1.8.1.8: protein-disulfide reductase
This is an abbreviated version!
For detailed information about protein-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.8
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1.8.1.8
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thioredoxins
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gsh
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monothiol
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ribonucleotide
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peroxiredoxins
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deglutathionylation
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glutathione-dependent
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redox-active
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reductases
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thiol-disulfide
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iron-sulfur
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fe-s
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redox-sensitive
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thioltransferase
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trx1
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thioredoxin-like
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dehydroascorbate
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nadph-dependent
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cys
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hydroperoxide
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deoxyribonucleotides
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selenoenzyme
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auranofin
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bola
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thioredoxin-dependent
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redox-dependent
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selenocysteine
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gsh-dependent
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trypanothione
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thiol-based
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diamide
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oxidoreduction
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dtnb
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peroxidases
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redox-regulated
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sulfenic
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dsba
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ask1
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poplar
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selenoproteins
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sideroblast
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thiol-dependent
- 1.8.1.8
- thioredoxins
- gsh
- monothiol
- ribonucleotide
- peroxiredoxins
-
deglutathionylation
-
glutathione-dependent
-
redox-active
- reductases
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thiol-disulfide
-
iron-sulfur
- fe-s
-
redox-sensitive
- thioltransferase
- trx1
-
thioredoxin-like
- dehydroascorbate
-
nadph-dependent
- cys
- hydroperoxide
- deoxyribonucleotides
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selenoenzyme
- auranofin
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bola
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thioredoxin-dependent
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redox-dependent
- selenocysteine
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gsh-dependent
- trypanothione
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thiol-based
- diamide
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oxidoreduction
- dtnb
- peroxidases
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redox-regulated
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sulfenic
- dsba
- ask1
- poplar
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selenoproteins
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sideroblast
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thiol-dependent
Reaction
Synonyms
AhpF, disulfide reductase, EC 1.6.4.4, ERdj5, ERp16, glutaredoxin, HvTrxh2, insulin-glutathione transhydrogenase, LpdA, MA3736, MA_1658, MdrA, methanoredoxin, More, NAD(P)H:protein-disulfide oxidoreductase, NADH-linked disulfide reductase, panthethine 4'4-diphosphate-specific reductase, PDI reductase, PDO, PfPDO, PH1130 protein, PhDsb, protein disulfide isomerase reductase, protein disulfide oxidoreductase, protein disulfide reductase, protein-disulfide oxidoreductase, protein-disulfide reductase (NAD(P)H), reductase, protein disulfide, thiol-disulfide oxidoreductase, TON_0319, TTC0486, WhiB1, WhiB1/Rv3219
ECTree
1.8.1.8 protein-disulfide reductaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.8.1.8 - protein-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
2,6-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)+
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-
-
-
?
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
DTNB + NAD(P)H
5-mercapto-2-nitrobenzoate + NAD(P)+
-
-
-
-
?
NADH + CoA-SS-pantetheine-4'-phosphate
NAD+ + CoA + 4'-phosphopantetheine
-
-
-
-
?
NADH + pantethine 4',4''-diphosphate
NAD+ + 4'-phosphopantetheine
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-
-
-
?
NADH + pantethine 4',4''-diphosphate + H+
NAD+ + 4'-phosphopantetheine
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-
-
-
?
peroxiredoxin disulfide + NAD(P)H
reduced peroxiredoxin + NAD(P)+
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-
-
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ir
peroxiredoxin disulfide + NADH
reduced peroxiredoxin + NAD+
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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
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-
ir
SurR disulfide + NADH + H+
SurR + NAD+
substrate is a transcription factor involved in the sulfur response
-
-
?
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
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-
-
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
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-
-
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
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-
-
?
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
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-
-
?
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
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-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
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-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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-
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
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reaction rate with NADPH is approximately twice that with NADH
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?
protein disulfide + NADH
protein dithiol + NAD+
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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
?
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-
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
?
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-
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
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-
?
additional information
?
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-
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
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-
?
additional information
?
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-
computational analysis reveals the different behavior of the two active sites
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-
?
additional information
?
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-
the disulfide reductase system varies with the organism, overview
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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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-
?
additional information
?
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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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-
?
additional information
?
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Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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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-
?
