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Enzyme Nomenclature
Information on EC 1.8.1.9 - thioredoxin-disulfide reductase
Word Map on EC 1.8.1.9
- 1.8.1.9
- selenium
- peroxidase
-
selenoproteins
- selenocysteine
- superoxide
- peroxiredoxins
- gsh
- catalase
- glutaredoxins
-
anticancer
- auranofin
-
selenoenzyme
- hydroperoxide
-
redox-active
- fad
-
ribonucleotide
- dithiols
-
flavoproteins
- dtnb
-
flavoenzyme
-
thioredoxin-like
-
se-deficient
- sulforaphane
-
iodothyronine
-
deiodinases
-
selenocysteine-containing
-
selenolate
-
redox-sensitive
- thioredoxin-1
-
thiol-disulfide
-
secis
-
selenium-containing
-
deoxyribonucleotides
-
thiol-dependent
-
selenium-deficient
-
organoselenium
- selenomethionine
- lipoamide
-
thiol-based
-
se-dependent
- trypanothione
-
redox-regulated
- ebselen
- 1-chloro-2,4-dinitrobenzene
-
thioredoxin-dependent
- diselenide
-
selenium-dependent
-
thioltransferase
- medicine
- analysis
-
n-heterocyclic
- selenophosphate
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.1.9
-
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RECOMMENDED NAME
GeneOntology No.
thioredoxin-disulfide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
A flavoprotein (FAD).; light
-
-
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
catalytic mechanism
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
UV-light radical reduction mechanism
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
UV-light radical reduction mechanism
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
inhibition mechanism
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
catalytic mechanism; oxidation-reduction cycle of thioredoxin
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
three-dimensional structure
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
catalytic mechanism; oxidation-reduction cycle of thioredoxin
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH; inhibition mechanism
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
catalytic mechanism; electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
2 conformations possible, termed FR and FO conformation, which differ in their fluorescence spectroscopic behaviour, their accessibility for inhibitors and in the efficiency of electron transfer to FAD, involving position 138 in the wild-type and the mutant C138S; electron transfer in the enzyme complex of apoenzyme, FAD and thioredoxin with NADPH
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
oxidation-reduction cycle of thioredoxin
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
oxidation-reduction cycle of thioredoxin
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
conformational change upon reduction wth NADPH or tris-(2-carboxyethyl)phosphine
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
oxidation-reduction cycle of thioredoxin
-
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
catalytic mechanism
-
-
thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+
catalytic mechanism
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
additional information
-
the enzyme utilizes oxygen, requires NADH or NADPH, and readily generates the reduced paraquat radical
reduction
-
-
-
-
reduction
-
reduction of the thioredoxin disulfide in two sequential one-electron steps using a [Fe2S2]2+/+ ferredoxin as the electron donor
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
thioredoxin:NADP+ oxidoreductase
A flavoprotein (FAD).
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CAS REGISTRY NUMBER
COMMENTARY
9074-14-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
393993, 394747, 394904, 394908, 394913, 394918, 394922, 394928, 394931, 394933, 394935, 394946, 394948, 394950, 394951, 394952, 394953, 659211, 659480, 687454, 698055
-
-
-
394906, 394908, 394909, 394911, 394917, 394934, 394940, 394941, 394944, 394947, 658795, 659211, 672588, 673655, 674452, 674618, 675564, 675915, 685442, 685557, 686259, 686636, 686863, 686897, 687225, 688735, 688929, 689444, 689720, 689751, 696439, 698055, 710896, 711069, 711283, 711672, 711755, 711966, 712064, 712072, 712944, 713067, 724685, 725059
-
-
-
658794, 684845, 684906, 685032, 685436, 686324, 687171, 687762, 688358, 689060, 689708, 696492, 697613, 698054, 712655
SwissProt
-
394922, 394947, 674618, 674898, 677195, 686139, 686563, 686894, 688590, 696235, 696435, 697613, 710835, 711146, 711369, 712944, 724278
-
-
transgenic mice with cardiac-specific expression of a dominant-negative 14-3-3h protein mutant (DN 14-3-3h) after induction of experimental diabetes. Marked downregulation of thioredoxin reductase in DN 14-3-3h mice compared to wild-type mice after induction of diabetes
-
-
-
394921, 394930, 394942, 659211, 672906, 672938, 674192, 674452, 677197, 684858, 686938, 687621, 696235, 698055, 710835, 711101, 711342, 711966, 712072, 712446, 712943, 712944, 713067, 726048
-
-
involvement of thioredoxin reductase in the dimethyl sulphoxide reductase system
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
the TrxR/thioredoxin pathway is of central importance in limiting cellular reactive oxygen species
physiological function
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
-
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
-
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
-
inhibition of mitochondrial thioredoxin reductase leads to oxidation of downstream enzymes such as thioredoxin and peroxiredoxin
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
-
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
-
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
-
physiological function
-
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
-
isoform Txnrd1 but not Txnrd2 is required for cerebellar development
physiological function
-
Txnrd1 gene is essential for normal development during embryogenesis; Txnrd2 gene is essential for normal development during embryogenesis
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
-
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
-
NTRC is the most important pathway for chloroplast 2-Cys peroxiredoxins reduction, probably the only one during the night
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
-
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 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
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
-
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
TrxR1 plays a key role in protection against oxidant stress
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
-
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
-
TrxR helps maintenance of redox homeostasis in Plasmodium infection. TrxR is essential for the survival of erythrocytic stages of parasites
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
-
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
-
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
-
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
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-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
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol
2-nitro-5-thiobenzoate + oxidized dithiothreitol
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoicacid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
Entamoeba histolytica thioredoxin disulfide 41 + NADPH + H+
Entamoeba histolytica thioredoxin 41 + NADP+
-
-
-
-
?
Escherichia coli thioredoxin disulfide + NADPH + H+
Escherichia coli thioredoxin + 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
-
-
?
methylseleninate + NADPH
CH3SeH + NADP+
-
also utilizes glutathione instead of NADPH
-
ir
NADPH + thioredoxin disulfide
NADP+ + thioredoxin
-
mechanism, Cys57 attacks Cys490 in the interchange reaction between the N-terminal dithiol and the C-terminal disulfide
-
-
?
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 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
?
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 + 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 3 + NADP+
thioredoxin 3 disulfide + NADPH + H+
-
-
-
-
?
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'-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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
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+
-
-
-
-
?
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+
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+
-
-
-
-
?
juglone + NADPH + H+
?
-
isoform TrxR2 displays strikingly lower activity with juglone compared to isoform TrxR1
-
-
?
methylseleninate + H2O2
?
-
addition of selenocysteine increases the activity by 20%
-
-
?
NADPH + H+ + ubiquinone-10
NADP+ + ubiquinol-10
-
HEK cells overexpressing TrxR1 reduce ubiquinone-10
-
-
?
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
-
radical reduction, prevention of cells from UV-generated free radical caused damage on the skin
-
-
?
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
-
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
-
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
-
-
-
-
?
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
-
-
?
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
-
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
-
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
-
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
-
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
-
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+
-
i.e. DTNB
-
-
?
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+
-
in presence of NADPH, coupled assay
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
?
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+
-
i.e. DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
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 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 + NADH + H+
thioredoxin + NAD+
-
-
-
-
?
thioredoxin disulfide + NADH + H+
thioredoxin + NAD+
MtNTRC can use either NADPH or NADH as cofactors
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
thioredoxin-1 from Anopheles gambiae or Plasmodium falciparum, thioredoxin-2 from Drosophila melanogaster
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
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+
-
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+
MtNTRC can use either NADPH or NADH as cofactors
-
-
?
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+
-
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+
-
-
-
-
?
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
?
-
-
thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis
-
-
-
additional information
?
-
-
specific for NADPH, B side of nicotinamide ring
-
-
-
additional information
?
-
-
the enzyme does not reduce hydrogen peroxide or insulin
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
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 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
?
-
-
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
?
-
-
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
?
-
-
the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin
-
-
-
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 is endowed with an additional NADH oxidase activity
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADPH + H+ + ubiquinone-10
NADP+ + ubiquinol-10
-
HEK cells overexpressing TrxR1 reduce ubiquinone-10
-
-
?
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 3 + NADP+
thioredoxin 3 disulfide + NADPH + H+
-
-
-
-
?
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
-
defense against oxidative stress
-
-
?
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
-
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
-
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
-
detoxification of hydrogen peroxide, protection of the cell against oxidative damage
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
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 + NADH + H+
thioredoxin + NAD+
-
-
-
-
?
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+
-
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+
O89049, Q9Z0J5
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
P29509
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
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
?
-
-
thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis
-
-
-
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
?
-
-
thioredoxin reductase is essential for formate dehydrogenase H production and for labelling the formate dehydrogenase H polypeptide with 75Se-selenite
-
-
-
additional information
?
-
Q16881
HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
-
-
-
additional information
?
-
Q16881
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
?
-
-
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
?
-
-
the enzyme can promote oxidative stress by redox cycling of paraquat: paraquat + O2 + NADPH + H+ --> paraquat radical + O2- radical + NADP+
-
-
-
additional information
?
-
-
ribonucleotide reductase, thioredoxin and thioredoxin reductase constitute a system necessary for the biosynthesis of deesoxyribonucleotides
-
-
-
additional information
?
-
O89049
mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity
-
-
-
additional information
?
-
-
the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin
-
-
-
additional information
?
-
-
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
wild-type and chimeric mutants partly from Salmonella typhimurium AhpF protein
FAD
wild-type, 0.7 mol per mol of subunit, mutant C147A, 0.3 mol per mol of subunit
FAD
-
the flavin (FAD/FADH2) and disulfide/dithiol couples are very close in thermodynamic potentials
FAD
-
-
394921, 394930, 394942, 394945, 698053, 710835, 711101, 711146, 711342, 711966, 712072, 712446, 712943, 712944
FAD
-
-
FAD
-
-
394911, 394923, 394934, 394939, 394940, 394941, 394944, 394945, 394947, 394954, 672588, 710896, 711146, 711283, 711672, 711755, 711966, 712064, 712072, 712655, 712944, 725059
NADPH
-
; approximately four times more activity was evident with NADPH when compared to NADH
NADPH
-
-
NADPH
-
-
394747, 394904, 394905, 394908, 394910, 394913, 394918, 394922, 394928, 394931, 394933, 394935, 394946, 394948, 394951, 394952, 394953, 659480, 698055, 713481
NADPH
-
-
394922, 394945, 394947, 685151, 685189, 686563, 690139, 696235, 696435, 697613, 710835, 711146, 711369, 712944, 724278
NADPH
-
higher affinity and catalytic efficiency with NADPH compared to NADH
NADPH
-
the catalytic efficiency with NADPH is 2500fold higher than with NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Na2SeO3
enhances hepatic TrxR1 activity, but only on the condition that it causes liver injury
Selenite
-
selenium treatment results in increased expression of almost all TrxR1 mRNA variants with increasing concentrations of selenite
selenium
selenocysteine
additional information
selenium
-
the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
-
the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
-
the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
-
TrxR1 contains a selenocysteine in the active site (Gly-Cys-SeCys-Gly)
selenium
-
selenoprotein, expression and function depends on adequate supply of selenium; selenoprotein, expression and function depends on adequate supply of selenium
selenium
-
the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
-
thioredoxin reductase is a selenoprotein; thioredoxin reductase is a selenoprotein
selenium
-
the enzyme possesses selenium in the form of selenocysteine in the active site
selenium
selenoprotein. TrxR1 is more sensitive to Se depletion than TrxR2, greater changes in liver than kidney. There is a prioritisation of TrxR2 over TrxR1 during Se deficiency such that TrxR1 expression is more sensitive to Se supply than TrxR2 but this sensitivity of TrxR1 is not fully accounted for by TrxR1 5' or 3'-untranslated region sequences when assessed using luciferase reporter constructs
selenium
-
the presence of a selenium atom is not chemically required to catalyze the reduction of the disulfide bond of thioredoxin
selenium
-
TrxR1 is a selenoprotein that contains a selenocysteine residue at the penultimate C-terminal
selenium
-
thioredoxin reductase 1 is a selenoprotein, the oxidized enzyme presents a selenenylsulfide motif in trans-configuration, with the selenium atom of selenocysteine-498 positioned beneath the side chain of Tyr-116
selenium
-
the enzyme possesses selenium in the form of selenocysteine in the active site
selenium
-
all three isoenzymes of mammalian TrxR contain an essential selenocysteine residue, which is the target of several drugs in cancer treatment or mercury intoxication
selenocysteine
-
contains selenocysteine as part of the redox active selenosulfide in the active center; encoded by TGA stop codon
selenocysteine
-
contains selenocysteine as part of the redox active selenosulfide in the active center
selenocysteine
-
contains selenocysteine as part of the redox active selenosulfide in the active center; heparin affinity depends on the selenium content, binding can be induced by reduction of the enzyme with NADPH or tris-(2-carboxyethyl)phosphine; isoform 1 contains 1 selenium per subunit, the mitochondrial isoform 2 contains 0.5 selenium per subunit
selenocysteine
-
contains selenocysteine as part of the redox active selenosulfide in the active center; encoded by TGA stop codon
additional information
-
not a selenoenzyme, but instead contains a highly unusual redox-active Cys-Cys sequence
additional information
-
TrxR-1(cyto) is not a selenoprotein; TrxR-1(mito) is not a selenoprotein
additional information
-
DmTR shows high catalytic activity without the presence of a selenocysteine
additional information
-
DmTR shows high catalytic activity without the presence of a selenocysteine
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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-(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-[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,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-[(2,5-di-tert-butyl-4-hydroxyphenyl)methylidene]-5-[(3,5-di-tert-butyl-4-hydroxyphenyl)methylidene]piperidin-4-one
-
-
(4-ammoniothiophenolato)(4'-toyl-2,2':6',2''-terpyridine)platinum(II) nitrate
-
-
-
(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
-
-
1,2-[bis(1,2-benzisoselenazolone-3(2H)-ketone)]ethane
-
apoptosis induced by the inhibitor is through Bcl-2/Bax and caspase-3 pathways
2-aminothiazolium [trans-tetrachlorobis(2-aminothiazole)ruthenate(III)]
-
-
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-hydroxy-2-nonenal
-
0.005-0.025 mM, IC50: 0.0038 mM, irreversible inhibition; 0.05 mM, remarkable lost inhibition
4-[6-fluoro-1-(phenylsulfonyl)-1H-indol-2-yl]-4-hydroxycyclohexa-2,5-dien-1-one
-
-
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
chaetocin
-
competitive inhibitor with anticancer effects, complete inhibition at 0.015 mM
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
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
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
NAD+
-
NAD+ acts as poor competitive inhibitor respect to both NADPH and NADH
palmarumycin CP1
-
0.001 mM, the naphthoquinone spiroketal fungal metabolite palmarumycin CP1 is a potent inhibitor of thioredoxin reductase-1, IC50: 0.00035 mM
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
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
reactive oxygen species
-
0.1 mM, ROS generated by xanthine/xanthine oxidase enhance the inhibitory effect of flavonoids
-
sulforaphane
-
0.04 mM, 50% inhibition after 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
trans-[bis(2-amino-5-methylthiazole)tetrachlororuthenate(III)]
-
selective inhibition of TrxR1
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-)
-
-
[(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-nitro-4-(trifluoromethyl)benzene]
-
IC50: 0.02 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; 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
-
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-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
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
-
-
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
-
-
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
-
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
aurothioglucose
-
about 90% residual activity after 8 h at 0.005 mM, about 80% residual activity after 8 h at 0.05 mM
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
-
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
-
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
-
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
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+
-
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
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
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
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
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
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
trans,trans-curcumin
-
IC50: 0.0036 mM, irreversible inhibition after incubation at room temperature for 2 h in vitro
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
-
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
-
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.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
C-terminal redox active disulfide; part of the active site
cysteine
-
1 pair of redox active cysteines at the N-terminal active center and 1 pair of selenenylsulfide at the C-terminus, crucial for the reduction of thioredoxin
EDTA
-
if the concentration of EDTA in the reaction mixture is higher than 0.1 mM the enzyme shows full activity
EDTA
-
if the concentration of EDTA in the reaction mixture is higher than 0.1 mM the enzyme shows full activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.25
dithionitrobenzene
-
pH and temperature not specified in the publication
2.5
H2O2
-
wild-type enzyme, Km-value can be reduced by addition of selenocysteine
0.0027
lipoic acid
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
0.0013
thioredoxin 1
-
wild type enzyme, pH and temperature not specified in the publication
0.0011
thioredoxin 3
-
wild type enzyme, pH and 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
0.09
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
0.45
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
0.71
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
0.83
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)
-
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
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
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
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
0.023
NADH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.1
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
0.0018
NADPH
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.00235
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)
0.0063
NADPH
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
0.00031
thioredoxin
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.0047
thioredoxin
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.0062
thioredoxin
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.61
thioredoxin
-
thioredoxin from Escherichia coli, wild type enzyme
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
-
0.00637
thioredoxin disulfide
-
full length enzyme, in 50 mM potassium phosphate pH 7.0, at 25°C
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
additional information
additional information
-
Km-values are pH-dependent
-
additional information
additional information
-
additionally to the Arabidopsis thaliana thioredoxin, several other thioredoxins have been tested, Km-values
-
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 truncated enzymes forms
-
additional information
additional information
-
KM-values of semisynthetic truncated mTR3 enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
43.7
thioredoxin 1
Saccharomyces cerevisiae
-
wild type enzyme, pH and temperature not specified in the publication
34
thioredoxin 3
Saccharomyces cerevisiae
-
wild type enzyme, pH and temperature not specified in the publication
-
0.018
5,5'-dithiobis(2-nitrobenzoic acid)
Homo sapiens
-
TrxR-16 mutant K29R/H108Y/A119N/V478E
0.23
5,5'-dithiobis(2-nitrobenzoic acid)
Entamoeba histolytica
-
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)
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.55
5,5'-dithiobis(2-nitrobenzoic acid)
Homo sapiens
-
TrxR-16, TrxR lacking the last 16 C-terminal amino acids
1.2
5,5'-dithiobis(2-nitrobenzoic acid)
Schistosoma mansoni
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C
1.6
5,5'-dithiobis(2-nitrobenzoic acid)
Drosophila melanogaster
-
full-length Drosophila enzyme with C-terminal sequence SCCS
1.77
5,5'-dithiobis(2-nitrobenzoic acid)
Solanum lycopersicum
-
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)
Caenorhabditis elegans
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
2.4
5,5'-dithiobis(2-nitrobenzoic acid)
Drosophila melanogaster
-
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)
Caenorhabditis elegans
-
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)
Drosophila melanogaster
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
8.28
5,5'-dithiobis(2-nitrobenzoic acid)
Homo sapiens
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
15.6
5,5'-dithiobis(2-nitrobenzoic acid)
Mus musculus
-
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)
Schistosoma mansoni
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
18.73
5,5'-dithiobis(2-nitrobenzoic acid)
Homo sapiens
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
20.83
5,5'-dithiobis(2-nitrobenzoic acid)
Mus musculus
-
full-length mouse enzyme with C-terminal sequence GCUG
20.85
5,5'-dithiobis(2-nitrobenzoic acid)
Mus musculus
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
21.6
5,5'-dithiobis(2-nitrobenzoic acid)
Drosophila melanogaster
-
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)
Homo sapiens
-
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)
Rattus norvegicus
-
purified, recombinant, tetrameric enzyme
47.72
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
mutant enzyme Y116T, in TE buffer, at 20°C
48.42
5,5'-dithiobis(2-nitrobenzoic acid)
Mus musculus
-
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)
Rattus norvegicus
-
mutant enzyme Y116I, in TE buffer, at 20°C
70.3
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
wild type enzyme, in TE buffer, at 20°C
106.3
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
purified, recombinant, dimeric enzyme
24.1
5-hydroxy-1,4-naphthoquinone
Rattus norvegicus
-
wild type enzyme, in TE buffer, at 20°C
52.75
5-hydroxy-1,4-naphthoquinone
Rattus norvegicus
-
mutant enzyme Y116T, in TE buffer, at 20°C
174.3
5-hydroxy-1,4-naphthoquinone
Rattus norvegicus
-
mutant enzyme Y116I, in TE buffer, at 20°C
50.3
DTNB
Escherichia coli
-
chimeric enzyme mutant, partly from Salmonella typhimurium AhpF protein
0.06
NADH
Solanum lycopersicum
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.2
NADH
Entamoeba histolytica
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.817
NADH
Methanosarcina acetivorans
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
0.25
NADPH
Entamoeba histolytica
-
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
Solanum lycopersicum
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.65
NADPH
Methanosarcina acetivorans
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
0.052 - 2.1
thioredoxin
Caenorhabditis elegans
-
thioredoxin from Escherichia coli, wild type enzyme
0.38
thioredoxin
Solanum lycopersicum
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.5
thioredoxin
Entamoeba histolytica
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.25
thioredoxin
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
10.17
thioredoxin
Caenorhabditis elegans
-
thioredoxin from Escherichia coli, wild type enzyme
42.9
thioredoxin 2
Saccharomyces cerevisiae
-
wild type enzyme, pH and temperature not specified in the publication
-
47.1
thioredoxin 2
Saccharomyces cerevisiae
-
mutant enzyme K137A, pH and temperature not specified in the publication
-
2
thioredoxin 41
Entamoeba histolytica
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
2.2
thioredoxin 41
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
2.6
thioredoxin 8
Entamoeba histolytica
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
2.7
thioredoxin 8
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
-
0.083
thioredoxin disulfide
Mus musculus
-
full-length mouse enzyme with C-terminal sequence SCCS
0.13
thioredoxin disulfide
Mus musculus
-
full-length mouse enzyme with C-terminal sequence GCCG
1.175
thioredoxin disulfide
Methanosarcina acetivorans
-
Methanosarcina acetivorans thioredoxin 7, cosubstrate: NADPH, pH and temperature not specified in the publication
5.8
thioredoxin disulfide
Drosophila melanogaster
-
full-length Drosophila enzyme with C-terminal sequence SCCS
30
thioredoxin disulfide
Schistosoma mansoni
-
full length enzyme, in 50 mM potassium phosphate pH 7.0, at 25°C
37
thioredoxin disulfide
Mus musculus
-
full-length mouse enzyme with C-terminal sequence GCUG
additional information
additional information
Escherichia coli
-
transhydrogenase activity of mutants and wild-type enzyme with thioredoxin and FAD
-
additional information
additional information
Escherichia coli
-
wild-type and recombinant chimeric mutants in a coupled assay
-
additional information
additional information
Drosophila melanogaster
-
turnover number of truncated enzyme forms
-
additional information
additional information
Mus musculus
-
turnover number of semisynthetic truncated mTR3 enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
667
lipoic acid
Homo sapiens
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
2025
34000
thioredoxin 1
Saccharomyces cerevisiae
-
wild type enzyme, pH and temperature not specified in the publication
3921
31000
thioredoxin 3
Saccharomyces cerevisiae
-
wild type enzyme, pH and temperature not specified in the publication
42630
0.17
5,5'-dithiobis(2-nitrobenzoic acid)
Entamoeba histolytica
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
221
0.22
5,5'-dithiobis(2-nitrobenzoic acid)
Drosophila melanogaster
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
221
0.23
5,5'-dithiobis(2-nitrobenzoic acid)
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
221
4.78
5,5'-dithiobis(2-nitrobenzoic acid)
Caenorhabditis elegans
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
221
5.27
5,5'-dithiobis(2-nitrobenzoic acid)
Drosophila melanogaster
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
221
5.45
5,5'-dithiobis(2-nitrobenzoic acid)
Caenorhabditis elegans
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
221
21.2
5,5'-dithiobis(2-nitrobenzoic acid)
Homo sapiens
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
221
45.33
5,5'-dithiobis(2-nitrobenzoic acid)
Mus musculus
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
221
58.33
5,5'-dithiobis(2-nitrobenzoic acid)
Mus musculus
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
221
95
5,5'-dithiobis(2-nitrobenzoic acid)
Solanum lycopersicum
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
221
178
5,5'-dithiobis(2-nitrobenzoic acid)
Homo sapiens
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
221
183.3
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
purified, recombinant, tetrameric enzyme
221
333.5
5,5'-dithiobis(2-nitrobenzoic acid)
Homo sapiens
-
wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C
221
495
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
purified, recombinant, dimeric enzyme
221
513.3
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
mutant enzyme Y116I, in TE buffer, at 20°C
221
526.7
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
mutant enzyme Y116T, in TE buffer, at 20°C
221
748.3
5,5'-dithiobis(2-nitrobenzoic acid)
Rattus norvegicus
-
wild type enzyme, in TE buffer, at 20°C
221
7343
5-hydroxy-1,4-naphthoquinone
Rattus norvegicus
-
mutant enzyme Y116I, in TE buffer, at 20°C
1344
7557
5-hydroxy-1,4-naphthoquinone
Rattus norvegicus
-
mutant enzyme Y116T, in TE buffer, at 20°C
1344
10620
5-hydroxy-1,4-naphthoquinone
Rattus norvegicus
-
wild type enzyme, in TE buffer, at 20°C
1344
372
Lipoamide
Homo sapiens
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
925
1737
Lipoamide
Homo sapiens
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C
925
0.6
NADH
Solanum lycopersicum
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
8
1.1
NADH
Methanosarcina acetivorans
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
8
84
NADH
Entamoeba histolytica
-
with 5,5'-dithiobis(2-nitrobenzoicacid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
8
103.3
NADPH
Methanosarcina acetivorans
-
cosubstrate: 5,5'-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication
5
140
NADPH
Entamoeba histolytica
-
with 5,5'-dithiobis(2-nitrobenzoic acid) as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
5
150
NADPH
Solanum lycopersicum
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
5
75
thioredoxin
Entamoeba histolytica
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
121
260
thioredoxin
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
121
1230
thioredoxin
Solanum lycopersicum
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
121
52000
thioredoxin 2
Saccharomyces cerevisiae
-
mutant enzyme K137A, pH and temperature not specified in the publication
11573
73000
thioredoxin 2
Saccharomyces cerevisiae
-
wild type enzyme, pH and temperature not specified in the publication
11573
600
thioredoxin 41
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
14402
880
thioredoxin 41
Entamoeba histolytica
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
14402
890
thioredoxin 8
Entamoeba histolytica
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
14403
950
thioredoxin 8
Entamoeba histolytica
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
14403
13.7
thioredoxin disulfide
Methanosarcina acetivorans
-
Methanosarcina acetivorans thioredoxin 7, cosubstrate: NADPH, pH and temperature not specified in the publication
476
41450
thioredoxin disulfide
Rattus norvegicus
-
mutant enzyme Y116I, in TE buffer, at 20°C
476
42150
thioredoxin disulfide
Rattus norvegicus
-
mutant enzyme Y116T, in TE buffer, at 20°C
476
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.25 - 1.3
1-chloro-2,4-dinitrobenzene
-
pH and temperature not specified in the publication
additional information
additional information
-
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)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0383
(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
0.0042
(2E,5E)-2,5-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)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
0.0089
(2E,6E)-2,6-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)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
0.0046
(3E,5E)-3,5-bis(3-bromo-4-hydroxy-5-methoxybenzylidene)piperidin-4-one
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
0.2
1,4-dihydroxyanthroquinone
Rattus norvegicus
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
1,8-dihydroxyanthroquinone
Rattus norvegicus
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0086
2-aminothiazolium [trans-tetrachlorobis(2-aminothiazole)ruthenate(III)]
Rattus norvegicus
-
-
0.0636
2-benzyloxycinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
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
0.0083
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
0.0065
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
0.0027
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
0.000082
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
0.0205
allyl isothiocyanate
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
0.2
aloin A
Rattus norvegicus
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); 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
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0033
Benzyl isothiocyanate
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
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
0.38
diallyl disulfide
Homo sapiens
-
25°C, 30 min preincubation in assay with 5,5'-dithiobis(2-nitrobenzoic acid) as substrate
0.2
frangulin A
Rattus norvegicus
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
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
0.0032
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
0.2
sennoside A
Rattus norvegicus
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); 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
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); 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
O89049, Q9Z0J5
IC50 above 0.2 mM, isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4); IC50 above 0.2 mM, isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
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
O62768
IC50 above 0.06 mM, in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.0191
theaflavin-3'-monogallate
Bos taurus
O62768
in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.0216
theaflavin-3,3'-digallate
Bos taurus
O62768
in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.018
theaflavin-3-monogallate
Bos taurus
O62768
in 50 mM potassium phosphate, 1 mM EDTA, pH 7.5
0.0713
trans-cinnamaldehyde
Rattus norvegicus
-
1 h incubation with recombinant TrxR, in TE buffer, at 25°C
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
0.02
1,1'-sulfanediylbis[2-nitro-4-(trifluoromethyl)benzene]
Plasmodium falciparum
-
IC50: 0.02 mM
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
0.007
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
0.18
aloe emodin
Rattus norvegicus
O89049, Q9Z0J5
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.2
aloe emodin
Rattus norvegicus
O89049, Q9Z0J5
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
O89049, Q9Z0J5
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.194
chrysophanol
Rattus norvegicus
O89049, Q9Z0J5
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.049
hypericin
Rattus norvegicus
O89049, Q9Z0J5
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.198
hypericin
Rattus norvegicus
O89049, Q9Z0J5
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
O89049, Q9Z0J5
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.185
physcion
Rattus norvegicus
O89049, Q9Z0J5
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0046
pseudohypericin
Rattus norvegicus
O89049, Q9Z0J5
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.0079
pseudohypericin
Rattus norvegicus
O89049, Q9Z0J5
isoform TrxR2, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.084
Rhein
Rattus norvegicus
O89049, Q9Z0J5
isoform TrxR1, at 25°C in 0.2 M Na, K-phosphate buffer (pH 7.4)
0.123
Rhein
Rattus norvegicus
O89049, Q9Z0J5
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
0.00000167
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
-
purified double mutant C535S/C88A as homodimer, insulin coupled assay
0.3
0.4
-
homodimer of mutant C88A, insulin coupled assay; purified double mutant C535S/C88A as heterodimer with the wild-type, insulin coupled assay
0.5
-
activity with 5,5'-dithiobis(2-nitrobenzoic acid) and NADH, pH and temperature not specified in the publication
0.77
-
enzyme from cell-free extract, with NADPH, in 50 mM potassium phosphate buffer (pH 7.0), at 22°C
1.5
-
purified mutant C535A as heterodimer with the wild-type, insulin coupled assay
2.2
-
purified mutant C88A as heterodimer with the wild-type, insulin coupled assay
4.3
-
mutant H509A, coupled assay with DTNB; wild-type enzyme, coupled assay with DTNB
5.1
-
mutant enzyme C145S, in 50 mM potassium phosphate (pH 7.0), at 20°C
5.5
-
mutant enzyme C142S, in 50 mM potassium phosphate (pH 7.0), at 20°C
5.6
-
mutant enzyme C145A, in 50 mM potassium phosphate (pH 7.0), at 20°C
6.4
-
mutant enzyme C142A, in 50 mM potassium phosphate (pH 7.0), at 20°C
22
29.7
-
wild type enzyme, in 50 mM potassium phosphate (pH 7.0), at 20°C
36.4
using thioredoxin disulfide, insulin, and NADPH as substrates, at 25°C
150.6
using 5,5'-dithiobis(2-nitrobenzoic acid) and NADPH as substrates, at 25°C
367.7
-
after 478fold purification, with NADPH, in 50 mM potassium phosphate buffer (pH 7.0), at 22°C
additional information
0.3
-
activity with 5,5'-dithiobis(2-nitrobenzoic acid) and NADPH, pH and temperature not specified in the publication
additional information
-
enzyme quantification by immunochemical method, investigation of cross-reactivity of specific antibodies with enzymes from other species, calf tissue overview
additional information
-
wild-type and chimeric mutants with and without amino acid exchanges
additional information
-
hemolysate TR activity ranges from 0.05-1.212 mU/mg hemoglobin at baseline and 0.06-1.98 mU/mg hemoglobin at 6 months
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.1
-
cytosolic and mitochondrial TrxR1 isoform; TrxR-1(cyto); TrxR-1(mito)
7.4
7.5
6.5
-
the truncated enzyme shows a pH optimum for the reduction of 5,5'-dithiobis(2-nitrobenzoic acid) at pH 6.5
7.5
-
the truncated enzyme shows a pH optimum for the reduction of 5,5'-dithiobis(2-nitrobenzoic acid) at pH 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 60% of maximal activity
6.5 - 9
-
pH 6.5: about 40% of maximal activity, pH 9.0: about 50% of maximal activity, wild-type enzyme
6.5 - 9.5
-
pH 6.5: 45% of maximal activity, pH 9.5: about 50% of maximal activity, mutant enzyme Sec489C
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 95
-
70°C: about 50% of maximal activity, 95°C: about 95% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
development and differentiation of the cells from transgenic mice lacking Txnrd2 expression is not significantly impaired
-
genetic polymorphisms in the human selenoprotein P gene is associated with differences in thioredoxin reductase 1 concentrations
-
Bach1 repression of ferritin and thioredoxin reductase1 is heme-sensitive in cells and in vitro and coordinates expression with heme oxygenase1, beta-globin, and NADP(H) quinone (oxido) reductase1
-
quantification of the expression of alternative mRNA forms (alpha1/2, alpha6, alpha7/8, alpha10/11, alpha13, gamma2-4, and beta1) in six different human malignant mesothelioma cell lines of epithelioid (STAV-AB and M-14-K), sarcomatoid (STAV-FCS and ZL34), or mixed phenotype (M-28-K and M-9-K). The lowest level of TrxR1 is seen for the two sarcomatoid forms (STAV-FCS and ZL34), whereas the epithelioid phenotypes generally show very high levels of TrxR1. The major transcript form expressed in all cell lines is alpha1/2, followed by alpha7/8. The lowest level is observed for alpha6, which comprises less than 1% of the total a forms
-
mice lacking Txnrd1 in the nervous system are significantly smaller and display ataxia and tremor. A strikingly patterned cerebellar hypoplasia is observed. Proliferation of the external granular layer is strongly reduced and fissure formation and laminar organisation of the cerebellar cortex is impaired in the rostral portion of the cerebellum. Purkinje cells are ectopically located and their dendrites stunted. The Bergmann glial network is disorganized and shows a pronounced reduction in fiber strength. Neuron-specific inactivation of Txnrd1 does not result in cerebellar hypoplasia, suggesting a vital role for Txnrd1 in Bergmann glia or neuronal precursor cells; nervous system-specific Txnrd2 null mice develop normally
TGF-betA1-treatment up-regulated thioredoxin reductase 1
-
H157, U1810 and H611. Selenium treatment results in increased expression of almost all TrxR1 mRNA variants with increasing concentrations of selenite
-
in some case of glucocorticoid-resistant alopecia areata patients, the expression of TrxR1 is decreased in outer root sheath
-
inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells
-
TrxR activity declines in during the first 21 days in milk. TrxR may be an important antioxidant defense mechanism in peripheral blood mononuclear cells that is compromised during the periparturient period
-
U1906E and U1906L. Selenium treatment results in increased expression of almost all TrxR1 mRNA variants with increasing concentrations of selenite
-
transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. The TXNRD1_v3 isoform contains an atypical N-terminal glutaredoxin domain. Expression of the transcript of this isoform is found predominantly in testis but is also detected in ovary, spleen, heart, liver, kidney, and pancreas
; NTRC may be involved in the scavenging of peroxides produced in green tissues during the day or the night and in seeds during germination
thioredoxin reductase 1 is upregulated in synovial cell from patients with rheumatoid arthritis. TRXR1 suppresses hydrogen peroxide and inhibits apoptosis of rheumatoid arthritis synovial cells
-
thioredoxin reductase activity in rheumatoid arthritis cells is significantly higher than in osteoarthritis cells
-
development and differentiation of the cells from transgenic mice lacking Txnrd2 expression is not significantly impaired
-
Hg(II) potently inhibits (at concentrations of 5-50 nM) TrxR1 activity in both cell-free and intracellular assays
additional information
-
prolonged selenium-deficient diet in MsrA knockout mice lowers thioredoxin reductase activity
-
mouse embryos homozygous for a targeted null mutation of the txnrd1 gene, encoding the cytosolic thioredoxin reductase, are viable at embryonic day 8.5 (E8.5) but not at E9.5. Txnrd1 is required for correct patterning of the early embryo and progression to later development
-
transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. The TXNRD1_v3 isoform contains an atypical N-terminal glutaredoxin domain. Expression of the transcript of this isoform is found predominantly in testis but is also detected in ovary, spleen, heart, liver, kidney, and pancreas
-
heparin affinity depends on the selenium content; high and low affinity form with respect to heparin
-
-
-
transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. The TXNRD1_v3 isoform contains an atypical N-terminal glutaredoxin domain. Expression of the transcript of this isoform is found predominantly in testis but is also detected in ovary, spleen, heart, liver, kidney, and pancreas
-
lead exposure causes a marked increase in the thioredoxin reductase-1 activity in the kidney of rats. This is the only parameter affected by low lead doses both after acute and chronic exposure
; NTRC may be involved in the scavenging of peroxides produced in green tissues during the day or the night and in seeds during germination
-
although the OsNTRC gene is expressed in roots and shoots of seedlings, the protein is exclusively found in shoots and mature leaves
-
liver biopsy sections from hepatocellular carcinoma patients. Elevated exresssion level in tumor tissue compared to internal control
-
transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. The TXNRD1_v3 isoform contains an atypical N-terminal glutaredoxin domain. Expression of the transcript of this isoform is found predominantly in testis but is also detected in ovary, spleen, heart, liver, kidney, and pancreas
-
thioredoxin reductase activity is significantly increased by Picual extra virgin olive oil, but not by Arbequina extra virgin olive oil as compared with palm oil intervention
-
-
-
TR1 is uniquely overexpressed in cancer cells and its knockdown in a mouse cancer cell line driven by oncogenic k-ras results in orphological changes characteristic of parental (normal) cells, without significant effect on cell growth under normal growth conditions. When grown in serum-deficient medium, TR1 deficient cancer cells lose self-sufficiency of growth, manifest a defective progression in their S phase and a decreased expression of DNA polymerase alpha
-
transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. The TXNRD1_v3 isoform contains an atypical N-terminal glutaredoxin domain. Expression of the transcript of this isoform is found predominantly in testis but is also detected in ovary, spleen, heart, liver, kidney, and pancreas
-
transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. The TXNRD1_v3 isoform contains an atypical N-terminal glutaredoxin domain. Expression of the transcript of this isoform is found predominantly in testis but is also detected in ovary, spleen, heart, liver, kidney, and pancreas
-
Abeta-resistant PC-12 cells display higher levels of thioredoxin and thioredoxin reductase
-
thioredoxin reductase activity is reduced in placentas from pregnant women living at high altitude
-
although mRNA encoding both Trx h isoforms (HvTrxh1 and HvTrxh2) is present in embryo and aleurone layers, the corresponding proteins differ in spatiotemporal appearance. HvNTR1 resides in the starchy endosperm during germination; although mRNA encoding both Trx h isoforms (HvTrxh1 and HvTrxh2) is present in embryo and aleurone layers, the corresponding proteins differ in spatiotemporal appearance. HvNTR2 resides in the starchy endosperm during germination
-
although the OsNTRC gene is expressed in roots and shoots of seedlings, the protein is exclusively found in shoots and mature leaves
-
transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. The TXNRD1_v3 isoform contains an atypical N-terminal glutaredoxin domain. Expression of the transcript of this isoform is found predominantly in testis but is also detected in ovary, spleen, heart, liver, kidney, and pancreas
additional information
-
extensive alternative splicing occurs in the 5' region of TXNRD1. In total 21 different transcripts are identified, potentially encoding five isoforms of TrxR1 carrying alternative N-terminal domains
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
one of the two hydrogenosomal TrxR isoforms, TrxRh1, carries an N-terminal extension resembling known hydrogenosomal targeting signals; TrxR isoform, TrxRh2, has no N-terminal targeting signal but is nonetheless efficiently targeted to hydrogenosomes
-
the Grx domain of TXNRD1_v3 localizes first in the emerging protrusion and is then followed into the protrusions by actin and subsequently by tubulin. TXNRD1_v3 can guide actin polymerization in relation to cell membrane restructuring
-
there is a higher nuclear expression of thioredoxin reductase 1 in proliferating cells than in nonproliferating cells
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Lactococcus lactis subsp. cremoris (strain MG1363)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
34000
35000
52000
54386
-
2 * 54386, highly active enzyme form, calculated from amino acid sequence
55000
56000
57000
58000
60000
63700
-
mitochondrial TrxR1 isoform, deduced from amino acid sequence
65000
66000
67000
68000
73000 - 75000
-
amino acid analysis based on 2 mol FAD per molecule of enzyme
75000
78000
90000
110000
120000
150000
153000
-
low-molecular-mass form of NTRC observed in the presence of NADPH or dithiothreitol, gel filtration
52000
3 * 52000, native MtNTRC seems to be a polymer probably comprising three subunits linked by disulphide bridges, SDS-PAGE; reducing SDS-PAGE, with His-tag
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
-
consisting of a highly conserved 13-kDa catalytic subunit, which houses the [Fe4S4] cluster and the adjacent disulfide, and a variable subunit of similar or smaller size, which shows little sequence conservation between species
homodimer
homotetramer
4 * 54662, calculated from sequence of cDNA; 4 * 63000, SDS-PAGE
polymer
in non-reducing SDS-PAGE, NTRC appears as a single band of 150000 Da corresponding to a polymer probably comprising three subunits linked by disulphide bridges
trimer
3 * 52000, native MtNTRC seems to be a polymer probably comprising three subunits linked by disulphide bridges, SDS-PAGE
?
-
x * 53200, TrxR-1(cyto), calculation from nucleotide sequence; x * 63700, TrxR-1(mito), calculation from nucleotide sequence
?
x * 52320, isoform SEP1, calculated from amino acid sequence; x * 59000, isoform SEP1, SDS-PAGE
dimer
-
2 * 55000-57000, isoforms TR1 and TR3, SDS-PAGE; 2 * 55000-57000, isoforms TR1 and TR3, SDS-PAGE
dimer
-
2 * 55000-57000, isoforms TR1 and TR3, SDS-PAGE; 2 * 55000-57000, isoforms TR1 and TR3, SDS-PAGE; 2 * 67000, isoform TR1, SDS-PAGE
dimer
-
FAD-binding domain (residues 10-125 and 251-318) and NADPH-binding domain (residues 126-250)
dimer
-
incubation of the purified enzyme with NADPH (or dithiothreitol) triggers the formation of the dimer
dimer
-
2 * 55000-57000, isoforms TR1 and TR3, SDS-PAGE; 2 * 67000, isoform TR1, SDS-PAGE
homodimer
-
2 * 53117, isoform TrxR1, calculated from amino acid sequence; 2 * 54769, isoform TrxR2, calculated from amino acid sequence
homodimer
-
2 * 54386, highly active enzyme form, calculated from amino acid sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method in the presence of 35% PEG 4000, 0.2 M ammonium acetate and citric acid buffer pH 5.1 at 25°C
-
hanging drop diffusion method at 20°C, X-ray crystal structure of DmTR at 2.4 A resolution in which the enzyme was truncated to remove the C-terminal tripeptide sequence Cys-Cys-Ser
-
crystal structures of thioredoxin reductase in complex with NADP+ in the oxidized and sodium dithionite-reduced form of the enzyme at 1.7 A and 1.45 A resolution, respectively
-
crystals of hTrxR1 are grown at 25°C by the hanging-drop technique. Crystal structure of hTrxR1 (Sec->Cys) in complex with FAD and NADP+ at a resolution of 2.8 A
-
in complex with FAD, NADPH and/or (N-acetyl-4-aminothiophenolato)(2,2':6',2''-terpyridine)platinum(II) chloride, sitting drop vapor diffusion method, using 5 mM MgSO4, 5% (w/v) PEG 3350, 50 mM MES pH 6.0 and 20% (w/v) 1,6-hexanediol
-
hanging drop vapor diffusion method, using 24% (w/v) PEG 400, 2% Jeffamine M-600, and 0.1 M citrate buffer pH 3.5
in the presence of 10 mM NADP+, hanging drop vapor diffusion method, using 15% polyethylene glycol 3350, 12% ethylene glycol, and 0.1 M HEPES, pH 7.5
-
hanging drop vapor diffusion method, using 0.1 M MES buffer, pH 6.5, 10% PEG 20000, at 18°C; hanging drop vapor diffusion method, using 0.1 M MES buffer, pH 6.5, 10% (w/v) PEG 20000, at 18°C
hanging-drop vapour diffusion in the presence of PEG 3000 as precipitant after treatment with hydrogen peroxide
-
hanging drop vapor diffusion method, using 22% (w/v) PEG 3350, 0.1 M HEPES pH 7.2, 0.2 M NaNO3, 5 mM dithiothreitol, or beta-mercaptoethanol
-
TGR alone or in complex with NADH and GSSG, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.4, 20% PEG 3350, 0.2 M KI and 5 mM beta-mercaptoethanol or 0.2 M magnesium formate, 20% PEG 6000, 0.1 M Hepes, pH 7.0-7.5 and 5 mM beta-mercaptoethanol (TGR with reduced and ordered C-terminus)
wild type and mutant enzymes with or without NADP+, using 12-15% (w/v) polyethylene glycol 2000 monomethyl ether, 0.1 M (NH4)2SO4, and 50 mM sodium acetate (pH 4.6); wild type enzyme in complex with NADP+ and mutant enzyme C147A, using 12-15% (w/v) poly-ethylene glycol 2000 monomethyl ether, 0.1 M (NH4)2SO4 and 50 mM sodium acetate (pH 4.6)
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
the purified enzyme is stable at pH 6.0-7.0 and relatively stable even at pH 8.0-9.0, but quite unstable below pH 5.0
725691
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
65
70 - 90
-
the enzyme is stable at temperatures ranging from 4°C to 70°C for 30 min. However, the enzyme activity is drastically reduced at 80°C and completely inactivated at 90°C
80 - 95
-
enzyme activity increases along with the rise of temperature up to 95°C, and more than 60% of the activity remains after incubation for 28 h at 80°C and 50% remains after 9 h at 95°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
tightly bound FAD is not replaced during heat treatment or guanidinium hydrochloride
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the reduced enzyme is very labile to O2, decrease of selenium content and activity after exposure to air, protection by NADPH, NADP+ and tris-(2-carboxyethyl)phosphine
-
394954
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2',5'-ADP Sepharose column chromatography and phenylarsine oxide Sepharose column chromatography
-
2',5'-ADP Sepharose column chromatography and phenylarsine oxide-Sepharose column chroamtography
-
2',5'-ADP Sepharose column chromatography, PAO Sepharose column chromatography, and Superdex 200 gel filtration
-
; 2',5'-ADP-agarose affinity chromatography and Superose size exclusion chromatography
-
ammonium sulfate precipitation, 2'5'-ADP Sepharose 4B affinity column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, DEAE-Sephacel gel filtration, 2',5'-ADP-Sepharose 4B affinity chromatography, and omega-aminohexyl-Sepharose 4B column chromatography
-
chitin resin column chromatography and DEAE anion exchange column chromatography
-
chitin-agarose column gel filtration and S200 column size-exclusion chromatography
-
DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography
DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
-
heparin affinity depends on the selenium content, binding can be induced by reduction of the enzyme with NADPH or tris-(2-carboxyethyl)phosphine
-
HisBind HiTrap metal-affinity column chromatography, 2',5'-ADP-Sepharose column chromatography, and CNBr-activated Sepharose column chromatography
Ni-NTA affinity column chromatography, gel filtration; Ni-NTA column chromatography
Ni2+ affinity column chromatography
Ni2+-chelating Sepharose column chromatography and Superdex 75 column gel filtration
recombinant enzyme with an amino-terminal hexa-His-tag, extrasequence does not affect enzymatic activity, one-step Ni-NTA affinity column chromatography
recombinant enzyme-thioredoxin subunit complex C135-C32 and mutant S135-S32
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli
-
recombinant wild-type cytosolic and mitochondrial isoforms and mutants from Escherichia coli
-
wild-type and mutant enzymes
DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography
-
DEAE column column chromatography, 2',5'-ADP Sepharose 4B column chromatography, phenyl Sepharose column chromatography, and Ni-NTA agarose column chromatography
-
HisBind HiTrap metal-affinity column chromatography, 2',5'-ADP-Sepharose column chromatography, and CNBr-activated Sepharose column chromatography
-
HisBind HiTrap metal-affinity column chromatography, 2',5'-ADP-Sepharose column chromatography, and CNBr-activated Sepharose column chromatography
-
HisBind HiTrap metal-affinity column chromatography, 2',5'-ADP-Sepharose column chromatography, and CNBr-activated Sepharose column chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli ER2566 cells
expression in Escherichia coli
expression in Escherichia coli as a His-tagged protein; expression of wild-type as His-tagged protein and mutant C53S in Escherichia coli, DNA sequence analysis
expression in Escherichia coli with an amino-terminal hexa-His-tag for purification
expression of cytosolic and mitochondrial isoform as His-tagged enzymes in Escherichia coli
-
expression of hemagglutinin-tagged TrxRh1 in transfected Trichomonas vaginalis cells reveales that its N-terminal extension is necessary to import the protein into the organelles
-
expression of His-tagged or Strep-tagged wild-type and mutants in Escherichia coli, DNA sequence analysis
-
HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
-
nucleotide sequence analysis and comparison; nucleotide sequence analysis and comparison
-
overexpression of antisense mutant in Escherichia coli, expression of wild-type in COS-7 cells, amino acid sequence analysis
-
overexpression of wild-type and mutant enzymes from plasmids; trxB gene, DNA sequence analysis
-
overproduction of thioredoxin reductase in Lactobacillus plantarum WCFS1 improves the tolerance of the strain towards an oxidative stress produced by hydrogen peroxide or diamide
-
recombinant protein carrying an amino terminal His6-tag is produced in Escherichia coli; recombinant protein carrying an aminoterminal His6-tag is produced in Escherichia coli
-
subunit complex of enzyme via C135 with thioredoxin C32, mutant complex S135-S32, expression from plasmid
-
the full-length Sec489Cys mutant as well as the truncated mTR3 missing the C-terminal CUG tripeptide sequence is expressed as a TR-intein-chitin binding domain fusion protein in Escherichia coli
-
the internal conservative sequence of TrxR1 is cloned into the pMD18-T vector
truncated form of thioredoxin reductase (missing the C-terminal eight amino acids-TRtrunc), is produced by amplifying the coding region
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activities of thioredoxin reductase in Plasmodium berghei-infected erythrocytes are higher than those in normal host cells
-
OxyR regulates TrxB expression by promoting trxB transcription from the P2 site when oxidative stresses lowers the transcription from the constitutive P1 site
the expression of TrxR1 can be induced by UV and heat (37°C). The expression level of TrxR1 increases gradually between 0 and 1 h, and is maintained at a high level after 2 h after heat or UV exposure
the highest level of enzyme expression is observed after exposure to 10mg/l of Cd+ for 24 h followed by 20 mg/l for 48 h. The upregulation of mRNA is more pronounced after 24 h exposure to 50 and 100 mg/L of paraquat compared to 12 h exposure
the transcript of NTRC increases throughout 24 h hardening, whereas the encoded protein amount and total NTR activity decrease once and the increase during hardening
thioredoxin reductase activity gradually increases 4fold within ca. 70 h when cells are transferred to the medium containing 10 nM selenite, selenium is essential for the induction of thioredoxin reductase activity at the translational level but not at the transcriptional level
transcription of thioredoxin reductase is markedly elevated in the sarA mutant under conditions of aerobic, as well as micro-aerophilic growth, indicating that SarA acts as a negative regulator of thioredoxin reductase expression, 2-3fold higher level of thioredoxin reductase is observed in the sarA mutant as compared to the wild type strain
-
TxnRd1 expression is elevated by more than 50fold in FaDu and HeLa cells and by more than 20fold in SCC-1 cells compared with either MSK-Leuk1 cells or keratinocytes. TxnRd activity is about 20fold higher in FaDu and HeLa cells and about 7fold higher in SCC-1 cells compared with that in keratinocytes or MSK-Leuk1 cells
-
OxyR regulates TrxB expression by promoting trxB transcription from the P2 site when oxidative stresses lowers the transcription from the constitutive P1 site
-
OxyR regulates TrxB expression by promoting trxB transcription from the P2 site when oxidative stresses lowers the transcription from the constitutive P1 site
-
-
the transcript of NTRC increases throughout 24 h hardening, whereas the encoded protein amount and total NTR activity decrease once and the increase during hardening
the transcript of NTRC increases throughout 24 h hardening, whereas the encoded protein amount and total NTR activity decrease once and the increase during hardening
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C142A
-
mutant shows reduced reductase activity compared to the wild type enzyme
C142S
-
mutant shows reduced reductase activity compared to the wild type enzyme
C145A
-
mutant shows reduced reductase activity compared to the wild type enzyme
C145S
-
mutant shows reduced reductase activity compared to the wild type enzyme
A164G/R183F
-
the mutant shows reduced activity but is still able to dimerize though with an increase in intermediary forms
A164G/V182E
-
the mutant shows increased activity compared to the wild type enzyme
A164G/V182E/R183F
-
the mutant shows reduced activity compared to the wild type enzyme but is still able to dimerize though with an increase in intermediary forms
C489S
-
mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C489S/C490S
-
mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
C490S
-
mutant is incapable of reducing thioredoxin and can only be reduced to the 2-electron-state of enzyme
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
-
exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 138 is remaining; fluorescence spectroscopic investigation of the interaction with the flavin group
C135S/C32S
-
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
-
fluorescence spectroscopic investigation of the interaction with the flavin group
C138S
C138S/C35S
-
fluorescence spectroscopic investigation of the interaction with the flavin group
C32S
-
exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 35 is remaining, low activity; fluorescence spectroscopic investigation of the interaction with the flavin group
C35S
-
exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 32 is remaining; fluorescence spectroscopic investigation of the interaction with the flavin group
TrxR-16
-
truncated form of TrxR missing the last 16 C-terminal amino acids, without thioredoxin-reducing activity
C535S
-
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
-
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
C88A
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
-
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
Y116I
-
the mutation decreases sensitivity to inhibition by cisplatin and lowers catalytic efficiency in reduction of thioredoxin compared to the wild type enzyme; 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
C57S
-
inactive mutant containing a redox-active [Fe4S4]3+/2+ center, can be reduced by dithionite
C53S
site-directed mutagenesis, no activity since the redox cycle system is abolished
additional information
C138S
-
exchange of 1 cysteine in the active center disulfide, 1 cysteine at position 135 is remaining, very low activity; fluorescence spectroscopic investigation of the interaction with the flavin group
C88A
-
construction of a homodimer and a heterodimer, the latter containing 1 mutant and 1 wild-type subunit, activity is reduced by 4 and 90%
C147A
in the active site of the C147A mutant, which exhibits a marginal NADH oxidase activity, the FAD is canonically bound to the enzyme; the mutant exhibits a marginal NADH oxidase activity with FAD canonically bound to the enzyme
additional information
-
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
-
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
-
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
-
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
-
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
-
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
-
thioredoxin is cut off the native fusion protein thioredoxin-thioredoxin reductase resulting in enhanced activity
additional information
-
truncated enzyme mutant without catalytic active C-terminus
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
thioredoxin reductase-1 may be an early indicator of acute exposure to low lead doses
medicine
medicine
-
target for immunostimulating effect of 1-chloro-2,4-dinitrobenzene as agent in AIDS treatment
medicine
-
TrxR1 may be one putative cause for glucocorticoid resistance in alopecia areata, AA, through the impact on intracellular redox system
medicine
-
both pharmacological and toxicological effects of anti-cancer drug cisplatin involve TrxR inactivation, and the large enhancement on cisplatin cure rate in H22 ascites model by using amifostine is, at least in part, ascribed to its selective modulation on TrxR
medicine
-
tumor-bearing mice treated with 1,2-[bis(1,2-benzisoselenazolone-3(2H)-ketone)]ethane shows an increase of life span with a comparable effect to cyclophosphamide. Potential usage of 1,2-[bis(1,2-benzisoselenazolone-3(2H)-ketone)]ethane as a therapeutic agent against non-solid tumors
medicine
-
TR1 acts largely as a pro-cancer protein and it is a primary target in cancer therapy
medicine
-
TR1 acts largely as a pro-cancer protein and it is a primary target in cancer therapy
medicine
-
inhibition of thioredoxin reductase represents a potential target in pancreatic cancer and provides a biomarker of effect of lead indolequinones in this type of cancer
medicine
-
inhibition of thioredoxin reductase represents a potential target in pancreatic cancer and provides a biomarker of effect of lead indolequinones in this type of cancer
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