acid)
7343 - 10620
5-hydroxy-1,4-naphthoquinone
282 - 12300
Arabidopsis thaliana thioredoxin 3
-
80
Babesia bovis thioredoxin
pH 8.0, 30°C
-
470
ebsulfur
-
pH 7.5, temperature not specified in the publication
60.5
ebsulfur disulfide
-
pH 7.5, temperature not specified in the publication
10 - 63.1
Escherichia coli thioredoxin
-
9840
Hordeum vulgare thioredoxin 1
wild-type, pH 7.5, temperature not specified in the publication
-
140 - 6800
Hordeum vulgare thioredoxin 2
-
1630 - 10200
Hordeum vulgare thioredoxin 2 mutant E86A
-
5490
Hordeum vulgare thioredoxin 2 mutant G57P
wild-type, pH 7.5, temperature not specified in the publication
-
1030
Hordeum vulgare thioredoxin 2 mutant I51G
wild-type, pH 7.5, temperature not specified in the publication
-
667
lipoic acid
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
34000
thioredoxin 1
-
wild type enzyme, pH and temperature not specified in the publication
52000 - 73000
thioredoxin 2
-
31000
thioredoxin 3
-
wild type enzyme, pH and temperature not specified in the publication
-
600 - 880
thioredoxin 41
-
890 - 950
thioredoxin 8
-
13.7 - 65940
thioredoxin disulfide
0.075
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 8.0, 30°C
0.1
5,5'-dithio-bis(2-nitrobenzoic acid)
truncated mutant, pH 7.2, temperature not specified in the publication
0.38
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 7.2, temperature not specified in the publication
4.33
5,5'-dithio-bis(2-nitrobenzoic acid)
pH 7.2, temperature not specified in the publication
42
5,5'-dithio-bis(2-nitrobenzoic acid)
-
pH 7.8, 37°C
0.17
5,5'-dithiobis(2-nitrobenzoic acid)
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.22
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
0.23
5,5'-dithiobis(2-nitrobenzoic acid)
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
4.78
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
5.27
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
5.45
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
21.2
5,5'-dithiobis(2-nitrobenzoic acid)
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
45.33
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
58.33
5,5'-dithiobis(2-nitrobenzoic acid)
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
95
5,5'-dithiobis(2-nitrobenzoic acid)
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
178
5,5'-dithiobis(2-nitrobenzoic acid)
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
183.3
5,5'-dithiobis(2-nitrobenzoic acid)
purified, recombinant, tetrameric enzyme
333.5
5,5'-dithiobis(2-nitrobenzoic acid)
-
wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C
495
5,5'-dithiobis(2-nitrobenzoic acid)
purified, recombinant, dimeric enzyme
513.3
5,5'-dithiobis(2-nitrobenzoic acid)
mutant enzyme Y116I, in TE buffer, at 20°C
526.7
5,5'-dithiobis(2-nitrobenzoic acid)
mutant enzyme Y116T, in TE buffer, at 20°C
748.3
5,5'-dithiobis(2-nitrobenzoic acid)
wild type enzyme, in TE buffer, at 20°C
7343
5-hydroxy-1,4-naphthoquinone
mutant enzyme Y116I, in TE buffer, at 20°C
7557
5-hydroxy-1,4-naphthoquinone
mutant enzyme Y116T, in TE buffer, at 20°C
10620
5-hydroxy-1,4-naphthoquinone
wild type enzyme, in TE buffer, at 20°C
282
Arabidopsis thaliana thioredoxin 3
mutant Delta42-47, pH 7.5, temperature not specified in the publication
-
361
Arabidopsis thaliana thioredoxin 3
mutant W42A/M43A, pH 7.5, temperature not specified in the publication
-
1050
Arabidopsis thaliana thioredoxin 3
mutant M43A, pH 7.5, temperature not specified in the publication
-
2550
Arabidopsis thaliana thioredoxin 3
mutant N45A/D46A, pH 7.5, temperature not specified in the publication
-
4240
Arabidopsis thaliana thioredoxin 3
mutant W42A, pH 7.5, temperature not specified in the publication
-
5340
Arabidopsis thaliana thioredoxin 3
mutant G225R/G226D/P227V, pH 7.5, temperature not specified in the publication
-
6000
Arabidopsis thaliana thioredoxin 3
wild-type, pH 7.5, temperature not specified in the publication
-
7460
Arabidopsis thaliana thioredoxin 3
mutant G225R/G226D, pH 7.5, temperature not specified in the publication
-
9620
Arabidopsis thaliana thioredoxin 3
mutant G222D/A223G/G224E, pH 7.5, temperature not specified in the publication
-
12300
Arabidopsis thaliana thioredoxin 3
pH 7.5, temperature not specified in the publication
-
10
Escherichia coli thioredoxin
pH 8.0, 30°C
-
63.1
Escherichia coli thioredoxin
wild-type, pH 7.5, temperature not specified in the publication
-
140
Hordeum vulgare thioredoxin 2
pH 7.5, temperature not specified in the publication
-
228
Hordeum vulgare thioredoxin 2
mutant W42A, pH 7.5, temperature not specified in the publication
-
713
Hordeum vulgare thioredoxin 2
mutant M43A, pH 7.5, temperature not specified in the publication
-
1490
Hordeum vulgare thioredoxin 2
mutant R140A, pH 7.5, temperature not specified in the publication
-
1710
Hordeum vulgare thioredoxin 2
mutant G225R/G226D/P227V, pH 7.5, temperature not specified in the publication
-
3300
Hordeum vulgare thioredoxin 2
mutant N45A/D46A, pH 7.5, temperature not specified in the publication
-
5410
Hordeum vulgare thioredoxin 2
mutant G222D/A223G/G224E, pH 7.5, temperature not specified in the publication
-
6180
Hordeum vulgare thioredoxin 2
mutant N139A, pH 7.5, temperature not specified in the publication
-
6330
Hordeum vulgare thioredoxin 2
mutant G225R/G226D, pH 7.5, temperature not specified in the publication
-
6800
Hordeum vulgare thioredoxin 2
wild-type, pH 7.5, temperature not specified in the publication
-
1630
Hordeum vulgare thioredoxin 2 mutant E86A
mutant R140A, pH 7.5, temperature not specified in the publication
-
9230
Hordeum vulgare thioredoxin 2 mutant E86A
wild-type, pH 7.5, temperature not specified in the publication
-
10200
Hordeum vulgare thioredoxin 2 mutant E86A
mutant N139A, pH 7.5, temperature not specified in the publication
-
5.6
Lipoamide
mutant enzyme Y116T, in TE buffer, at 20°C
7.5
Lipoamide
mutant enzyme Y116I, in TE buffer, at 20°C
372
Lipoamide
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
1737
Lipoamide
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
0.6
NADH
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
1.1
NADH
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
2.48
NADH
truncated mutant, pH 7.2, temperature not specified in the publication
84
NADH
-
with 5,5'-dithiobis(2-nitrobenzoicacid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
26.5
NADPH
pH 7.2, temperature not specified in the publication
103.3
NADPH
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
140
NADPH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
150
NADPH
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
398.5
NADPH
truncated mutant, pH 7.2, temperature not specified in the publication
1170
NADPH
-
pH 7.8, 37°C
1220
NADPH
pH 7.2, temperature not specified in the publication
75
thioredoxin
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
260
thioredoxin
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1230
thioredoxin
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
52000
thioredoxin 2
-
mutant enzyme K137A, pH and temperature not specified in the publication
-
73000
thioredoxin 2
-
wild type enzyme, pH and temperature not specified in the publication
-
600
thioredoxin 41
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
880
thioredoxin 41
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
890
thioredoxin 8
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
950
thioredoxin 8
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
13.7
thioredoxin disulfide
-
Methanosarcina acetivorans thioredoxin 7, cosubstrate: NADPH, pH and temperature not specified in the publication
1900
thioredoxin disulfide
pH 7.0, 30°C
3700
thioredoxin disulfide
pH 7.0, 30°C
14920
thioredoxin disulfide
purified, recombinant, tetrameric enzyme
31700
thioredoxin disulfide
purified, recombinant, dimeric enzyme
41450
thioredoxin disulfide
mutant enzyme Y116I, in TE buffer, at 20°C
42150
thioredoxin disulfide
mutant enzyme Y116T, in TE buffer, at 20°C
65940
thioredoxin disulfide
wild type enzyme, in TE buffer, at 20°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0018
(1E,4E)-1,5-bis(3,4-dihydroxyphenyl)penta-1,4-dien-3-one
Sus scrofa
-
pH 7.4, 25°C
0.0137
(1E,4E)-1,5-bis(3,5-di-tert-butyl-4-hydroxyphenyl)penta-1,4-dien-3-one
Sus scrofa
-
pH 7.4, 25°C
0.003
(1E,4E)-1,5-bis(3-bromo-4-hydroxy-5-methoxyphenyl)penta-1,4-dien-3-one
Sus scrofa
-
pH 7.4, 25°C
0.0017
(1E,4E)-1,5-bis(4-hydroxy-3,5-dimethoxyphenyl)penta-1,4-dien-3-one
Sus scrofa
-
pH 7.4, 25°C
0.0063
(1E,4E)-1,5-bis(4-hydroxyphenyl)penta-1,4-dien-3-one
Sus scrofa
-
pH 7.4, 25°C
0.0383
(1E,4Z,6E)-1,7-di-2-furyl-5-hydroxyhepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.05
(1E,4Z,6E)-1-(2-bromophenyl)-5-hydroxy-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0622
(1E,4Z,6E)-1-[4-(dimethylamino)phenyl]-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0003
(1E,4Z,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0016
(1E,4Z,6E)-5-hydroxy-1,7-bis(5-methyl-2-furyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0005
(1E,4Z,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(5-methyl-2-furyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.001
(1E,4Z,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-[5-(hydroxymethyl)-2-furyl]hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.02
(1E,4Z,6E)-5-hydroxy-1-(4-hydroxyphenyl)-7-(2-thienyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.02
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxy-3-methoxyphenyl)-1-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.057
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxy-3-methoxyphenyl)-1-phenylhepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0138
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxyphenyl)-1-(3,4,5-trimethoxyphenyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0233
(1E,4Z,6E)-5-hydroxy-7-(4-hydroxyphenyl)-1-phenylhepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.002
(1E,4Z,6E)-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]-1-(3,4,5-trimethoxyphenyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0008
(1E,4Z,6E)-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]-1-(4-methoxyphenyl)hepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0013
(1E,4Z,6E)-5-hydroxy-7-[5-(hydroxymethyl)-2-furyl]-1-phenylhepta-1,4,6-trien-3-one
Homo sapiens
-
pH 7.4, 37°C
0.0081
(2E,5E)-2,5-bis(3,4-dihydroxybenzylidene)cyclopentanone
Sus scrofa
-
pH 7.4, 25°C
0.0042
(2E,5E)-2,5-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)cyclopentanone
Sus scrofa
-
pH 7.4, 25°C
0.0033
(2E,5E)-2,5-bis(4-hydroxybenzylidene)cyclopentanone
Sus scrofa
-
pH 7.4, 25°C
0.0407
(2E,5E)-2,5-bis[(3,5-di-tert-butyl-4-hydroxyphenyl)methylidene]cyclopentanone
Sus scrofa
-
pH 7.4, 25°C
0.00052
(2E,5E)-2,5-bis[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]cyclopentanone
Sus scrofa
-
pH 7.4, 25°C
0.0048
(2E,6E)-2,6-bis(3,4-dihydroxybenzylidene)cyclohexanone
Sus scrofa
-
pH 7.4, 25°C
0.0089
(2E,6E)-2,6-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)cyclohexanone
Sus scrofa
-
pH 7.4, 25°C
0.0241
(2E,6E)-2,6-bis(4-hydroxybenzylidene)cyclohexanone
Sus scrofa
-
pH 7.4, 25°C
0.0453
(2E,6E)-2,6-bis[(3,4-dimethoxyphenyl)methylidene]cyclohexanone
Sus scrofa
-
pH 7.4, 25°C
0.0064
(2E,6E)-2,6-bis[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]cyclohexanone
Sus scrofa
-
pH 7.4, 25°C
0.0051
(2E,6E)-2-(4-hydroxybenzylidene)-6-(4-hydroxy-3-methoxybenzylidene)cyclohexanone
Homo sapiens
-
pH 7.4, 37°C
0.0249
(2E,6E)-2-[(4-hydroxyphenyl)methylidene]-6-[(3,4,5-trimethoxyphenyl)methylidene]cyclohexanone
Homo sapiens
-
pH 7.4, 37°C
0.0462
(3E,5E)-3,5-bis(3,4-dihydroxybenzylidene)piperidin-4-one
Sus scrofa
-
pH 7.4, 25°C
0.0046
(3E,5E)-3,5-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)piperidin-4-one
Sus scrofa
-
pH 7.4, 25°C
0.071
(3E,5E)-3,5-bis(4-hydroxybenzylidene)-4-oxopiperidinium
Sus scrofa
-
pH 7.4, 25°C
0.0306
(3E,5E)-3,5-bis[(3,4-dimethoxyphenyl)methylidene]piperidin-4-one
Sus scrofa
-
pH 7.4, 25°C
0.00086
(3E,5E)-3,5-bis[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]piperidin-4-one
Sus scrofa
-
pH 7.4, 25°C
0.0184
(3E,5E)-3-[(2,5-di-tert-butyl-4-hydroxyphenyl)methylidene]-5-[(3,5-di-tert-butyl-4-hydroxyphenyl)methylidene]piperidin-4-one
Sus scrofa
-
pH 7.4, 25°C
0.00007442
(4-ammoniothiophenolato)(2,2':6',2''-terpyridine)platinum(II) chloride
Homo sapiens
in 50 mM Tris-HCl, pH 8.0, at 37°C
-
0.00007002
(4-ammoniothiophenolato)(4'-toyl-2,2':6',2''-terpyridine)platinum(II) nitrate
Homo sapiens
in 50 mM Tris-HCl, pH 8.0, at 37°C
-
0.00006977
(4-hydroxylthiophenolato)(2,2':6',2''-terpyridine)platinum(II) chloride
Homo sapiens
in 50 mM Tris-HCl, pH 8.0, at 37°C
-
0.00005826
(4-hydroxylthiophenolato)(4'-toyl-2,2':6',2''-terpyridine)platinum(II) chloride
Homo sapiens
in 50 mM Tris-HCl, pH 8.0, at 37°C
-
0.00000096 - 0.00000406
(4-methylpyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
0.00000155 - 0.00000586
(4-methylpyrimidine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
0.00007426
(N-acetyl-4-aminothiophenolato)(2,2':6',2''-terpyridine)platinum(II) chloride
Homo sapiens
in 50 mM Tris-HCl, pH 8.0, at 37°C
-
0.00007786
(N-acetyl-4-aminothiophenolato)(4'-toyl-2,2':6',2''-terpyridine)platinum(II) nitrate
Homo sapiens
in 50 mM Tris-HCl, pH 8.0, at 37°C
-
0.00000161 - 0.00000412
(pyridine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
0.00000154 - 0.0000062
(pyridine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
0.00000192 - 0.00000673
(pyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
0.0005 - 0.004
1,1'-sulfanediylbis(2,4-dinitrobenzene)
0.02 - 0.15
1,1'-sulfanediylbis[2-nitro-4-(trifluoromethyl)benzene]
0.03 - 0.2
1,3-dinitro-5-(trifluoromethyl)benzene
0.2
1,4-dihydroxyanthroquinone
0.2
1,8-dihydroxyanthroquinone
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.00225
1-chloro-2,4-dinitrobenzene
Haemonchus contortus
-
pH 7.8, 37°C
0.00036
15-deoxy-D-12,14-PGJ2
Rattus norvegicus
-
0.06 mM, IC50: 0.00036 mM
0.0086
2-aminothiazolium [trans-tetrachlorobis(2-aminothiazole)ruthenate(III)]
Rattus norvegicus
-
0.017 - 0.0994
2-benzoyloxycinnamaldehyde
0.0636
2-benzyloxycinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.008 - 0.1
2-chloro-1,3-dinitro-5-(trifluoromethyl)benzene
0.0253
2-hydroxycinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.000146
2-hydroxymethyl-5-methoxy-1-methyl-3-[(2,4,6-trifluorophenoxy)methyl]indole-4,7-dione
Rattus norvegicus
-
in 100 mM potassium phosphate buffer, pH 7.4, at 22°C
0.1
2-pentoxycinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.02
3,4-estronequinone
Rattus norvegicus
-
0.032 mM, IC50: 0.02 mM
0.0083
3-(4-[[2-(1-hydroxy-4-oxocyclohexa-2,5-dien-1-yl)-1H-indol-1-yl]sulfonyl]phenyl)propanoic acid
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.0098
3-(4-[[6-fluoro-2-(1-hydroxy-4-oxocyclohexa-2,5-dien-1-yl)-1H-indol-1-yl]sulfonyl]phenyl)propanoic acid
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.01 - 0.08
4,5-dinitro-1,3-benzodioxole
0.002 - 0.01
4,6-dinitro-2,1,3-benzothiadiazole
0.0065
4-(1,3-benzothiazol-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.0761
4-(1,3-benzoxazol-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.1043
4-(1-benzothien-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.0063
4-(5-fluoro-1,3-benzothiazol-2-yl)-4-hydroxycyclohexa-2,5-dien-1-one
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.0038
4-hydroxy-2-nonenal
Rattus norvegicus
-
0.005-0.025 mM, IC50: 0.0038 mM, irreversible inhibition
0.0029
4-hydroxy-4-[1-(phenylsulfonyl)-1H-indol-2-yl]cyclohexa-2,5-dien-1-one
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.012
4-hydroxynonenal
Rattus norvegicus
-
0.06 mM, IC50: 0.012 mM
0.002 - 0.05
4-nitro-2,1,3-benzothiadiazole
0.0027
4-[6-fluoro-1-(phenylsulfonyl)-1H-indol-2-yl]-4-hydroxycyclohexa-2,5-dien-1-one
Rattus norvegicus
-
pH 7.5, determined after 60 min incubation of recombinant rat TrxR with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, irreversible
0.007 - 0.0844
5-fluoro-2-hydroxycinnamaldehyde
0.000082
5-methoxy-1,2-dimethyl-3-[1-oxo-2-(2,4,6-trifluorophenyl)ethyl]indole-4,7-dione
Rattus norvegicus
-
in 100 mM potassium phosphate buffer, pH 7.4, at 22°C
0.2
5-nitro-1,3-benzodioxole
Homo sapiens
-
IC50: 0.2 mM
0.01 - 0.09
5-nitro-2,1,3-benzothiadiazole
0.002 - 0.14
6,7-dinitroquinoxaline
0.04 - 0.2
6-nitroquinoxaline
0.019
Ag+
Meleagris gallopavo
-
pH 7.5, 50°C
0.0205
allyl isothiocyanate
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
0.00000074 - 0.00000245
auranofin
0.00012
aurothioglucose
Fasciola hepatica
-
IC50: 120 nM
0.0033
Benzyl isothiocyanate
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
0.529
Cd2+
Meleagris gallopavo
-
pH 7.5, 50°C
0.004
chaetocin
Homo sapiens
-
using 5,5'-dithiobis(2-nitrobenzoic acid) as substrate, in 100 mM potassium phosphate (pH 7.0), at 22°C
0.00023
chloro[N(4)-ortho-chlorophenyl-2-acetylpyridinethiosemicarbazonato]gold(III)dichloroaurate(I)
Rattus norvegicus
-
pH 7.0, 37°C
0.181 - 0.194
chrysophanol
0.38
diallyl disulfide
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
0.00016
dichloro[N(4)-ortho-chlorophenyl-2-acetylpyridinethiosemicarbazonato]antimony(III)
Rattus norvegicus
-
pH 7.0, 37°C
0.001
diphenylene iodonium
Mus musculus
-
IC50: 0.001 mM
0.61
Fe3+
Meleagris gallopavo
-
pH 7.5, 50°C
0.513
leukotriene A4 methyl ester
Rattus norvegicus
-
0.06 mM, IC50: 0.513 mM
0.0000171 - 0.000158
methylmercury
0.62
myricetin
Rattus norvegicus
-
0.05 mM, strong inhibitory effect, IC50: 0.62 mM
0.00035
palmarumycin CP1
Homo sapiens
-
0.001 mM, the naphthoquinone spiroketal fungal metabolite palmarumycin CP1 is a potent inhibitor of thioredoxin reductase-1, IC50: 0.00035 mM
0.075
phenethyl isothiocyanate
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
0.068
Prostaglandin A2
Rattus norvegicus
-
0.06 mM, IC50: 0.068 mM
0.0046 - 0.0079
pseudohypericin
0.0032
PX-911
Homo sapiens
-
0.001 mM, a water-soluble prodrug of a palmarumycin CP1 analogue, IC50: 0.0032 mM
0.00028
PX-916
Homo sapiens
-
0.001 mM, a water-soluble prodrug of a palmarumycin CP1 analogue, potent inhibitor of purified human thioredoxin reductase-1, IC50: 0.00028 mM
0.00027
PX-960
Homo sapiens
-
0.001 mM, a water-soluble prodrug of a palmarumycin CP1 analogue, IC50: 0.00027 mM
0.97
quercetin
Rattus norvegicus
-
0.05 mM, strong inhibitory effect, IC50: 0.97 mM
0.04
sulforaphane
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
0.06
theaflavin
Bos taurus
IC50 above 0.06 mM, in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.0191
theaflavin-3'-monogallate
Bos taurus
in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.0216
theaflavin-3,3'-digallate
Bos taurus
in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.018
theaflavin-3-monogallate
Bos taurus
in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.0015 - 0.01
trans,trans-curcumin
0.0713
trans-cinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.0238
trans-[bis(2-amino-5-methylthiazole)tetrachlororuthenate(III)]
Rattus norvegicus
-
0.00000167 - 0.00000682
trisodium (4,5-dihydro-1,3-thiazole-2-thiolato-kappaS2)[3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)]aurate(3-)
0.00000062 - 0.00000695
trisodium [3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)](pyrimidine-2-thiolato-kappaS)aurate(3-)
additional information
additional information
Homo sapiens
black tea extract and theaflavins (mixture of theaflavin, theaflavin-3-monogallate, theaflavin-3'-monogallate and theaflavin-3,3'-digallate) inhibit the purified TrxR1 with IC50 44 mg/ml and 21 mg/ml, respectively
-
0.00000096
(4-methylpyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000406
(4-methylpyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000155
(4-methylpyrimidine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000586
(4-methylpyrimidine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000161
(pyridine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000412
(pyridine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000154
(pyridine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.0000062
(pyridine-2-thiolato-kappaS)[1,1'-(1,3,7-triaza-5-phosphabicyclo[3.3.1]nonane-3,7-diyl-kappaP)diethanone]gold
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000192
(pyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000673
(pyrimidine-2-thiolato-kappaS)(1,3,5-triaza-7-phosphatricyclo[3.3.1.13,7]decane-kappaP)gold
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.0005
1,1'-sulfanediylbis(2,4-dinitrobenzene)
Plasmodium falciparum
-
IC50: 0.0005 mM
0.004
1,1'-sulfanediylbis(2,4-dinitrobenzene)
Homo sapiens
-
IC50: 0.004 mM
0.02
1,1'-sulfanediylbis[2-nitro-4-(trifluoromethyl)benzene]
Plasmodium falciparum
-
IC50: 0.02 mM
0.15
1,1'-sulfanediylbis[2-nitro-4-(trifluoromethyl)benzene]
Homo sapiens
-
IC50: 0.15 mM
0.03
1,3-dinitro-5-(trifluoromethyl)benzene
Plasmodium falciparum
-
IC50: 0.03 mM
0.2
1,3-dinitro-5-(trifluoromethyl)benzene
Homo sapiens
-
IC50: 0.2 mM
0.2
1,4-dihydroxyanthroquinone
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
1,4-dihydroxyanthroquinone
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.017
2-benzoyloxycinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.0994
2-benzoyloxycinnamaldehyde
Escherichia coli
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.008
2-chloro-1,3-dinitro-5-(trifluoromethyl)benzene
Plasmodium falciparum
-
IC50: 0.008 mM
0.1
2-chloro-1,3-dinitro-5-(trifluoromethyl)benzene
Homo sapiens
-
IC50: 0.1 mM
0.01
4,5-dinitro-1,3-benzodioxole
Plasmodium falciparum
-
IC50: 0.01 mM
0.08
4,5-dinitro-1,3-benzodioxole
Homo sapiens
-
IC50: 0.08 mM
0.002
4,6-dinitro-2,1,3-benzothiadiazole
Homo sapiens
-
IC50: 0.002 mM
0.01
4,6-dinitro-2,1,3-benzothiadiazole
Plasmodium falciparum
-
IC50: 0.01 mM
0.002
4-nitro-2,1,3-benzothiadiazole
Plasmodium falciparum
-
IC50: 0.002 mM
0.05
4-nitro-2,1,3-benzothiadiazole
Homo sapiens
-
IC50: 0.05 mM
0.007
5-fluoro-2-hydroxycinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.0844
5-fluoro-2-hydroxycinnamaldehyde
Escherichia coli
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
0.01
5-nitro-2,1,3-benzothiadiazole
Plasmodium falciparum
-
IC50: 0.01 mM
0.09
5-nitro-2,1,3-benzothiadiazole
Homo sapiens
-
IC50: 0.09 mM
0.002
6,7-dinitroquinoxaline
Plasmodium falciparum
-
IC50: 0.002 mM
0.14
6,7-dinitroquinoxaline
Homo sapiens
-
IC50: 0.14 mM
0.04
6-nitroquinoxaline
Plasmodium falciparum
-
IC50: 0.04 mM
0.2
6-nitroquinoxaline
Homo sapiens
-
IC50: 0.2 mM
0.18
aloe emodin
Rattus norvegicus
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
aloe emodin
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
aloin A
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
aloin A
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
anthrone
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
anthrone
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.00000074
auranofin
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000245
auranofin
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.181
chrysophanol
Rattus norvegicus
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.194
chrysophanol
Rattus norvegicus
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0025
Cu2+
Entamoeba histolytica
-
in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.46
Cu2+
Meleagris gallopavo
-
pH 7.5, 50°C
0.0036
curcumin
Rattus norvegicus
-
IC50: 0.0036 mM
0.0382
curcumin
Sus scrofa
-
pH 7.4, 25°C
0.2
frangulin A
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
frangulin A
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.049
hypericin
Rattus norvegicus
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.198
hypericin
Rattus norvegicus
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0000171
methylmercury
Mus musculus
-
TrxR from liver, pH and temperature not specified in the publication
0.000078
methylmercury
Mus musculus
-
TrxR from kidney, pH and temperature not specified in the publication
0.000158
methylmercury
Mus musculus
-
TrxR from brain, pH and temperature not specified in the publication
0.132
physcion
Rattus norvegicus
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.185
physcion
Rattus norvegicus
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0046
pseudohypericin
Rattus norvegicus
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0079
pseudohypericin
Rattus norvegicus
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.084
Rhein
Rattus norvegicus
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.123
Rhein
Rattus norvegicus
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
sennoside A
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
sennoside A
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
sennoside B
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
sennoside B
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
skyrin glucoside
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
skyrin glucoside
Rattus norvegicus
IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0015
trans,trans-curcumin
Homo sapiens
-
0.01-0.05 mM, IC50: 0.0015 mM, irreversible inhibition
0.0036
trans,trans-curcumin
Rattus norvegicus
-
IC50: 0.0036 mM, irreversible inhibition after incubation at room temperature for 2 h in vitro
0.01
trans,trans-curcumin
Homo sapiens
-
pH and temperature not specified in the publication
0.00000167
trisodium (4,5-dihydro-1,3-thiazole-2-thiolato-kappaS2)[3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)]aurate(3-)
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000682
trisodium (4,5-dihydro-1,3-thiazole-2-thiolato-kappaS2)[3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)]aurate(3-)
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000062
trisodium [3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)](pyrimidine-2-thiolato-kappaS)aurate(3-)
Homo sapiens
-
isoform TrxR1, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.00000695
trisodium [3,3',3''-(phosphanetriyl-kappaP)tribenzenesulfonato(3-)](pyrimidine-2-thiolato-kappaS)aurate(3-)
Homo sapiens
-
isoform TrxR2, in 0.2 M Na/K phosphate buffer (pH 7.4), at 37°C
0.0034
Zn2+
Entamoeba histolytica
-
in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
3.4
Zn2+
Meleagris gallopavo
-
pH 7.5, 50°C
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additional information
NTRC can be considered as a TRX that bears its own NTR, which might explain the high catalytic efficiency of the enzyme. The catalytically active form of NTRC is a homodimer arranged in a head-to-tail conformation, which interacts with 2-Cys PRXs through the TRX domain with high affinity for NADPH
drug target
anti-cancer target. Selenocysteine is important for the biological functions of mammalian TrxR and distinguishes it from prokaryotic thioredoxin reductases. Therefore it is a promising drug target
drug target
-
drug-resistant Staphylococcus aureus, especially methicillin-resistant (MRSA) and vancomycin-resistant Staphylococcus aureus (VRSA), pose a great threat to human health globally. The Trx system in GSH-deficient pathogens is a viable antibacterial drug target
drug target
-
ebselen as an inhibitor of thiol-dependent enzymes in pathogens
drug target
-
drug-resistant Staphylococcus aureus, especially methicillin-resistant (MRSA) and vancomycin-resistant Staphylococcus aureus (VRSA), pose a great threat to human health globally. The Trx system in GSH-deficient pathogens is a viable antibacterial drug target
-
evolution
based on sequence analysis, YpdA belongs to the pyridine nucleotide-disulfide oxidoreductase family of proteins that use flavin adenine dinucleotide (FAD) to transport reducing equivalents from NAD(P)H to cysteine residues
evolution
-
based on sequence analysis, YpdA belongs to the pyridine nucleotide-disulfide oxidoreductase family of proteins that use flavin adenine dinucleotide (FAD) to transport reducing equivalents from NAD(P)H to cysteine residues
-
evolution
-
based on sequence analysis, YpdA belongs to the pyridine nucleotide-disulfide oxidoreductase family of proteins that use flavin adenine dinucleotide (FAD) to transport reducing equivalents from NAD(P)H to cysteine residues
-
malfunction
-
ablation of cytosolic thioredoxin reductase (Txnrd1) or mitochondrial thioredoxin reductase (Txnrd2) yields embryonic lethal phenotypes
malfunction
-
cells deficient in isoformTR1 are particularly sensitive to diamide, while isoform TR3-knockdown cells are more sensitive to hydrogen peroxide
malfunction
-
in the absence of NTRC, imbalanced metabolic activities presumably modulate the chloroplast retrograde signals, leading to altered expression of nuclear genes and, ultimately, to the formation of the pleiotrophic phenotypes in ntrc mutant plants
malfunction
-
inhibition of mitochondrial thioredoxin reductase leads to oxidation of downstream enzymes such as thioredoxin and peroxiredoxin
malfunction
-
reporter gene transactivation by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. Decreased reporter gene activity in thioredoxin reductase null cells is due to reduced p53 specific activity rather than reduced p53 protein levels
malfunction
-
stable knockdown of TxnRd1 in both HeLa and FaDu cells nearly abolishes curcumin-mediated radiosensitization. TxnRd1 knockdown cells show decreased radiation-induced reactive oxygen species and sustained extracellular signal-regulated kinase 1/2 activation
malfunction
-
TrxR knocked out parasites are non-viable
malfunction
-
Txnrd1 knock-out cells cannot be rescued from glutathione depletion-induced cell death either by antioxidants, xCT overexpression, or co-culturing with xCT-overexpressing cells that condition the medium with Cys
malfunction
-
combined deficiencies of three thioredoxin m isoforms and NADPH-dependent thioredoxin reductase C (NTRC) leads to a cumulative decrease in leaf pigmentation, tetrapyrrole biosynthesis intermediate contents, 5-aminolevulinic acid synthesis rate, and Mg-protoporphyrin IX methyltransferase activity
malfunction
in plants with altered content of the NADPH-dependent chloroplast thioredoxin system, the strict correlation between lumenal pH and non-photochemical quenching is partially lost
malfunction
-
the disruption of the gene ntrC triggers a global change in the cellular physiology of A.7120 involving fluctuations in the proteome, metabolome and activities of antioxidant enzymes. However, the lack of NTRC does not drastically alter viability
malfunction
-
TRR1 deletion causes sensitivity to the inhibitors of the TORC1 pathway, such as rapamycin. This correlates with low Tor2p kinase levels and indicates a direct role of Trr1p in its stability. The autophagy caused by nitrogen starvation is reduced in the trr1DELTA mutant
malfunction
truncated polypeptides containing either the NTR or the TRX domain of NTRC showed that this novel enzyme could display both activities. Overexpression of 2-Cys PRXs, which has no significant effect in wild-type plants, resultes in further growth impairment in the ntrc mutant background (lacking individual TRXs), showing that the severity of the ntrc phenotype depends on 2-Cys PRXs levels. Very severe growth inhibition phenotypes of mutants combining the deficiencies of NTRC and TRXs f or x are also rescued by decreasing the contents of 2-Cys PRXs
malfunction
Trxrd2-/- cells are more susceptible to glutathione depletion. Loss of Trxrd2 results in enhanced peroxynitrite steady-state levels in both vascular endothelial cells and vessels
malfunction
YpdA overexpression confers greater resistance to stress. The YpdA G10A mutant protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium. Decreased fitness of the ypdA mutant results in reduced survival in neutrophils (PMNs). The ypdA mutant survives less well than the parent and the complemented mutant. The survival of SH1000 (BSH null strain), akin to the ypdA mutant, is also less than the parent and complemented mutant in this assay
malfunction
-
YpdA overexpression confers greater resistance to stress. The YpdA G10A mutant protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium. Decreased fitness of the ypdA mutant results in reduced survival in neutrophils (PMNs). The ypdA mutant survives less well than the parent and the complemented mutant. The survival of SH1000 (BSH null strain), akin to the ypdA mutant, is also less than the parent and complemented mutant in this assay
-
malfunction
-
in the absence of NTRC, imbalanced metabolic activities presumably modulate the chloroplast retrograde signals, leading to altered expression of nuclear genes and, ultimately, to the formation of the pleiotrophic phenotypes in ntrc mutant plants
-
malfunction
-
YpdA overexpression confers greater resistance to stress. The YpdA G10A mutant protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium. Decreased fitness of the ypdA mutant results in reduced survival in neutrophils (PMNs). The ypdA mutant survives less well than the parent and the complemented mutant. The survival of SH1000 (BSH null strain), akin to the ypdA mutant, is also less than the parent and complemented mutant in this assay
-
malfunction
-
reporter gene transactivation by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. Decreased reporter gene activity in thioredoxin reductase null cells is due to reduced p53 specific activity rather than reduced p53 protein levels
-
metabolism
-
the TrxR/thioredoxin pathway is of central importance in limiting cellular reactive oxygen species
metabolism
the enzyme is involved in a thioredoxin like system with thioredoxin reductase (PH1426). The redox potential of the redox protein is similar to that of thioredoxin from Escherichia coli and lower than that of glutathione
metabolism
Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. Bdr additionally functions as a bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. The BSH redox network comprised of three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. BrxC (YtxJ) is a monothiol bacilliredoxin and Bdr is bacilliredoxin reductase. DNA-binding transcription factor OhrR is inactivated by S-bacillithiolation. BrxB can regenerate active OhrR, with generation of BrxB-SSB. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. Following their inactivation, S-bacillithiolated OhrR (OhrR-SSB) and MetE (MetE-SSB) can be reduced by two bacilliredoxin (Brx) proteins, BrxA and BrxB. The enzyme is part of the BSH redox network comprising three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. Both BrxA and BrxB are dithiol class enzymes and are detected in vivo in their S-bacillithiolated forms after oxidative stress
metabolism
regulation of enzyme activity based on thiol-disulfide exchange is a regulatory mechanism in which the protein disulfide reductase activity of thioredoxins (TRXs) plays a central role. Plant chloroplasts are equipped with a complex set of up to 20 TRXs and TRX-like proteins, the activity of which is supported by reducing power provided by photosynthetically reduced ferredoxin (FDX) with the participation of a FDX-dependent TRX reductase (FTR). Therefore, the FDX-FTR-TRXs pathway allows the regulation of redox-sensitive chloroplast enzymes in response to light. In addition, chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. The NTRC gene encodes a polypeptide containing both NTR and TRX domains. NTRC is unique to oxygenic photosynthetic organisms. Both redox systems, NTRC and FDX-FTR-TRXs, participate in fine-tuning chloroplast performance in response to changes in light intensity. Participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxidase, in the control of the reducing activity of chloroplast TRXs as well as in the rapid oxidation of stromal enzymes upon darkness. Analysis of relationship of 2-Cys PRXs with NTRC and the FDX-FTR-TRXs redox systems for fine-tuning chloroplast performance in response to changes in light intensity and darkness, overview. The activity of thiol-dependent peroxidases (TPXs) relies on the disulfide reductase activity of NTRC, TRXs, and glutaredoxins (GRXs)
metabolism
the TrxR/Pdo redox cascade can use H2 as the electron donor when the frhAGB-encoded hydrogenase mediates electron transfer. When FrhAGB is replaced with FrhAG, it also catalyzes the reduction of Pdo with slightly weaker activity. The specific activity of the FrhAG hydrogenase is 40% lower than that of the FrhAGB hydrogenase
metabolism
-
Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. Bdr additionally functions as a bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. The BSH redox network comprised of three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. BrxC (YtxJ) is a monothiol bacilliredoxin and Bdr is bacilliredoxin reductase. DNA-binding transcription factor OhrR is inactivated by S-bacillithiolation. BrxB can regenerate active OhrR, with generation of BrxB-SSB. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. Following their inactivation, S-bacillithiolated OhrR (OhrR-SSB) and MetE (MetE-SSB) can be reduced by two bacilliredoxin (Brx) proteins, BrxA and BrxB. The enzyme is part of the BSH redox network comprising three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. Both BrxA and BrxB are dithiol class enzymes and are detected in vivo in their S-bacillithiolated forms after oxidative stress
-
metabolism
-
the enzyme is involved in a thioredoxin like system with thioredoxin reductase (PH1426). The redox potential of the redox protein is similar to that of thioredoxin from Escherichia coli and lower than that of glutathione
-
physiological function
Thermosynechococcus vestitus
-
NADPH thioredoxin reductase C functions as an electron donor to 2-Cys peroxiredoxin and transfers the reducing power from NADPH to the peroxiredoxin, which reduces peroxides in the cyanobacterium under oxidative stress
physiological function
-
NTRC is the most important pathway for chloroplast 2-Cys peroxiredoxins reduction, probably the only one during the night
physiological function
-
transcriptional activation of aniA and norB under microaerobic conditions is dependent on thioredoxin reductase, TrxB plays an important role in promoting the survival of gonococci during cervical infection
physiological function
Txnrd1 gene is essential for normal development during embryogenesis
physiological function
Txnrd2 gene is essential for normal development during embryogenesis
physiological function
-
glutathione deficiency can be rescued by forced expression of xCT (the substrate-specific subunit of the cystine/glutamate antiporter), which additionally requires the presence of functional isoform Txnrd1, but not isoform Txnrd2
physiological function
-
isoform Txnrd1 but not Txnrd2 is required for cerebellar development
physiological function
NTRC is maintained at a constant level during hardening and functions as an antioxidant with 2-Cys peroxiredoxin in the acquisition of freezing tolerance of Chlorella
physiological function
-
NTRC regulates several key processes, including chlorophyll biosynthesis and the shikimate pathway, in chloroplasts. NTRC has a critical role in the regulation of photoperiod-dependent metabolic and developmental processes in Arabidopsis
physiological function
-
the thioredoxin reductase-1 splice variant TXNRD1_v3 is an atypical inducer of cytoplasmic filaments and cell membrane filopodia. The glutaredoxin domain of TXNRD1_v3 is an atypical regulator of the cell cytoskeleton that potently induces formation of highly ordered cytoplasmic filaments and cell membrane filopodia
physiological function
-
the thioredoxin system has a large number of functions in DNA synthesis, defense against oxidative stress and apoptosis or redox signaling with reference to many diseases
physiological function
-
the thioredoxin system, comprising thioredoxin, thioredoxin reductase, and NADPH, is critical for cellular stress response, protein repair, and protection against oxidative damage
physiological function
-
the thioredoxin system, comprising thioredoxin, thioredoxin reductase, and NADPH, is critical for cellular stress response, protein repair, and protection against oxidative damage
physiological function
-
thioredoxin reductase 1 overexpression upregulates monocyte chemoattractant protein-1 release in human endothelial cells by 34%. TrxR1 enhances reactive oxygen species generation, NF-kappaB activity and subsequent monocyte chemoattractant protein-1 expression in endothelial cells, and may promote rather than prevent vascular endothelium from forming atherosclerotic plaque
physiological function
-
thioredoxin reductase-1 mediates curcumin-induced radiosensitization of squamous carcinoma cells. Overexpressing catalytically active TxnRd1 in HEK-293 cells, with low basal levels of TxnRd1, increases their sensitivity to curcumin alone and to the combination of curcumin and ionizing radiation
physiological function
-
Trr2/Trx3 and Trr2/GSH systems exhibit similar capacities for supporting peroxidredoxin 1 catalysis. TRR2 is required for cadmium and hydrogen peroxide resistance promoted by overexpression of peroxiredoxin 1
physiological function
-
TrxR helps maintenance of redox homeostasis in Plasmodium infection. TrxR is essential for the survival of erythrocytic stages of parasites
physiological function
TrxR1 plays a key role in protection against oxidant stress
physiological function
a double knockout mutant lacking NtrC and sulfiredoxin shows a phenotype similar to the NtrC mutant, while the sulfiredoxin mutant resembles wild-type plants. The deficiency of NtrC causes reduced overoxidation of 2-Cys peroxiredoxins, whereas the deficiency of sulfiredoxin has the opposite effect. The disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation. The overoxidation of chloroplast 2-Cys peroxiredoxins shows no circadian oscillation. The low level of 2-Cys peroxiredoxin overoxidation in the NtrC mutant is light dependent
physiological function
a knockout mutant strain displays higher level of reactive oxygen species in normal growth conditions. Oxidative stress treatments such as hydrogen peroxide, methyl-viologen or high light irradiance lead to an increase in the expression of genes related to reactive oxygen species detoxification, including NtrC and peroxiredoxin genes, with a concomitant increase in the amount of NtrC and 2-Cys peroxiredoxin. The mutant shows a pronounced overoxidation of 2-Cys peroxiredoxin and a time-delay recovery of its reduced form upon oxidative stress treatments
physiological function
Arabidopsis thaliana NtrC knockout mutants show lower magnesium protoporphyrin IX and magnesium protoporphyrin IX monomethylester steady-state levels, the substrate and the product of protoporphyrin IX methyltransferase CHLM preceding MgPMME cyclase, while protoporphyrin IX strongly accumulates in mutant leaves after 5-aminolevulinic acid feeding. The mutant has a reduced capacity to synthesize 5-aminolevulinic acid and reduced CHLM activity compared with the wild-type. The contents of glutamyl-transfer RNA reductase1 and CHLM are reduced. NtrC physically interacts with glutamyl-transfer RNA reductase1 and CHLM. NtrC mutant plants contain partly oxidized CHLM, the wild-type has only reduced CHLM
physiological function
Arabidopsis thaliana plants lacking NtrC tolerate high light intensities, display drastically elevated non-photochemical quenching component qE, have larger trans-thylakoid pH differences and have 10fold higher zeaxanthin levels under low and medium light intensities. A double-knockout mutant, lacking additionally photosystem II component PsbS, is devoid of qE. This double mutant grows faster than the NtrC mutant and has a higher chlorophyll content. The photosystem II activity is partially restored, and linear electron transport rates under low and medium light intensities are twice as high as compared with plants lacking NtrC alone
physiological function
growth rate of isoform Ntr1 mutants is significantly lower than that of control cells
physiological function
growth rate of isoform Ntr2 mutants is significantly lower than that of control cells
physiological function
HepG2 cells utilize cytosolic thioredoxin reductase TrxR1 and thioredoxin to defend against the high glucose/palmitate-mediated increase in reactive oxygen species. Enhanced TrxR1/thioredoxin palmitoylation occurs in parallel with a decrease in their activities
physiological function
-
loss of glutathione reductase, thioredoxin reductase and thioredoxin peroxidase-encoding genes results in strains severely attenuated in their ability to grow in rice cells and that fail to produce spreading necrotic lesions on the leaf surface. The thioredoxin proteins contribute to cell-wall integrity. Glutathione and thioredoxin gene expression, under axenic growth conditions, is dependent on both the presence of glucose and the sugar/NADPH sensor Tps1
physiological function
mutants lacking both NtrC and thioredoxin Trxs f, which participate in metabolic redox regulation, or, to a lower extent Trx x, which has antioxidant function, show severe growth-retarded phenotypes, decreased photosynthesis performance, and almost abolished light-dependent reduction of fructose-1,6-bisphosphatase. The combined deficiency of both redox systems provokes aberrant chloroplast ultrastructure. Both the NtrC-Trx f1f2 and NtrC-trx x mutants show high mortality at the seedling stage, which is overcome by the addition of an exogenous carbon source
physiological function
overexpression of isoform NTRC in Arabidopsis thaliana leads to a freezing and cold stress tolerance, whereas a knockout mutant shows a stress-sensitive phenotype. The recombinant NTRC proteins exhibits a cryoprotective activity for malate dehydrogenase and lactic dehydrogenase. Recombinant NTRC efficiently protect RNA and DNA from RNase A and metal catalyzed oxidation damage, respectively. The C-terminal thioredoxin domain is required for the nucleic acid-protein complex formation
physiological function
overexpression wild-type NtrC promotes plant growth by increasing leaf size and biomass yield of the rosettes. Complementation of the mutant with the full-length NtrC gene containing an active reductase but an inactive Trx domain, or vice versa, recovers wild-type chloroplast phenotype and, partly, rosette biomass production
physiological function
plants lacking functional NtrC show localized cell death accompanied by elevated accumulation of hydrogen peroxide in response to Pseudomonas syringae pathogens. The NtrC mutant shows enhanced bacterial growth and disease susceptibility of pathogens and elevated jasmonic acid-mediated signaling pathways in response to Pseudomonas syringae pathogens
physiological function
the enhanced NtrC transcript expression upon methyl viologen treamtment confers oxidative stress tolerance. Overexpressing plants show extreme drought tolerance with lower water loss compared to wild-type and NtrC mutant strains. Drought-responsive genes such as RD29A and DREB2A are enhanced in overexpressing strains by drought, compared to wild-type and NtrC mutant strains
physiological function
the NtrC-dependent redox regulation of CHLI-1 ATPase contributes to the chlorophyll-deficient phenotype of NtrC mutants
physiological function
-
the thioredoxin system plays a major role in releasing the L chain of tetanus neurotoxin and botulinum neurotoxins after their translocation across the membrane of the endocytic vesicle
physiological function
Trx1 shows reversible association with tissue factor in human serum and plasma samples. The association is dependent on Trx1 residue Cys73 that bridges tissue factor residue Cys209 via a disulfide bond. Trx1 Cys73 is absolutely required for Trx1 to interfere with factor FVIIa binding to purified and cell-surface tissue factor, consequently suppressing tissue factor-dependent procoagulant activity and proteinase-activated receptor-2 activation. Trx1/TrxR plays an important role in sensing the alterations of NADPH/NADP+ states and transducing this redox-sensitive signal into changes in tissue factor activity. With NADPH, Trx1/TrxR facilitates the reduction of tissue factor, causing a decrease in tissue factor activity, with NADP+, Trx1/TrxR promotes the oxidation of tissue factor, leading to an increase in its activity
physiological function
-
under cadmium stress conditions, NTR activity and thioredoxin h3 and thioredoxin h4 expression are stimulated, while the overall activity of thioredoxin decreases. When incubated with Cd ions in vitro, the disulfide reductase activity of thioredoxin h3 and f isoforms is drastically inhibited. The NADPH status is also affected, since cadmium treatment provokes an increase in oxidized state of coenzyme as compared to control redox ratio
physiological function
Bdr (YpdA) functions as an NADPH-dependent bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue
physiological function
chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. Redox regulation is an additional layer of control of the signaling function of the chloroplast. Redox regulation based on dithiol-disulfide interchange constitutes an essential regulatory mechanism that allows the rapid adaptation of chloroplast metabolism to light
physiological function
-
cytosolic thioredoxin reductase 1 is required for correct folding of proteins entering the endoplasmic reticulum, in the reconstituted translation/translocation system as well as in intact cells grown in culture
physiological function
enzyme YpdA participates in stress response upon exposure to specific physiologically relevant stresses. Role of YpdA in regulating BSH and BSSB levels, the enzyme is responsible for the recycling of oxidized bacillithiol disulfide (BSSB) to the reduced form (BSH). Enzyme YpdA plays in protecting Staphylococcus aureus cells from the oxidative killing by human neutrophils (PMNs)
physiological function
redox regulation in heterotrophic organisms relies on NADPH, thioredoxins, and an NADPH-dependent TRX reductase (NTR). NTRC-dependent regulation of 2-Cys peroxiredoxin (PRX) is critical for optimal function of the photosynthetic apparatus
physiological function
-
role of the enzyme (NTRC) in the regulation of the NADPH pool. Biological significance of NTRC in oxidative stress management. NTRC is not involved in the membrane organization process
physiological function
the enzyme (NTRC) plays a crucial role in the activation of the NDH-dependent electron flow in darkness (chlororespiration) and during dark to light transitions. The enzyme stimulates the activity of NDH-dependent cyclic electron flow and is involved in the regulation of generation of proton motive force, thylakoid conductivity to protons, and redox balance between the thylakoid electron transfer chain and the stroma during changes in light conditions
physiological function
the enzyme (TrxR) can use NADPH to reduce thioredoxin disulfide which passes the reducing equivalent to its downstream substrates involved in various biomedical events, such as ribonucleotide reductase for deoxyribonucleotide and DNA synthesis, or peroxiredoxins for counteracting oxidative stress
physiological function
the mitochondrial thioredoxin/peroxiredoxin system encompasses NADPH, thioredoxin reductase 2 (TrxR2), thioredoxin 2, and peroxiredoxins 3 and 5 (Prx3 and Prx5) and is crucial to regulate cell redox homeostasis via the efficient catabolism of peroxides. Endothelial TrxR2 controls both the steady-state concentration of peroxynitrite, the product of the reaction of superoxide radical and nitric oxide, and the integrity of the vascular system
physiological function
the NADPH-dependent chloroplast thioredoxin system (NTRC) contributes to downregulation of a slow-relaxing constituent of NPQ, whose induction is independent of lumenal acidification. Overexpression of NTRC enhances the ability to adjust the excitation balance between photosystem II (PSII) and photosystem I (PSI), and improves the ability to oxidize the electron transfer chain during changes in light conditions
physiological function
-
the thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. This reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system
physiological function
thioredoxin reductase system provides the minimal cytosolic components required for reducing proteins within the ER lumen
physiological function
-
thioredoxin reductase Trr1p controls TORC1-regulated processes. The TORC1 complex promotes growth and protein synthesis when nutrients, particularly amino acids, are abundant. It also represses catabolic processes, like autophagy, which are activated during starvation
physiological function
TrxR from the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H. In Thermococcus onnurineus NA1, the frhAGB-encoded hydrogenase, a homologue of the F420-reducing hydrogenase of methanogens, interacts with thioredoxin reductase (TrxR). Electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to TrxR and reduced Pdo (protein disulfide oxidoreductase, UniProt ID B6YTB7), a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR is 7fold less efficient than when NADPH is the electron donor. TrxR can use H2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NADPH in Thermococcus onnurineus strain NA. The frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologue, F420-reducing hydrogenases of methanogens. The TrxR (TON_1603) of the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is a typical prokaryotic NADP-dependent thioredoxin reductase (NTR) with a preference for NADPH over NADH. The TrxR/Pdo redox couple is capable of reducing cystine to cysteine, which subsequently reduced dimethyl sulfoxide (DMSO) to dimethylsulfide (DMS). Because growth is enhanced by substituting DMSO for elemental sulfur (S0) as an electron sink for excess reducing power
physiological function
-
transcriptional activation of aniA and norB under microaerobic conditions is dependent on thioredoxin reductase, TrxB plays an important role in promoting the survival of gonococci during cervical infection
-
physiological function
-
enzyme YpdA participates in stress response upon exposure to specific physiologically relevant stresses. Role of YpdA in regulating BSH and BSSB levels, the enzyme is responsible for the recycling of oxidized bacillithiol disulfide (BSSB) to the reduced form (BSH). Enzyme YpdA plays in protecting Staphylococcus aureus cells from the oxidative killing by human neutrophils (PMNs)
-
physiological function
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Bdr (YpdA) functions as an NADPH-dependent bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue
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physiological function
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NTRC regulates several key processes, including chlorophyll biosynthesis and the shikimate pathway, in chloroplasts. NTRC has a critical role in the regulation of photoperiod-dependent metabolic and developmental processes in Arabidopsis
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physiological function
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the thioredoxin system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin (Trx), is one of the major disulfide reductase systems used by bacteria against oxidative stress. This reductase system is crucial for the survival of the pathogenic bacterium Staphylococcus aureus, which lacks a natural glutathione/glutaredoxin (Grx) system
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physiological function
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NTRC is maintained at a constant level during hardening and functions as an antioxidant with 2-Cys peroxiredoxin in the acquisition of freezing tolerance of Chlorella
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physiological function
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enzyme YpdA participates in stress response upon exposure to specific physiologically relevant stresses. Role of YpdA in regulating BSH and BSSB levels, the enzyme is responsible for the recycling of oxidized bacillithiol disulfide (BSSB) to the reduced form (BSH). Enzyme YpdA plays in protecting Staphylococcus aureus cells from the oxidative killing by human neutrophils (PMNs)
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C142A
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mutant shows reduced reductase activity compared to the wild type enzyme
C142S
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mutant shows reduced reductase activity compared to the wild type enzyme
C145A
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mutant shows reduced reductase activity compared to the wild type enzyme
C145S
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mutant shows reduced reductase activity compared to the wild type enzyme
A164G/R183F
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the mutant shows reduced activity but is still able to dimerize though with an increase in intermediary forms
A164G/V182E
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the mutant shows increased activity compared to the wild type enzyme
A164G/V182E/R183F
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the mutant shows reduced activity compared to the wild type enzyme but is still able to dimerize though with an increase in intermediary forms
C140S
no activity with substrate CHLI-1 ATPase
C120A/C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C122A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A/C120A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A/C120A/C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C14A/C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C220A
site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
C122A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C14A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C14A/C120A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C14A/C220A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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C220A
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site-directed mutagenesis, the mutant retains NADPH oxidase activity, but with reduced activity compared to the wild-type enzyme
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TR-GCCS
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mutant with C-terminal sequence of GCCS
TR-SCCS
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mutant with C-terminal sequence of SCCS
C489S
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mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C489S/C490S
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mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C490S
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mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
E469A
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the mutant retains 28% of the wild type activity
E469Q
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the mutant retains 35% of the wild type activity
E470A
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the mutant retains 70% of the wild type activity
H106F
catalytic activity drops considerably yet pH-profile does not reveal differences
H106N
catalytic activity drops considerably yet pH-profile does not reveal differences
H106Q
catalytic activity drops considerably yet pH-profile does not reveal differences
C135S/C32S
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via the active disulfide centers a subunit complex of tightly bound enzyme, C135 and C138, and thioredoxin, C32 and C35, is formed, exchange of one cysteine for one serine in each protein by site-directed mutagenesis, conformation analysis
C135S/C35S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C136S
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site-directed mutagenesis, reduced activity
C138S/C35S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C139S
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site-directed mutagenesis, reduced activity
C535S
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site-directed mutagenesis, changed conformation
C73S
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recombinant, His-tagged
TrxR-16
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truncated form of TrxR missing the last 16 C-terminal amino acids, without thioredoxin-reducing activity
TrxR-16 K29R
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without thioredoxin-reducing activity
TrxR-16 K29R/H108Y
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without thioredoxin-reducing activity
TrxR-16 K29R/H108Y/A119N/V478E
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without thioredoxin-reducing activity
U498C
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1.4fold higher GSSG-reducing activity compared to the TrxR-16 enzyme
C145S
active site cysteine residue. Kinetic data
C148S
residue Cys148 probably performs an initial nucleophilic attack on the active site disulfide in thioredoxin disulfide. Kinetic data
Delta42-47
FAD-domain mutant. Kinetic data
G222D/A223G/G224E
NADPH-domain mutant. Kinetic data
G225R/G226D
NADPH-domain mutant. Kinetic data
G225R/G226D/P227V
NADPH-domain mutant. Kinetic data
M43A
mutant in a loop of the FAD-binding domain, strongly affects the interaction with thioredoxin. Kinetic data
N139A
NADPH-domain mutant. Kinetic data
N45A/D46A
FAD-domain mutant. Kinetic data
R140A
NADPH-domain mutant. Kinetic data
W42A
mutant in a loop of the FAD-binding domain, strongly affects the interaction with thioredoxin. Kinetic data
W42A/M43A
mutant in a loop of the FAD-binding domain, strongly affects the interaction with thioredoxin
Sec489C
pH-optimum shifts from pH 7.0 to 8.0
U489C
barely detectable activity towards thioredoxin and hydrogen peroxide
C535S
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construction of a homodimer and heterodimer, the latter containing 1 mutant and 1 wild-type subunit, activity is reduced by 56 and 92%, respectively
C535S/C88A
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double mutant, construction of a homodimer and a heterodimer, the latter containing 1 mutant and 1 wild-type subunit, activity is reduced by 89 and 95%, respectively
C88S
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site-directed mutagenesis, no activity
C93A
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site-directed mutagenesis, no activity
H509A
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site-directed mutagenesis, reduced activity
H509Q
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site-directed mutagenesis, reduced activity
C146S
no activity against insulin disulfide, no DTNB-reducing activity
C35S
strong activity as high as that of a wild type against insulin disulfide, 98% of residual activity. The activity of C35S against the reduction of DTNB was not decreased
C146S
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no activity against insulin disulfide, no DTNB-reducing activity
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C35S
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strong activity as high as that of a wild type against insulin disulfide, 98% of residual activity. The activity of C35S against the reduction of DTNB was not decreased
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C458S
inactive mutant of SCCS
C458S/C475T
inactive mutant of SCCS
C475T
inactive mutant of SCCS
SCCS
mutant with flanking serine residues introduced into the C-terminal tetrapeptide of the wild type enzyme, less than 0.5% activity of the wild type enzyme
SeC498C
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antisense technique, exchange in the catalytic active selenosulfide at the C-terminus, resulting in higher pH-optimum, 100fold lower turnover number, 10fold lower Km-value, no activity with H2O2
SeC498G
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antisense technique, reduced activity
SeC498S
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antisense technique, reduced activity
U498C
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specific activity of 50% of wild-type enzyme
Y116F
the mutant protein is not soluble
K137A
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the mutation does not alter enzyme activity
C57S
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inactive mutant containing a redox-active [Fe4S4]3+/2+ center, can be reduced by dithionite
C87A
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inactive mutant containing a redox-inactive [Fe4S4]2+ cluster
C53S
site-directed mutagenesis, no activity since the redox cycle system is abolished
C135S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C135S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 138 is remaining
C138S
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C138S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C138S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 135 is remaining, very low activity
C32S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C32S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 35 is remaining, low activity
C35S
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fluorescence spectroscopic investigation of the interaction with the flavin group
C35S
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exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 32 is remaining
C88A
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site-directed mutagenesis, no activity
C88A
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construction of a homodimer and a heterodimer, the latter containing 1 mutant and 1 wild-type subunit, activity is reduced by 4 and 90%
Y116I
the mutation decreases sensitivity to inhibition by cisplatin and lowers catalytic efficiency in reduction of thioredoxin compared to the wild type enzyme
Y116I
the mutation decreases sensitivity to inhibition by cisplatin, lowers catalytic efficiency in reduction of thioredoxin, and increases turnover using 5-hydroxy-1,4-naphthoquinone (juglone) as substrate compared to the wild type enzyme
C147A
significantly reduced activity, decrease in FAD content
C147A
the mutant exhibits a marginal NADH oxidase activity with FAD canonically bound to the enzyme
C147A
in the active site of the C147A mutant, which exhibits a marginal NADH oxidase activity, the FAD is canonically bound to the enzyme
G10A
site-directed mutagenesis, the mutation completely abolishes cofactor binding activity as glycine 10 is the first glycine residue in a putative Rossman fold domain (GxGxxG), which is characteristic of cofactor binding enzymes and presumed to function in the reduction of oxidized bacillithiol disulfide (BSSB). The YpdA G10A protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium
G10A
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site-directed mutagenesis, the mutation completely abolishes cofactor binding activity as glycine 10 is the first glycine residue in a putative Rossman fold domain (GxGxxG), which is characteristic of cofactor binding enzymes and presumed to function in the reduction of oxidized bacillithiol disulfide (BSSB). The YpdA G10A protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium
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G10A
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site-directed mutagenesis, the mutation completely abolishes cofactor binding activity as glycine 10 is the first glycine residue in a putative Rossman fold domain (GxGxxG), which is characteristic of cofactor binding enzymes and presumed to function in the reduction of oxidized bacillithiol disulfide (BSSB). The YpdA G10A protein is unable to consume NADPH or NADH. Carbohydrate metabolism is mostly down regulated in the mutant, reduced fitness of the ypdA mutant in the competitive fitness assays with the wild-type in chemical defined medium
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additional information
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where insertion of alanine between the redox-active Cys residues of the C-terminal redox center has very little effect on DTNB reductase activity
additional information
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His-tagged transcript specific mutants, varied N-terminus, 1 null-mutant
additional information
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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When the C-terminus of DmTR is changed from a carboxylate to either a thiocarboxylate or a hydroxamic acid, the result is a mutant enzyme with an about 1.7fold increase in activity with thioredoxin. Alanine insertion mutants (DmTR-SCACS and DmTR-SCAACS) show activity with thioredoxin that is greatly reduced compared to that of wild-type DmTR. Increasing the ring size of the Cys-Cys dyad results in a 150-300fold loss in kcat, while the Km is affected little. The 5,5'-dithiobis(2-nitrobenzoic acid) reductase activity of DmTR is also increased when the negative charge at the C-terminus is either neutralized by converting the carboxylate to a neutral hydroxamic acid or modulated by conversion to a thiocarboxylate. Similar to the Sec-containing mammalian enzyme, the truncated DmTR mutant also shows very high 5,5'-dithiobis(2-nitrobenzoic acid) reductase activity, as do the alanine insertion mutants
additional information
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additional information
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trxB gene is combined to chimeric enzyme NT-TrR by exchanging the N-terminus of Escherichia coli with the N-terminus of Salmonella typhimurium AhpF gene protein, which encodes a protein with about 35% homology in the N-terminal region, 2 other mutants are constructed in the same way but with double mutation C129S/C132S and C342S/C345S, the first in the Escherichia coli part and the latter in the Salmonella part of the chimeric protein, activity corressponding to organism wild-type giving the N-terminal part, except for C342S/C345S chimeric mutant who has no activity
additional information
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transposon mutagenesis
additional information
expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
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expression as a truncated form without both the plastid-targetingpeptide and Trx domain
additional information
the mutant in the which Sec and Cys residues are switched (TR-GUCG), shows activity similar to that of the Sec489Cys mutant (TR-GCCG). Replacement of the Cys-Sec dyad with a Sec-Sec dyad (TR-GUUG) results in a mutant enzyme with very low catalytic activity. Even if the kcat values are normalized for selenium content, the TR-GUCG and TR-GUUG mutants have catalytic activity 90fold and 185fold lower, respectively, than that of the wild-type enzyme. The mutants in which alanine residues are inserted to increase the ring size (TR-GCAUG and TR-GCAAUG) show only a modest decrease in catalytic activity, 6fold and 4fold, respectively
additional information
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the mutant in the which Sec and Cys residues are switched (TR-GUCG), shows activity similar to that of the Sec489Cys mutant (TR-GCCG). Replacement of the Cys-Sec dyad with a Sec-Sec dyad (TR-GUUG) results in a mutant enzyme with very low catalytic activity. Even if the kcat values are normalized for selenium content, the TR-GUCG and TR-GUUG mutants have catalytic activity 90fold and 185fold lower, respectively, than that of the wild-type enzyme. The mutants in which alanine residues are inserted to increase the ring size (TR-GCAUG and TR-GCAAUG) show only a modest decrease in catalytic activity, 6fold and 4fold, respectively
additional information
the truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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the truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid shows no activity with thioredoxin disulfide + NADPH
additional information
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thioredoxin is cut off the native fusion protein thioredoxin-thioredoxin reductase resulting in enhanced activity
additional information
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truncated enzyme mutant without catalytic active C-terminus
additional information
mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
additional information
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mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
additional information
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mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
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additional information
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mutation of gene ypdA by replacing the ORF with a kanamycin cassette through homologous recombination in an SH1000 strain corrected for BSH production, and construction of the complement strain by replacing the kanamycin cassette with the native ypdA gene, phenotypes, overview. No obvious growth defect of the mutant vs. the parent or the complemented mutant in TSB is detected. Fitness defects might be masked by other metabolic pathways in rich media that neutralize the effect of stress. Accordingly, the fitness of the ypdA mutant is evaluated by a competition assay which has been shown to be useful for teasing out subtle fitness defects between closely related strains. Despite identical growth kinetics of the mutant vs. the parent in complex media such as TSB and CDM, overnight competition assays reveal that the wild-type strain out-competes the ypdA mutant in competitive growth in CDM, while the competitive index does not change in TSB media. These results suggest that while the ypdA mutation has a limited effect on growth in complex media in vitro, the mutant exhibits a fitness defect vs. the wild-type when grown competitively in chemically defined medium. Cells overexpressing YpdA are able to survive better than cells with just the empty vector, and this difference in survival is abolished when oxidative burst of PMNs is blocked by DPI
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