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Enzyme Nomenclature
Information on EC 1.8.1.8 - protein-disulfide reductase
Word Map on EC 1.8.1.8
- 1.8.1.8
- thioredoxins
- glutaredoxins
-
thiol-disulfide
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thioredoxin-like
- dithiols
-
er-resident
-
thioredoxin-related
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retrotranslocation
- trypanothione
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.8.1.8
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RECOMMENDED NAME
GeneOntology No.
protein-disulfide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein-dithiol + NAD(P)+ = protein-disulfide + NAD(P)H + H+
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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
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reduction
oxidation
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reduction
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reduction
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the enzyme catalyzes the DTT-mediated reduction of insulin disulfides
reduction
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reduces insulin disulfide in the presence of dithiothreitol at 30°C
reduction
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
protein disulfide reductase ERdj5 mediates endoplasmic reticulum-associated degradation in concert with EDEM1
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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)+
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-
?
5-hydroxy-1,4-naphthoquinone + NAD(P)H
5-hydroxy-1,4-naphthoquinol + NAD(P)+
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-
-
?
DTNB + NAD(P)H
5-mercapto-2-nitrobenzoate + NAD(P)+
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-
-
-
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NADH + CoA-SS-pantetheine-4'-phosphate
NAD+ + CoA + 4'-phosphopantetheine
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-
-
-
?
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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-
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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
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
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?
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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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
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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
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
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?
additional information
?
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the disulfide reductase system varies with the organism, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
FAD
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur cluster
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the enzyme contains an intermolecular Fe-S cluster that controls oligomerization as a mechanism to regulate protein disulfide reductase activity
Zn2+
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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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-phospho-ADP-ribose
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inhibition of 2,6-dimethyl-1,4-benzoquinone reduction
additional information
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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
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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
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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
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pH 6.2: about 50% of activity maximum, pH 7.8: about 20% of activity maximum
additional information
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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the enzyme is at a low level in log-phase cells but increases up to 10fold early in the stationary phase and has a similar specific activity in both the mother cell and the forespore compartment. The enzyme activity falls only slowly during spore germination and outgrowth
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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ERp16 mediates disulfide bond formation in the endoplasmic reticulum and plays an important role in cellular defense against prolonged ER stress
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup B (strain MC58)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
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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
dimer
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in the crystalline state via two zinc binding sites and an ionic network
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 10% (w/v) PEG 8000, 100 mM HEPES (pH 7.5), and 8 mM cystin at 20°C
purified recombinant His-tagged enzyme LpdA, hanging drop vapour diffusion method at room temperature, 0.003 ml protein solution containing 25 mg/ml protein, 10 mM HEPES, pH 7.5, mixed with 0.002 ml precipitant solution containing 0.1 M trisodium citrate, pH 5.4-5.8, 2.5-5.0% PEG 6000, 3-7 days depending on the pH, crystallization takes longer at higher pH-value, crystals are immersed in 10% PEG 6000, 100 mM MES, pH 5.75, and 25% glycerol, X-ray diffraction structure determination and analysis at 2.8 A resolution
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sitting-drop vapor diffusion method, crystals belong to the hexagonal space group P6522 with cell dimensions of a = b = 110.3 and c = 68.5 and with one molecule in the asymmtric unit. The structure is solved by multiple isomorphous replacement including anomalous scattering data. The structure is refined to 1.9 resolution
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analysis of the X-ray structure at 2.0 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, 8 weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli. Expression of ERp16 in HeLa cells inhibits the induction of apoptosis by agents that elicit ER stress, including brefeldin A, tunicamycin, and dithiothreitol
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gene lpdA, expression in Escherichia coli strain BL21(DE3) as His-tagged protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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enzyme is inhibited by mutation of either pair of Cys residues, i.e. Cys129-Cys132, or Cys345-Cys348, construction and functional analysis of a chimeric mutant enzyme comprising the enzymes N-terminal domain attached to the N-terminus of thioredoxin reductase from Escherichia coli, the chimeric mutant can reduce thioredoxin, which the wild-type AhpF is not capable of, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.8)
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