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2,6-dimethyl-1,4-benzoquinone + NAD(P)H
2,6-dimethyl-1,4-benzoquinol + NAD(P)+
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NAD(P)H
5-hydroxy-1,4-naphthoquinol + NAD(P)+
-
-
-
-
?
barley alpha-amylase/subtilisin inhibitor + ?
?
-
-
-
-
?
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
coenzyme M disulfide + glutathione disulfide
2 coenzyme M + glutathione
DTNB + NAD(P)H
5-mercapto-2-nitrobenzoate + NAD(P)+
-
-
-
-
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
insulin disulfide + NAD(P)H
? + NAD(P)+
-
-
-
-
?
insulin disulfide + NADPH
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
NAD+ + NADH
NADH + NAD+
-
enzyme-catalyzed interconversion
-
-
?
NADH + CoA-SS-CoA + H+
NAD+ + CoA
-
-
-
-
?
NADH + CoA-SS-pantetheine-4'-phosphate
NAD+ + CoA + 4'-phosphopantetheine
-
-
-
-
?
NADH + pantethine 4',4''-diphosphate
NAD+ + 4'-phosphopantetheine
-
-
-
-
?
NADH + pantethine 4',4''-diphosphate + H+
NAD+ + 4'-phosphopantetheine
-
-
-
-
?
peroxiredoxin disulfide + NAD(P)H
reduced peroxiredoxin + NAD(P)+
-
-
-
-
ir
peroxiredoxin disulfide + NADH
reduced peroxiredoxin + NAD+
-
enzyme recycles peroxiredoxin AhpC, enzyme acts in a catalytic cycle reaction together with peroxidase forming the bacterial alkyl hydroperoxide reductase system, formerly known as F-52a
-
-
ir
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
protein disulfide + NADH
protein dithiol + NAD+
SurR disulfide + NADH + H+
SurR + NAD+
substrate is a transcription factor involved in the sulfur response
-
-
?
thio-NAD+ + NAD(P)H
NAD+ + thio-NAD(P)H
-
-
-
-
?
additional information
?
-
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
-
-
-
?
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
-
-
-
?
coenzyme M disulfide + glutathione disulfide
2 coenzyme M + glutathione
-
-
-
?
coenzyme M disulfide + glutathione disulfide
2 coenzyme M + glutathione
-
-
-
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
-
-
-
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
-
-
-
?
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
-
-
-
?
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
-
-
-
?
insulin disulfide + ?
?
-
-
-
-
?
insulin disulfide + ?
?
-
-
-
-
?
insulin disulfide + ?
?
-
-
-
-
?
insulin disulfide + ?
?
-
-
-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
-
-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
-
-
-
?
insulin disulfide + NADPH
?
-
-
-
-
?
insulin disulfide + NADPH
?
-
-
-
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
-
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
-
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
reaction rate with NADPH is approximately twice that with NADH
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
-
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
-
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
-
-
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
-
-
-
r
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
-
-
-
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
-
-
-
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
-
-
-
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
-
-
-
?
protein disulfide + NADH
protein dithiol + NAD+
-
-
-
-
?
protein disulfide + NADH
protein dithiol + NAD+
-
the activity of MdrA and the organization of mdrA in a transcriptional unit with oxidative stress genes are consistent with a role in the oxidative stress response of Methanosarcina acetivorans
-
-
?
additional information
?
-
-
enzyme cannot catalyze the reduction of lipoyl substrates, because it lacks one of two cysteine residues involved in dithiol-disulfide interchange with lipoyl substrates and a His-Glu pair involved in general acid catalysis, no reduction of disulfide-bonded substrates
-
-
?
additional information
?
-
-
the enzyme is active only on disulfides containing pantethine 4',4"-diphosphate moieties, including pantethine 4',4"-diphosphate, oxidized coenzyme A, and coenzyme A in disulfide linkage to acyl carrier protein
-
-
?
additional information
?
-
-
the partially purified enzyme has no activity with cystine, GSSG or lipoic acid, and has high activity only with disulfides containing pantethine 4,4-diphosphate moieties either alone or as part of CoA. The enzyme utilizes only NADH as a reductant and is inactive with NADPH
-
-
?
additional information
?
-
-
computational analysis reveals the different behavior of the two active sites
-
-
?
additional information
?
-
-
the disulfide reductase system varies with the organism, overview
-
-
?
additional information
?
-
-
enzyme contains the CXXCD motif required in thioredoxin reductase for the dithiol-disulfide interchange reaction with thioredoxin corresponding to Cys345 and Cys348 in the enzyme, the enzyme is a thioredoxin reductase-like flavoprotein disulfide reductase, AhpF utilizes the CXXCD motif domain for electron shuttling to AhpC substrate, activity requires conformational changes, catalytic cycle, overview
-
-
?
additional information
?
-
a redox couple consiting of protein disulfide oxidoreductase and thioredoxin reductase TON_1603 has intracellular cystine-reducing activity, permitting recycling of cysteine. Cysteine or cystine is essentially required for DMSO reduction by whole cells and cell extracts
-
-
?
additional information
?
-
in a hybrid redox couple with Sulfolobus solfataricus thioredoxin reductase, thioredoxin reductase is able to reduce PDO in a concentration dependent manner with a calculated KM value of 34.72 microM
-
-
?
additional information
?
-
-
in a hybrid redox couple with Sulfolobus solfataricus thioredoxin reductase, thioredoxin reductase is able to reduce PDO in a concentration dependent manner with a calculated KM value of 34.72 microM
-
-
?
additional information
?
-
in a hybrid redox couple with Sulfolobus solfataricus thioredoxin reductase, thioredoxin reductase is able to reduce PDO in a concentration dependent manner with a calculated KM value of 34.72 microM
-
-
?
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Hatch, M.D.; Turner, J.F.
A protein disulfide reductase from pea seeds
Biochem. J.
76
556-562
1960
Avena sativa, Vicia faba, Hordeum vulgare, Pisum sativum, Triticum aestivum, Zea mays
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Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases
Arch. Biochem. Biophys.
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2005
Salmonella enterica subsp. enterica serovar Typhimurium
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Argyrou, A.; Vetting, M.W.; Blanchard, J.S.
Characterization of a new member of the flavoprotein disulfide reductase family of enzymes from Mycobacterium tuberculosis
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52694-52702
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Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase
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52
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A fluorescence-based assay for the reductase activity of protein disulfide isomerase
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350
105-112
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Homo sapiens
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Ladenstein, R.; Ren, B.
Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles
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273
4170-4185
2006
Pyrococcus furiosus, Pyrococcus horikoshii, Thermococcus kodakarensis, Saccharolobus solfataricus, Thermotoga maritima
brenda
Maeda, K.; Haegglund, P.; Finnie, C.; Svensson, B.; Henriksen, A.
Structural basis for target protein recognition by the protein disulfide reductase thioredoxin
Structure
14
1701-1710
2006
Hordeum vulgare
brenda
Swerdlow, R.D.; Setlow, P.
Purification and characterization of a Bacillus megaterium disulfide reductase specific for disulfides containing pantethine 4',4"-diphosphate
J. Bacteriol.
153
475-484
1983
Priestia megaterium
brenda
Swerdlow, R.D.; Green, C.L.; Setlow, B.; Setlow, P.
Identification of an NADH-linked disulfide reductase from Bacillus megaterium specific for disulfides containing pantethine 4',4''-diphosphate moieties
J. Biol. Chem.
254
6835-6837
1979
Priestia megaterium
brenda
Lessner, D.J.; Ferry, J.G.
The archaeon Methanosarcina acetivorans contains a protein disulfide reductase with an iron-sulfur cluster
J. Bacteriol.
189
7475-7484
2007
Methanosarcina acetivorans
brenda
Jeong, W.; Lee, D.Y.; Park, S.J.; Rhee, S.G.
ERp16, an endoplasmic reticulum-resident thiol-disulfide oxidoreductase: biochemical properties and role in apoptosis induced by endoplasmic reticulum stress
J. Biol. Chem.
283
25557-25566
2008
Homo sapiens
brenda
Kuroita, T.; Kanno, T.; Kawai, A.; Kawakami, B.; Oka, M.; Endo, Y.; Tozawa, Y.
Functional similarities of a thermostable protein-disulfide oxidoreductase identified in the archaeon Pyrococcus horikoshii to bacterial DsbA enzymes
Extremophiles
11
85-94
2007
Pyrococcus horikoshii (O58857), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58857)
brenda
Bartolucci, S.; de Pascale, D.; Rossi, M.
Protein disulfide oxidoreductase from Pyrococcus furiosus: biochemical properties
Methods Enzymol.
334
62-73
2001
Pyrococcus furiosus
brenda
Ren, B.; Ladenstein, R.
Protein disulfide oxidoreductase from Pyrococcus furiosus: structural properties
Methods Enzymol.
334
74-88
2001
Pyrococcus furiosus
brenda
Hagiwara, M.; Maegawa, K.; Suzuki, M.; Ushioda, R.; Araki, K.; Matsumoto, Y.; Hoseki, J.; Nagata, K.; Inaba, K.
Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5
Mol. Cell
41
432-444
2011
Mus musculus (Q9DC23)
brenda
Yenugudhati, D.; Prakash, D.; Kumar, A.K.; Kumar, R.S.; Yennawar, N.H.; Yennawar, H.P.; Ferry, J.G.
Structural and biochemical characterizations of methanoredoxin from Methanosarcina acetivorans, a glutaredoxin-like enzyme with coenzyme M-dependent protein disulfide reductase activity
Biochemistry
55
313-321
2016
Methanosarcina acetivorans (Q8TQ93), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8TQ93)
brenda
Pedone, E.; Fiorentino, G.; Pirone, L.; Contursi, P.; Bartolucci, S.; Limauro, D.
Functional and structural characterization of protein disulfide oxidoreductase from Thermus thermophilus HB27
Extremophiles
18
723-731
2014
Thermus thermophilus (Q72KI9), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72KI9)
brenda
Lim, J.K.; Jung, H.C.; Kang, S.G.; Lee, H.S.
Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1
Extremophiles
21
491-498
2017
Thermococcus onnurineus (B6YTB7)
brenda
Choi, A.R.; Kim, M.S.; Kang, S.G.; Lee, H.S.
Dimethyl sulfoxide reduction by a hyperhermophilic archaeon Thermococcus onnurineus NA1 via a cysteine-cystine redox shuttle
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54
31-38
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Thermococcus onnurineus (B6YTB7)
brenda
Pedone, E.; Saviano, M.; Bartolucci, S.; Rossi, M.; Ausili, A.; Scirè, A.; Bertoli, E.; Tanfani, F.
Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus A dynamic simulation and fourier transform infrared spectroscopic study
J. Proteome Res.
4
1972-1980
2005
Pyrococcus furiosus
brenda
Scir, A.; Pedone, E.; Ausili, A.; Saviano, M.; Baldassarre, M.; Bertoli, E.; Bartolucci, S.; Tanfani, F.
High hydrostatic pressure-induced conformational changes in protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A fourier-transform infrared spectroscopic study
Mol. Biosyst.
6
2015-2022
2010
Pyrococcus furiosus
brenda