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thioredoxin disulfide + insulin
thioredoxin + insulin disulfide
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + 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+
-
-
-
-
?
alloxan + NADPH
?
-
-
-
-
?
ebsulfur + NADP+
ebsulfur disulfide + NADPH + H+
-
-
-
-
?
ebsulfur disulfide + NADPH + H+
ebsulfur + NADP+
-
-
-
-
r
glutaredoxin 4 + NADPH
?
-
-
-
-
?
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 + NADP+
thioredoxin disulfide + NADPH
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
thioredoxin disulfide + NADPH + H+
?
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
thioredoxin K36E + NADP+
thioredoxin K36E disulfide + NADPH + H+
-
-
-
-
r
thioredoxin K36R + NADP+
thioredoxin K36R disulfide + NADPH + H+
-
-
-
-
r
thioredoxin P34S + NADP+
thioredoxin P34S disulfide + NADPH + H+
-
-
-
-
r
thioredoxin-CAC + NADP+
thioredoxin-CAC disulfide + NADPH + H+
-
-
-
-
r
thioredoxin-R + NADP+
thioredoxin-R disulfide + NADPH + H+
-
-
-
-
r
additional information
?
-
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
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
wide variety of electron acceptors
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay with DTNB
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
coupled assay, measurement of NADPH oxidation in presence of insulin and thioredoxin
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
NADH in the standard assay, wild-type and chimeric mutants with and without amino acid exchanges
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
substrate e.g. thioredoxin disulfide from phage T4
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH
-
metabolic function of thioredoxin reductase-thioredoxin system: supplies reducing equivalents for a wide variety of acceptors, e.g. : ribonucleotide reductase, nonspecific protein disulfide reductase, methionine sulfoxide reductase, D-proline reductase
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
?
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
-
-
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
ir
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
in presence of NADPH, coupled assay
-
r
thioredoxin + NADP+
thioredoxin disulfide + NADPH + H+
-
i.e. DTNB
-
ir
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
-
-
-
?
thioredoxin disulfide + NADPH + H+
thioredoxin + NADP+
-
the active site of Escherichia coli thioredoxin reductase contains a CATC motif without any selenocysteine and it specifically reduces oxidized Escherichia coli thioredoxin
-
-
?
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
?
-
-
-
-
-
?
additional information
?
-
-
reduction of thioredoxin by NADPH is virtually complete, equilibrium constant is 48 at pH 7
-
-
?
additional information
?
-
-
slowly reduces other proteins, e.g. insulin, lipoate and ribonuclease
-
-
?
additional information
?
-
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
additional information
?
-
-
redox system for electron transfer in the complex of apoenzyme, FAD and thioredoxin with NADPH or other electron acceptors
-
-
?
additional information
?
-
-
enzyme does not reduce ubiquinone-10
-
-
?
additional information
?
-
-
thioredoxin reductase is essential for formate dehydrogenase H production and for labelling the formate dehydrogenase H polypeptide with 75Se-selenite
-
-
?
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Williams, C.H.
Flavin-containing dehydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
89-173
1976
Escherichia coli
-
brenda
Pigiet, V.P.; Conley, R.R.
Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography
J. Biol. Chem.
252
6367-6372
1977
Escherichia coli
brenda
Lundstrm, J.; Holmgren, A.
Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
J. Biol. Chem.
265
9114-9120
1990
Bos taurus, Escherichia coli
brenda
Gleason, F.K.; Lim, C.J.; Gerami-Nejad, M.; Fuchs, J.A.
Characterization of Escherichia coli thioredoxins with altered active site residues
Biochemistry
29
3701-3709
1990
Escherichia coli
brenda
Schallreuter, K.U.; Pittelkow, M.R.; Wood, J.M.
EF-Hands calcium binding regulates the thioredoxin reductase/thioredoxin electron transfer in human keratinocytes
Biochem. Biophys. Res. Commun.
162
1311-1316
1989
Escherichia coli, Homo sapiens
brenda
Prongay, A.J.; Engelke, D.R.; Williams, C.H.
Characterization of two active site mutations of thioredoxin reductase from Escherichia coli [published erratum appears in J Biol Chem 1989 Jul 15;264(20):12113]
J. Biol. Chem.
264
2656-2664
1989
Escherichia coli
brenda
Russel, M.; Model, P.
Direct cloning of the trxB gene that encodes thioredoxin reductase
J. Bacteriol.
163
238-242
1985
Escherichia coli
brenda
O'Donnell, M.E.; Williams, C.H.
Reaction of both active site thiols of reduced thioredoxin reductase with N-ethylmaleimide
Biochemistry
24
7617-7621
1985
Escherichia coli
brenda
Grankvist, K.; Holmgren, A.; Luthman, M.; Tljedal, I.B.
Thioredoxin and thioredoxin reductase in pancreatic islets may participate in diabetogenic free-radical production
Biochem. Biophys. Res. Commun.
107
1412-1418
1982
Bos taurus, Escherichia coli, Mus musculus
brenda
Berglund, O.; Holmgren, A.
Thioredoxin reductase-mediated hydrogen transfer from Escherichia coli thioredoxin-(SH)2 to phage T4 thioredoxin-S2
J. Biol. Chem.
250
2778-2782
1975
Escherichia coli
brenda
Moore, E.C.; Reichard, P.; Thelander, L.
Enzymatic synthesis of desoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B
J. Biol. Chem.
239
3445-3452
1964
Escherichia coli
brenda
Lennon, B.W.; Williams, C.H., Jr.
Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis
Biochemistry
35
4704-4712
1996
Escherichia coli
brenda
Wang, P.F.; Veine, D.M.; Ahn, S.H.; Williams, C.H., Jr.
A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization
Biochemistry
35
4812-4819
1996
Escherichia coli
brenda
Veine, D.M.; Mulrooney, S.B.; Wang, P.F.; Williams, C.H., Jr.
Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin
Protein Sci.
7
1441-1450
1998
Escherichia coli
brenda
Van den Berg, P.A.W.; Mulrooney, S.B.; Gobets, B.; van Stokkum, I.H.M.; van Hoek, A.; Williams, C.H., Jr.; Visser, A.J.W.G.
Exploring the conformational equilibrium of E. coli thioredoxin reductase: characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopy
Protein Sci.
10
2037-2049
2001
Escherichia coli
brenda
Reynolds, C.M.; Poole, L.B.
Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity
Biochemistry
39
8859-8869
2000
Escherichia coli
brenda
Lundstroem-Ljung, J.; Birnbach, U.; Rupp, K.; Soeling, H.D.; Holmgren, A.
Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase
FEBS Lett.
357
305-308
1995
Escherichia coli
brenda
Watabe, S.; Makino, Y.; Ogawa, K.; Hiroi, T.; Yamamoto, Y.; Takahashi, S.Y.
Mitochondrial thioredoxin reductase in bovine adrenal cortex its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine
Eur. J. Biochem.
264
74-84
1999
Bos taurus, Escherichia coli
brenda
Wang, P.F.; Marcinkeviciene, J.; Williams, C.H., Jr.; Blanchard, J.S.
Thioredoxin Reductase-Thioredoxin Fusion Enzyme from Mycobacterium leprae: Comparison with the Separately Expressed Thioredoxin Reductase
Biochemistry
37
16378-16389
1998
Escherichia coli, Mycobacterium leprae
brenda
Xia, L.; Nordman, T.; Olsson, J.M.; Damdimopoulos, A.; Bjorkhem-Bergman, L.; Nalvarte, I.; Eriksson, L.C.; Arner, E.S.; Spyrou, G.; Bjornstedt, M.
The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress
J. Biol. Chem.
278
2141-2146
2003
Bos taurus, Escherichia coli, Homo sapiens, Rattus norvegicus
brenda
Fernandes, A.P.; Fladvad, M.; Berndt, C.; Andresen, C.; Lillig, C.H.; Neubauer, P.; Sunnerhagen, M.; Holmgren, A.; Vlamis-Gardikas, A.
A novel monothiol glutaredoxin (GRX4) from Escherichia coli can serve as a substrate for thioredoxin reductase
J. Biol. Chem.
280
24544-24552
2005
Escherichia coli
brenda
Takahata, M.; Tamura, T.; Abe, K.; Mihara, H.; Kurokawa, S.; Yamamoto, Y.; Nakano, R.; Esaki, N.; Inagaki, K.
Selenite assimilation into formate dehydrogenase H depends on thioredoxin reductase in Escherichia coli
J. Biochem.
143
467-473
2008
Escherichia coli
brenda
Chew, E.H.; Nagle, A.A.; Zhang, Y.; Scarmagnani, S.; Palaniappan, P.; Bradshaw, T.D.; Holmgren, A.; Westwell, A.D.
Cinnamaldehydes inhibit thioredoxin reductase and induce Nrf2: potential candidates for cancer therapy and chemoprevention
Free Radic. Biol. Med.
48
98-111
2010
Escherichia coli, Homo sapiens, Rattus norvegicus
brenda
Negri, A.; Rodriguez-Larrea, D.; Marco, E.; Jimenez-Ruiz, A.; Sanchez-Ruiz, J.; Gago, F.
Protein-protein interactions at an enzyme-substrate interface: Characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase
Proteins Struct. Funct. Bioinform.
78
36-51
2010
Escherichia coli (P0A9P4), Escherichia coli
brenda
Lu, J.; Vlamis-Gardikas, A.; Kandasamy, K.; Zhao, R.; Gustafsson, T.; Engstrand, L.; Hoffner, S.; Engman, L.; Holmgren, A.
Inhibition of bacterial thioredoxin reductase An antibiotic mechanism targeting bacteria lacking glutathione
FASEB J.
27
1394-1403
2013
Escherichia coli, Haemonchus contortus
brenda
Ren, X.; Zou, L.; Lu, J.; Holmgren, A.
Selenocysteine in mammalian thioredoxin reductase and application of ebselen as a therapeutic
Free Radic. Biol. Med.
127
238-247
2018
Escherichia coli, Homo sapiens (Q86VQ6), Homo sapiens (Q9NNW7)
brenda