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
-
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
- 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
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
Advanced search results
Substrates Products
Substrates Products on EC 1.8.1.8 - protein-disulfide reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REACTION DIAGRAM
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)+
-
-
-
-
?
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
-
-
-
-
?
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
SurR disulfide + NADH + H+
SurR + NAD+
substrate is a transcription factor involved in the sulfur response
-
-
?
2 coenzyme M + thionitrobenzoate
-
-
-
?
coenzyme M disulfide + 5,5'-dithiobis(2-nitrobenzoic acid)
2 coenzyme M + thionitrobenzoate
-
-
-
?
2 coenzyme M + glutathione
-
-
-
?
coenzyme M disulfide + glutathione disulfide
2 coenzyme M + glutathione
-
-
-
?
insulin + coenzyme A disulfide
-
-
-
?
insulin disulfide + 2 coenzyme A
insulin + coenzyme A disulfide
-
-
-
?
insulin + coenzyme M disulfide
-
-
-
?
insulin disulfide + 2 coenzyme M
insulin + coenzyme M disulfide
-
-
-
?
insulin + dithiothreitol disulfide
-
-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
NAD(P)H + protein disulfide
NAD(P)+ + protein dithiol
-
reaction rate with NADPH is approximately twice that with NADH
-
?
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
-
-
?
?
-
-
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
?
-
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
-
-
?