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Information on EC 1.8.1.8 - protein-disulfide reductase
for references in articles please use BRENDA:EC1.8.1.8
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.1 With NAD+ or NADP+ as acceptor
1.8.1.8 protein-disulfide reductase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.8.1.8
- thioredoxins
- gsh
- monothiol
- ribonucleotide
- peroxiredoxins
-
deglutathionylation
-
glutathione-dependent
-
redox-active
- reductases
-
thiol-disulfide
-
iron-sulfur
- fe-s
-
redox-sensitive
- thioltransferase
- trx1
-
thioredoxin-like
- dehydroascorbate
-
nadph-dependent
- cys
- hydroperoxide
- deoxyribonucleotides
-
selenoenzyme
- auranofin
-
bola
-
thioredoxin-dependent
-
redox-dependent
- selenocysteine
-
gsh-dependent
- trypanothione
-
thiol-based
- diamide
-
oxidoreduction
- dtnb
- peroxidases
-
redox-regulated
-
sulfenic
- dsba
- ask1
- poplar
-
selenoproteins
-
sideroblast
-
thiol-dependent
showSynonyms
glutaredoxin, disulfide reductase, protein disulfide reductase, pdi reductase, hvtrxh2, protein-disulfide reductase, pfpdo, erp16, phdsb, ma3736, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
disulfide reductase
EC 1.6.4.4
-
-
formerly
-
glutaredoxin
insulin-glutathione transhydrogenase
-
-
-
-
MA_1658
methanoredoxin
NAD(P)H:protein-disulfide oxidoreductase
-
-
-
-
PDO
PH1130 protein
PhDsb
protein disulfide oxidoreductase
protein disulfide reductase
protein-disulfide oxidoreductase
protein-disulfide reductase (NAD(P)H)
-
-
-
-
reductase, protein disulfide
-
-
-
-
TTC0486
WhiB1
WhiB1/Rv3219
additional information
-
enzyme is a member of the flavoprotein disulfide reductase family of enzymes
disulfide reductase
-
-
-
-
protein disulfide reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein-dithiol + NAD(P)+ = protein-disulfide + NAD(P)H + H+
-
-
-
-
protein-dithiol + NAD(P)+ = protein-disulfide + NAD(P)H + H+
detailed reaction mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
reduction
-
reduces insulin disulfide in the presence of dithiothreitol at 30°C
reduction
-
the enzyme catalyzes the DTT-mediated reduction of insulin disulfides
reduction
-
the enzyme catalyzes the DTT-mediated reduction of insulin disulfides
-
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SYSTEMATIC NAME
IUBMB Comments
protein-dithiol:NAD(P)+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9029-19-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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)+
-
Substrates: -
Products: -
Products: -
?
5-hydroxy-1,4-naphthoquinone + NAD(P)H
5-hydroxy-1,4-naphthoquinol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
barley alpha-amylase/subtilisin inhibitor + ?
?
-
Substrates: -
Products: -
Products: -
?
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
DTNB + NAD(P)H
5-mercapto-2-nitrobenzoate + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
NAD+ + NADH
NADH + NAD+
-
Substrates: enzyme-catalyzed interconversion
Products: -
Products: -
?
NADH + CoA-SS-pantetheine-4'-phosphate
NAD+ + CoA + 4'-phosphopantetheine
-
Substrates: -
Products: -
Products: -
?
NADH + pantethine 4',4''-diphosphate
NAD+ + 4'-phosphopantetheine
-
Substrates: -
Products: -
Products: -
?
NADH + pantethine 4',4''-diphosphate + H+
NAD+ + 4'-phosphopantetheine
-
Substrates: -
Products: -
Products: -
?
peroxiredoxin disulfide + NAD(P)H
reduced peroxiredoxin + NAD(P)+
-
Substrates: -
Products: -
Products: -
ir
peroxiredoxin disulfide + NADH
reduced peroxiredoxin + NAD+
-
Substrates: 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
Products: -
Products: -
ir
SurR disulfide + NADH + H+
SurR + NAD+
Substrates: substrate is a transcription factor involved in the sulfur response
Products: -
Products: -
?
thio-NAD+ + NAD(P)H
NAD+ + thio-NAD(P)H
-
Substrates: -
Products: -
Products: -
?
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
Substrates: -
Products: -
Products: -
?
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
Substrates: -
Products: -
Products: -
?
coenzyme M disulfide + glutathione disulfide
2 coenzyme M + glutathione
Substrates: -
Products: -
Products: -
?
coenzyme M disulfide + glutathione disulfide
2 coenzyme M + glutathione
Substrates: -
Products: -
Products: -
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
Substrates: -
Products: -
Products: -
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
Substrates: -
Products: -
Products: -
?
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
Substrates: -
Products: -
Products: -
?
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
Substrates: -
Products: -
Products: -
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
Substrates: -
Products: -
Products: -
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: -
Products: -
Products: -
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
Substrates: -
Products: -
Products: -
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
Substrates: -
Products: -
Products: -
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
Substrates: reaction rate with NADPH is approximately twice that with NADH
Products: -
Products: -
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
Substrates: -
Products: -
Products: -
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
Substrates: -
Products: -
Products: -
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
Substrates: -
Products: -
Products: -
r
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
protein disulfide + NADH
protein dithiol + NAD+
-
Substrates: -
Products: -
Products: -
?
protein disulfide + NADH
protein dithiol + NAD+
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: computational analysis reveals the different behavior of the two active sites
Products: -
Products: -
?
additional information
?
-
-
Substrates: the disulfide reductase system varies with the organism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
peroxiredoxin disulfide + NADH
reduced peroxiredoxin + NAD+
-
Substrates: 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
Products: -
Products: -
ir
protein disulfide + NAD(P)H
protein dithiol + NAD(P)+
-
Substrates: -
Products: -
Products: -
r
protein disulfide + NADH
protein dithiol + NAD+
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the disulfide reductase system varies with the organism, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD(P)H
-
NADH/SS binding domain structure, residues 328-449, physiological reductant is NADH, NADH is strongly favoured over NADPH
NADP+
-
tightly but noncovalentyl bound, 1 molecule per subunit, physiological cofactor
FAD
-
binding domain structure, residues 210-327 and 450-521, flavoenzyme, the redox-active disulfide in the N-terminal domain, Cys129-Cys132, of the enzyme is in functional communication with the thioredoxin reductase-like disulfide center in the C-terminal portion, Cys345-Cys348, and with FAD
FAD
-
tightly but noncovalentyl bound, 1 molecule per subunit, reaction mechanism
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur cluster
-
the enzyme contains an intermolecular Fe-S cluster that controls oligomerization as a mechanism to regulate protein disulfide reductase activity
Zn2+
-
in the crystal unit cell two neighboring PfPDO molecules are associated by two zinc ions to form a dimer in the crystal
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-phospho-ADP-ribose
-
inhibition of 2,6-dimethyl-1,4-benzoquinone reduction
additional information
-
enzyme is inhibited by alkylation of either pair of Cys residues, i.e. Cys129-Cys132, or Cys345-Cys348
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetics, ping-pong kinetic mechanism with NAD(P)H and 2,6-dimethyl-1,4-benzoquinone or 5-hydroxy-1,4-naphthoquinone
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
cell extract: 1.56 U/mg, after purification: 8.17 U/mg, one unit is defined as the amount of protein that produces an increase in 0.1 OD in 1 min at 650 nm
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 7.8
-
pH 6.2: about 50% of activity maximum, pH 7.8: about 20% of activity maximum
additional information
-
seven times as active in phosphate buffer as in Tris at the same pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE