1.8.1.9: thioredoxin-disulfide reductase
This is an abbreviated version!
For detailed information about thioredoxin-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.9
-
1.8.1.9
-
selenium
-
selenoproteins
-
selenocysteine
-
gsh
-
peroxiredoxins
-
dismutase
-
catalase
-
auranofin
-
glutaredoxins
-
trx1
-
selenoenzyme
-
hydroperoxide
-
peroxidases
-
fad
-
ribonucleotide
-
redox-active
-
cisplatin
-
dithiols
-
goldi
-
se-deficient
-
dtnb
-
iodothyronine
-
flavoenzyme
-
ebselen
-
redox-sensitive
-
selenium-containing
-
selenols
-
deiodinases
-
thiol-dependent
-
organoselenium
-
thioredoxin-like
-
selenium-deficient
-
se-dependent
-
n-heterocyclic
-
thioredoxin-dependent
-
diselenide
-
redox-regulated
-
selenium-dependent
-
thiol-disulfide
-
thiol-based
-
thioredoxin-1
-
ask1
-
carbene
-
1-chloro-2,4-dinitrobenzene
-
sulforaphane
-
secis
-
txnip
-
trypanothione
-
medicine
-
analysis
-
na2seo3
-
agriculture
-
thioredoxin-interacting
- 1.8.1.9
- selenium
-
selenoproteins
- selenocysteine
- gsh
- peroxiredoxins
- dismutase
- catalase
- auranofin
- glutaredoxins
- trx1
-
selenoenzyme
- hydroperoxide
- peroxidases
- fad
- ribonucleotide
-
redox-active
- cisplatin
- dithiols
-
goldi
-
se-deficient
- dtnb
-
iodothyronine
-
flavoenzyme
- ebselen
-
redox-sensitive
-
selenium-containing
-
selenols
-
deiodinases
-
thiol-dependent
-
organoselenium
-
thioredoxin-like
-
selenium-deficient
-
se-dependent
-
n-heterocyclic
-
thioredoxin-dependent
- diselenide
-
redox-regulated
-
selenium-dependent
-
thiol-disulfide
-
thiol-based
- thioredoxin-1
- ask1
-
carbene
- 1-chloro-2,4-dinitrobenzene
- sulforaphane
-
secis
-
txnip
- trypanothione
- medicine
- analysis
- na2seo3
- agriculture
-
thioredoxin-interacting
Reaction
Synonyms
all0737, ApTR, At2g41680, AtNTRA, AtNTRB, bacillithiol disulfide reductase, bacillithiol-disulfide reductase, BBOV_I002190, Bdr, BSSB reductase, CeTR2, DmTR, DmTrxR, DmTrxR-1, EC 1.6.4.5, EhTRXR, ferredoxin:thioredoxin reductase, FTR, general stress protein 35, GSP35, HCOI_01258400, hemolysate thioredoxin reductase, hemolysate TR, hTrxR, HvNTR1, HvNTR2, L-TR, L-TrxR, More, MtNTRC, mTR3, multifunctional thioredoxin-glutathione reductase, NAD(P)H:paraquat oxidoreductase, NADP-dependent thioredoxin reductase, NADP-linked thioredoxin reductase, NADP-thioredoxin reductase, NADP-thioredoxin reductase C, NADPH thioredoxin reductase, NADPH thioredoxin reductase C, NADPH-dependent thioredoxin reductase, NADPH-dependent thioredoxin reductase 2, NADPH-dependent thioredoxin reductase C, NADPH-dependent thioredoxin reductase I, NADPH-dependent thioredoxin reductase-1, NADPH-dependent TRX reductase, NADPH-thioredoxin reductase, NADPH-thioredoxin reductase C, NADPH-Trx reductase, NADPH2:oxidized thioredoxin oxidoreductase, NAPDH-dependent BSSB reductase, NTR, Ntr1, NTR2, Ntr3, NTRA, NTRAB, NtrB, NTRC, PH0178, PH1426, PhRP, PhTrxR, protein-disulfide oxidoreductase, reductase, thioredoxin, SEP1, taTrxR, TGR, thioredoxin glutathione reductase, thioredoxin h reductase, thioredoxin reductase, thioredoxin reductase (NADPH), thioredoxin reductase 1, thioredoxin reductase 2, thioredoxin reductase-1, thioredoxin reductase1, TON_1603, TR, TR1, TR2, TR3, TRase, TrR, Trr1, Trr1p, TRR2, Trx1, Trx3, TrxB, TrxB1, TrxB2, TrxR, TrxR-1(cyto), TrxR-1(mito), TrxR1, TrxR2, TrxR3, TrxRB3, TRXRD, TrxRh1, TrxRh2, TrxT, Txnrd1, TXNRD1-v3, Txnrd2, TXNRD3, TxrR-1, YpdA
ECTree
1.8.1.9 thioredoxin-disulfide reductaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.8.1.9 - thioredoxin-disulfide reductase
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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 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
-
-
?
2-Cys peroxiredoxin + NADH
?
-
NADH is a poor electron donor for NTRC activity
-
-
?
2-Cys peroxiredoxin + NADPH
?
-
NTRC is able to conjugate NADPH thioredoxin reductase and thioredoxin activities for the efficient reduction of 2-Cys peroxiredoxin
-
-
?
2-Cys peroxiredoxin A + NADPH + H+
2-Cys peroxiredoxin A disulfide + NADP+
-
-
-
-
?
2-Cys peroxiredoxin B + NADPH + H+
2-Cys peroxiredoxin B disulfide + NADP+
-
-
-
-
?
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+
-
-
-
?
Arabidopsis thaliana thioredoxin 3 + NADP+
Arabidopsis thaliana thioredoxin 3 disulfide + NADPH + H+
Babesia bovis thioredoxin + NADP+
Babesia bovis thioredoxin disulfide + NADPH + H+
-
-
-
?
CHLI-1 ATPase + NADPH + H+
CHLI-1 ATPase disulfide + NADP+
-
-
-
?
cystine + NADPH + H+
2 cysteine + NADP+
-
-
-
?
Entamoeba histolytica thioredoxin disulfide 41 + NADPH + H+
Entamoeba histolytica thioredoxin 41 + NADP+
-
-
-
-
?
Escherichia coli thioredoxin disulfide + NADPH + H+
Escherichia coli thioredoxin + NADP+
-
-
-
-
?
Hordeum vulgare thioredoxin 1 + NADP+
Hordeum vulgare thioredoxin 1 disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 + NADP+
Hordeum vulgare thioredoxin 2 disulfide + NADPH + H+
Hordeum vulgare thioredoxin 2 mutant E86A + NADP+
Hordeum vulgare thioredoxin 2 mutant E86A disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant G47P + NADP+
Hordeum vulgare thioredoxin 2 mutant G47P disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant G57P + NADP+
Hordeum vulgare thioredoxin 2 mutant G57P disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant I51G + NADP+
Hordeum vulgare thioredoxin 2 mutant I51G disulfide + NADPH + H+
Hordeum vulgare thioredoxin disulfide h1 + NADPH + H+
Hordeum vulgare thioredoxin h1 + NADP+
-
-
-
-
r
Hordeum vulgare thioredoxin disulfide h2 + NADPH + H+
Hordeum vulgare thioredoxin h2 + NADP+
-
-
-
-
r
human thioredoxin + NADP+
human thioredoxin disulfide + NADPH + H+
-
-
-
-
r
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(2-amino-2-oxoethyl)carbamoyl]-6-oxo-1,2,5-dithiazocan-7-] + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-L-cysteinylglycinamide + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(2-amino-2-oxoethyl)carbamoyl]-6-oxo-1,2,5-thiaselenazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-3-selanyl-L-alanylglycinamide + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(carboxymethyl)carbamoyl]-6-oxo-1,2,5-dithiazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-L-cysteinylglycine + NADP+
-
-
-
-
?
L-prolyl-L-threonyl-L-valyl-L-threonyl-N-[(4R,7R)-4-[(carboxymethyl)carbamoyl]-6-oxo-1,2,5-thiaselenazocan-7-yl]glycinamide + NADPH + H+
L-prolyl-L-threonyl-L-valyl-L-threonylglycyl-L-cysteinyl-3-selanyl-L-alanylglycine + NADP+
-
-
-
-
?
lipoamide + NADPH + H+
?
-
isoform TrxR2 displays strikingly lower activity with lipoamide compared to isoform TrxR1
-
-
?
lipoamide disulfide + NADPH + H+
lipoamide + NADP+
-
-
-
?
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
-
-
?
peroxiredoxin + NADPH + H+
peroxiredoxin disulfide + NADP+
-
-
-
?
Pro-Thr-Val-Thr-Gly-Cys-S-S-Cys-Gly + NADPH + H+
Pro-Thr-Val-Thr-Gly-Cys + Cys-Gly + NADP+
-
-
-
-
?
Pro-Thr-Val-Thr-Gly-Cys-S-S-selenoCys-Gly + NADPH + H+
Pro-Thr-Val-Thr-Gly-Cys + selenoCys-Gly + NADP+
-
-
-
-
?
protein disulfide isomerase + NADPH
protein disulfide isomerase + NADP+
-
-
protein disulfide isomerase with reduced disulfides
r
protein disulfide isomerase 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+
-
-
-
-
?
thioredoxin C-2 + NADP+
thioredoxin C-2 disulfide + NADPH + H+
-
-
-
-
r
thioredoxin-II + NADP+
thioredoxin-II disulfide + NADPH + H+
-
-
-
-
r
[thioredoxin reductase from Escherichia coli]-disulfide + NADH + H+
[thioredoxin reductase from Escherichia coli]-dithiol + NAD+
-
-
-
?
[thioredoxin reductase from Escherichia coli]-disulfide + NADPH + H+
[thioredoxin reductase from Escherichia coli]-dithiol + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol
2-nitro-5-thiobenzoate + oxidized dithiothreitol
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol
2-nitro-5-thiobenzoate + oxidized dithiothreitol
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
5'-thionitrobenzoic acid + NAD+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
requires thioredoxin for reduction of DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
native thioredoxin-thioredoxin reductase fusion protein
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
i.e. DTNB
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
coupled assay
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
C-terminal tetrapeptide sequences is Gly-Cys-Sec-Gly. Changing the C-terminal carboxylate of mTR3 to a carboxamide increases the activity of the enzyme. If the selenium content is normalized for both samples, the carboxamide mutant has nearly twice the activity as the semisynthetic wild-type carboxylate enzyme
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
isoform TrxR2 displays strikingly lower activity with 5,5'-dithiobis(2-nitrobenzoic acid) compared to isoform TrxR1
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
5'-thionitrobenzoic acid + NADP+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
5,5'-dithiobis-(2-nitrobenzoic acid) + NADPH + H+
2-nitro-5-thiobenzoate + NADP+
-
-
-
-
?
Arabidopsis thaliana thioredoxin 3 + NADP+
Arabidopsis thaliana thioredoxin 3 disulfide + NADPH + H+
-
-
-
?
Arabidopsis thaliana thioredoxin 3 + NADP+
Arabidopsis thaliana thioredoxin 3 disulfide + NADPH + H+
-
-
-
?
bis-gamma-glutamyl cystine + NADPH + H+
gamma-glutamyl cystine + NADP+
-
-
-
?
bis-gamma-glutamyl cystine + NADPH + H+
gamma-glutamyl cystine + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
BrxA bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxA + NADP+
-
-
-
?
BrxA bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxA + NADP+
-
-
-
?
BrxB bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxB + NADP+
-
-
-
?
BrxB bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxB + NADP+
-
-
-
?
BrxC bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxC + NADP+
-
-
-
?
BrxC bacilliredoxin disulfide + NADPH + H+
reduced bacilliredoxin BrxC + NADP+
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
-
-
-
?
Escherichia coli thioredoxin + NADP+
Escherichia coli thioredoxin disulfide + NADPH + H+
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
-
-
-
?
glutathione disulfide + NADPH + H+
glutathione + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
Hordeum vulgare thioredoxin 2 + NADP+
Hordeum vulgare thioredoxin 2 disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 + NADP+
Hordeum vulgare thioredoxin 2 disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant I51G + NADP+
Hordeum vulgare thioredoxin 2 mutant I51G disulfide + NADPH + H+
-
-
-
?
Hordeum vulgare thioredoxin 2 mutant I51G + NADP+
Hordeum vulgare thioredoxin 2 mutant I51G disulfide + NADPH + H+
-
-
-
?
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
-
-
?
oxidized bacillithiol disulfide + NADH + H+
reduced bacillithiol disulfide + NAD+
-
-
-
r
oxidized bacillithiol disulfide + NADH + H+
reduced bacillithiol disulfide + NAD+
-
-
-
r
oxidized bacillithiol disulfide + NADH + H+
reduced bacillithiol disulfide + NAD+
Staphylococcus aureus PS 47
-
-
-
r
oxidized bacillithiol disulfide + NADPH + H+
reduced bacillithiol disulfide + NADP+
-
-
-
r
oxidized bacillithiol disulfide + NADPH + H+
reduced bacillithiol disulfide + NADP+
-
-
-
r
oxidized bacillithiol disulfide + NADPH + H+
reduced bacillithiol disulfide + NADP+
Staphylococcus aureus PS 47
-
-
-
r
protein-disulfide + NADH + H+
protein-dithiol + NAD+
reduction activity for the disulfides in bovine insulin
-
-
?
protein-disulfide + NADH + H+
protein-dithiol + NAD+
Pyrococcus furiosus OT-3
reduction activity for the disulfides in bovine insulin
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
the enzyme is involved in a thioredoxin like system with thioredoxin reductase (PH1426). The redox potential of the redox protein is similar to that of thioredoxin from Escherichia coli and lower than that of glutathione
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
reduction activity for the disulfides in bovine insulin
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
Pyrococcus furiosus OT-3
the enzyme is involved in a thioredoxin like system with thioredoxin reductase (PH1426). The redox potential of the redox protein is similar to that of thioredoxin from Escherichia coli and lower than that of glutathione
-
-
?
protein-disulfide + NADPH + H+
protein-dithiol + NADP+
Pyrococcus furiosus OT-3
reduction activity for the disulfides in bovine insulin
-
-
?
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
-
-
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
-
-
-
-
?
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
-
?
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
-
-
r
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
-
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+
the enzyme forms a redox system with protein-disulfide oxidoreductase PhRP (PH0178)
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
the enzyme forms a redox system with protein-disulfide oxidoreductase PhRP (PH0178)
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
Thermosynechococcus vestitus
-
-
-
-
?
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
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH
thioredoxin + NADP+
Leptospira interrogans serovar Copenhageni Fiocruz L1-130
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
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+
-
the active site of Escherichia coli thioredoxin reductase contains a CATC motif without any selenocysteine and it specifically reduces oxidized Escherichia coli thioredoxin
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
the enzyme (TrxR) can use NADPH to reduce thioredoxin disulfide which passes the reducing equivalent to its downstream substrates involved in various biomedical events, such as ribonucleotide reductase for deoxyribonucleotide and DNA synthesis, or peroxiredoxins for counteracting oxidative stress
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
ebselen is an excellent substrate for mammalian Trx system
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
recombinant HvNTR1 and HvNTR2 exhibit virtually the same affinity toward HvTrxh1 and HvTrxh2, whereas HvNTR2 has slightly higher catalytic activity than HvNTR1 with both Trx h isoforms, and HvNTR1 has slightly higher catalytic activity toward HvTrxh1 than HvTrxh2
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
MtNTRC can use either NADPH or NADH as cofactors
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
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+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
[redox protein PhRP]-disulfide + NADH + H+
[redox protein PhRP]-dithiol + NAD+
redox protein PhRP from PH0178
-
-
?
[redox protein PhRP]-disulfide + NADH + H+
[redox protein PhRP]-dithiol + NAD+
Pyrococcus furiosus OT-3
redox protein PhRP from PH0178
-
-
?
[redox protein PhRP]-disulfide + NADPH + H+
[redox protein PhRP]-dithiol + NADP+
redox protein PhRP from PH0178
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[redox protein PhRP]-disulfide + NADPH + H+
[redox protein PhRP]-dithiol + NADP+
Pyrococcus furiosus OT-3
redox protein PhRP from PH0178
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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
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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
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the thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione
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the thioredoxin reductase/thioredoxin system can reduce oxidized glutathione and S-nitrosoglutathione
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the enzyme (TrxR) shows a weak ferredoxin/flavodoxin NADP+ oxidoreductase activity toward the flavodoxin-like protein NrdI
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the enzyme (TrxR) shows a weak ferredoxin/flavodoxin NADP+ oxidoreductase activity toward the flavodoxin-like protein NrdI
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the enzyme (TrxR) shows a weak ferredoxin/flavodoxin NADP+ oxidoreductase activity toward the flavodoxin-like protein NrdI
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Bdr and BrxB function cooperatively to debacillithiolate OhrR
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Bdr and BrxB function cooperatively to debacillithiolate OhrR
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incubation of Bdr with BSH under aerobic conditions reveals formation of an S-bacillithiolated species (Bdr-SSB). BrxC is a monothiol bacilliredoxin and Bdr is a bacilliredoxin reductase. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. The two bacilliredoxin (Brx) proteins, BrxA and BrxB, are substrates of Bdr. BrxC de-bacillithiolates enzyme Bdr in vitro. Bdr substrate specificity, overview
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incubation of Bdr with BSH under aerobic conditions reveals formation of an S-bacillithiolated species (Bdr-SSB). BrxC is a monothiol bacilliredoxin and Bdr is a bacilliredoxin reductase. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. The two bacilliredoxin (Brx) proteins, BrxA and BrxB, are substrates of Bdr. BrxC de-bacillithiolates enzyme Bdr in vitro. Bdr substrate specificity, overview
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Bdr and BrxB function cooperatively to debacillithiolate OhrR
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incubation of Bdr with BSH under aerobic conditions reveals formation of an S-bacillithiolated species (Bdr-SSB). BrxC is a monothiol bacilliredoxin and Bdr is a bacilliredoxin reductase. BrxC functions as a bacilliredoxin with BrxB-SBB and Bdr-SSB. The two bacilliredoxin (Brx) proteins, BrxA and BrxB, are substrates of Bdr. BrxC de-bacillithiolates enzyme Bdr in vitro. Bdr substrate specificity, overview
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thioredoxin reductase is essential for thiol/disulfide redox control and oxidative stress survival of the anaerobe Bacteroides fragilis
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specific for NADPH, B side of nicotinamide ring
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the enzyme does not reduce hydrogen peroxide or insulin
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NTRC shows both NADPH-dependent thioredoxin reductase and thioredoxin-like dithiol-disulfide oxidoreductase activities
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NTRC shows both NADPH-dependent thioredoxin reductase and thioredoxin-like dithiol-disulfide oxidoreductase activities
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NTRC shows both NADPH-dependent thioredoxin reductase and thioredoxin-like dithiol-disulfide oxidoreductase activities
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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
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in addition, the enzyme exhibits NAD(P)H dependent oxidase activity, which generates hydrogen peroxide from molecular oxygen
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reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
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slowly reduces other proteins, e.g. insulin, lipoate and ribonuclease
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redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
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redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
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thioredoxin reductase is essential for formate dehydrogenase H production and for labelling the formate dehydrogenase H polypeptide with 75Se-selenite
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R73G, R73D, and K36A site-directed mutants of thioredoxin are impaired to different extents in their ability to be reduced by TrxR
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R73G, R73D, and K36A site-directed mutants of thioredoxin are impaired to different extents in their ability to be reduced by TrxR
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Escherichia coli B / ATCC 11303
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reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
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reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
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reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
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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
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redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
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HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
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HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
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HEK-293 cells overexpressing TrxR2 are more resistant to impairment of complex III bypassing function of TrxR2
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function of TRXR1 in the self-defense mechanism against self-generated oxidative stress
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function of TRXR1 in the self-defense mechanism against self-generated oxidative stress
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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
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after successful cloning, overexpression and purification of PrxIII,18 Trx2 and TRR2, the PrxIII pathway is reconstituted and studied in vitro
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sulforaphane is an inducer for thioredoxin reductase. The dietary isothiocyanate, sulforaphane, is important in the regulation of thioredoxin reductase/thioredoxin redox system in cells
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binding of NADP+ enhances the ability of Ntr2 to bind thioredoxin
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no substrates: ferredoxin, flavodoxin
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no substrates: ferredoxin, flavodoxin
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no substrates: ferredoxin, flavodoxin
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Leptospira interrogans serovar Copenhageni Fiocruz L1-130
no substrates: ferredoxin, flavodoxin
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TR3 does not have catalytic preferences for mitochondrial thioredoxin versus cytosolic thioredoxin
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homozygous (-/-) knockout of Txnrd1 is embryonically lethal. No major effect of Txnrd1 hemizygosity and/or Se on male fertility and the viability of offspring
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homozygous (-/-) knockout of Txnrd1 is embryonically lethal. No major effect of Txnrd1 hemizygosity and/or Se on male fertility and the viability of offspring
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homozygous (-/-) knockout of Txnrd2 is embryonically lethal. No major effect of Txnrd2 hemizygosity and/or Se on male fertility and the viability of offspring
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homozygous (-/-) knockout of Txnrd2 is embryonically lethal. No major effect of Txnrd2 hemizygosity and/or Se on male fertility and the viability of offspring
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the enzyme can promote oxidative stress by redox cycling of paraquat: paraquat + O2 + NADPH + H+ --> paraquat radical + O2- radical + NADP+
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no substrate: chloroplastic thioredoxin x
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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
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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
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redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
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the enzyme catalyzes the reduction of protein-disulfide oxidoreductase PhRP (PH0178)
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the enzyme catalyzes the reduction of protein-disulfide oxidoreductase PhRP (PH0178)
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the enzyme catalyzes the reduction of protein-disulfide oxidoreductase PhRP (PH0178)
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specific for NADPH, B side of nicotinamide ring
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ribonucleotide reductase, thioredoxin and thioredoxin reductase constitute a system necessary for the biosynthesis of deesoxyribonucleotides
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mitochondrial respiratory chain and thioredoxin reductase regulate intermembrane Cu,Zn-superoxide dismutase activity
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the internal disulfide bond (CD7D5) of human neuroglobin can be reduced by thioredoxin reductase
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ebselen, 4,4'-bistrifluoromethyl-diphenyl diselenide, 2,4,6,2',4',6-hexamethyldiphenyl diselenide, and 4,4'-biscarboxydiphenyl diselenide are no substrates
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enzyme shows additionally NADH oxidase activity
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enzyme shows additionally NADH oxidase activity
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TrxRB3 also displays NADH oxidase activity
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TrxRB3 also displays NADH oxidase activity
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TrxRB3 is endowed with an additional NADH oxidase activity
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TrxRB3 is endowed with an additional NADH oxidase activity
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the yeast enzyme fails to reduce the human and Escherichia coli thioredoxin
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a redox couple consiting of protein disulfide oxidoreductase Ton_0319 and thioredoxin reductase has intracellular cystine-reducing activity, permitting recycling of cysteine. Cysteine or cystine is essentially required for DMSO reduction by whole cells and cell extracts
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TrxR from Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H
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Thermosynechococcus vestitus
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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
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the enzyme cannot use thioredoxin from Spirulina as an electron acceptor
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the enzyme cannot use thioredoxin from Spirulina as an electron acceptor
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slowly reduces other proteins, e.g. insulin, lipoate and ribonuclease
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redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
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redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
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