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
-
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
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Cofactor
Cofactor on EC 1.8.1.8 - protein-disulfide reductase
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NAD(P)H
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NADH/SS binding domain structure, residues 328-449, physiological reductant is NADH, NADH is strongly favoured over NADPH
NADP+
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tightly but noncovalentyl bound, 1 molecule per subunit, physiological cofactor
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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
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tightly but noncovalentyl bound, 1 molecule per subunit, reaction mechanism