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Information on EC 1.8.4.16 - thioredoxin:protein disulfide reductase
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1.8.4.16 thioredoxin:protein disulfide reductaseIUBMB Comments
DsbD is an inner membrane protein found in Gram-negative bacteria that transfers electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG, reducing disulfide bonds in the target proteins to dithiols. DsbD consists of three domains: a periplasmic N-terminal domain, a central transmembrane domain and a periplasmic C-terminal domain.
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Word Map
- 1.8.4.16
- chaperone
- methanothermobacter
-
pdi-like
-
extremophiles
- thermoautotrophicum
- gssg
-
testis-specific
- pdilt
-
mercuric
-
agrobacterium-mediated
-
nipponbare
-
non-protein
- phytochelatins
-
non-classical
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
a [protein] with reduced L-cysteine residues
+
=
a [protein] carrying a disulfide bond
+
Synonyms
disulfide isomerase-like protein, disulfide bond reductase, dsbdalpha, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dipZ
disulfide bond reductase
DsbD
NmDsbD
dipZ
-
-
-
-
DsbD
-
-
-
-
DsbD
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [DsbD protein] carrying a disulfide bond + a [protein] with reduced L-cysteine residues = a [DsbD protein] with reduced L-cysteine residues + a [protein] carrying a disulfide bond
(1b)
-
-
-
a [DsbD protein] with reduced L-cysteine residues + thioredoxin disulfide = a [DsbD protein] carrying a disulfide bond + thioredoxin
(1a)
-
-
-
a [protein] with reduced L-cysteine residues + thioredoxin disulfide = a [protein] carrying a disulfide bond + thioredoxin
overall reaction
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, ,
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SYSTEMATIC NAME
IUBMB Comments
thioredoxin:protein disulfide oxidoreductase (dithiol-forming)
DsbD is an inner membrane protein found in Gram-negative bacteria that transfers electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG, reducing disulfide bonds in the target proteins to dithiols. DsbD consists of three domains: a periplasmic N-terminal domain, a central transmembrane domain and a periplasmic C-terminal domain.
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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
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin-1
a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
CQQGFDGTQNSCK peptide containing amide-coupled tetraazacyclododecane-1,4,7,10-tetraacetic acid + GSSG
?
-
-
-
-
?
insulin + dithiothreitol
reduced insulin + oxidized dithiothreitol
-
-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[DsbE protein] carrying a disulfide bond + thioredoxin
[DsbE protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[HelX protein] carrying a disulfide bond + thioredoxin
[HelX protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[protein DsbC] carrying a disulfide bond + thioredoxin
[protein DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbE] carrying a disulfide bond + thioredoxin
[protein DsbE] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbG] carrying a disulfide bond + thioredoxin
[protein DsbG] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
-
-
?
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
?
-
-
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
additional information
?
-
-
electron transfer by the enzyme involves sequential reduction and oxidation of its three structural domains, in which reducing potential is transferred from cytoplasmic thioredoxin to the beta domain, then successively to gamma and alpha, and thence to periplasmic substrates. Formation of a disulfide bond between cysteines 163 and 285 of the beta domain is part of the mechanism of the transmembrane electron transfer by the enzyme
-
-
-
additional information
?
-
the enzyme does not catalyze the reduction of the disulfide of the thioredoxin-like oxidant DsbA
-
-
-
additional information
?
-
-
the enzyme includes three domains, each containing a pair of cysteine residues that perform a series of disulfide exchange reactions. In the first step, the transmembrane domain accepts electrons from thioredoxin in the cytoplasm; these are then transferred to the periplasmic C-terminal domain and finally to the N-terminal domain, which is also located in the periplasm
-
-
-
additional information
?
-
-
the enzyme is composed of three domains, each containing two redox-active cysteines. All six of these cysteines are required for enzyme activity. The N-terminal periplasmic domain DsbDalpha directly reduces DsbC. DsbDalpha is then itself reduced by the C-terminal periplasmic domain, DsbDgamma, a thioredoxin-like polypeptide. The resulting oxidized DsbDgamma is reduced by the membrane-embedded DsbDbeta domain that contains eight transmembrane segments. Electrons passed from cytoplasmic thioredoxin 1 restore DsbDbeta to the reduced form, thus allowing it to continue to transfer electrons to DsbDgamma
-
-
-
additional information
?
-
the enzyme transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment
-
-
-
additional information
?
-
-
the enzyme transports electrons without using a metabolite or a cofactor
-
-
-
additional information
?
-
-
the periplasmic protein TrbB relies on the enzyme from Escherichia coli for maintenance of its C-X-X-C redox active site motif which is responsible for its enzymatic activity
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin-1
a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbC protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[DsbE protein] carrying a disulfide bond + thioredoxin
[DsbE protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
[DsbG protein] carrying a disulfide bond + thioredoxin
-
-
-
-
?
[HelX protein] carrying a disulfide bond + thioredoxin
[HelX protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[protein DsbC] carrying a disulfide bond + thioredoxin
[protein DsbC] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbE] carrying a disulfide bond + thioredoxin
[protein DsbE] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
[protein DsbG] carrying a disulfide bond + thioredoxin
[protein DsbG] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
-
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
-
-
?
a [protein] carrying a disulfide bond + thioredoxin
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
-
overall reaction
?
-
-
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
a [protein] with reduced L-cysteine residues + thioredoxin disulfide
a [protein] carrying a disulfide bond + thioredoxin
-
overall reaction
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[CcmG protein] carrying a disulfide bond + thioredoxin
[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbC protein] carrying a disulfide bond + thioredoxin
[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
?
[DsbG protein] carrying a disulfide bond + thioredoxin
[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Leukemia L1210
Overexpression of protein disulfide isomerase-like protein in a mouse leukemia L1210 cell line selected for resistance to 4-methyl-5-amino-1-formylisoquinoline thiosemicarbazone, a ribonucleotide reductase inhibitor.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
-
brenda
additional information
two periplasmic domains of native NmDsbD in the oxidized (n-NmDsbDOx, c-NmDsbDOx) and reduced (n-NmDsbDRed, c-NmDsbDRed) forms
-
brenda
additional information
-
two periplasmic domains of native NmDsbD in the oxidized (n-NmDsbDOx, c-NmDsbDOx) and reduced (n-NmDsbDRed, c-NmDsbDRed) forms
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
enzyme absence enhances the sensitivity of the dsbA1A2 mutant to oxidative stress
malfunction
-
enzyme loss leads to hypersensitivity to dithiothreitol and benzylpenicillin
malfunction
-
enzyme absence enhances the sensitivity of the dsbA1A2 mutant to oxidative stress
-
metabolism
-
cytoplasmic electrons donated by thioredoxin are transferred into the periplasm via the enzyme
metabolism
-
the enzyme accepts electrons from cytoplasmic thioredoxin and shuttles these electrons via a well-defined cascade through the membrane-spanning region and into the periplasm
metabolism
-
the enzyme generates a reducing source in the periplasm, which is required for maintaining proper redox conditions
metabolism
-
the enzyme is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence
metabolism
-
the enzyme is required to maintain the functional oxidation state of DsbC and DsbG
metabolism
-
the enzyme mediates electron transfer from the cytoplasm across the membrane
metabolism
-
the enzyme transfers reducing potential to periplasmic protein disulfide bond isomerases and to the cytochromexa0c thioreduction pathway
metabolism
-
the enzyme is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence
-
physiological function
-
overproduction of the enzyme and protein disulfide isomerase DsbC markedly enhances periplasmic production of human nerve growth factor in Escherichia coli
physiological function
-
the enzyme is essential for bacterial growth at temperatures above 42°C
physiological function
-
the enzyme is essential for survival of Neisseria gonorrhoeae
physiological function
-
the enzyme is required for the survival Neisseria meningitides
physiological function
NmDsbD is essential for viability. To initiate electron transport across the inner membrane, the disulfide bonded cysteine residues in t-DsbD are reduced by cytoplasmic thioredoxin. The transmebrane part, t-DsbD, in turn reduces the disulfide bond in c-DsbD, which then reduces n-DsbD. Lastly, n-DsbD transfers electrons to periplasmic substrates including the isomerases DsbC and DsbG, which reshuffle non-native disulfide bonds in multi-cysteine containing, as well as the reductases CcmG (DsbE), and CcmH which are involved in cytochrome c maturation
physiological function
-
the enzyme is required for the survival Neisseria meningitides
-
physiological function
-
NmDsbD is essential for viability. To initiate electron transport across the inner membrane, the disulfide bonded cysteine residues in t-DsbD are reduced by cytoplasmic thioredoxin. The transmebrane part, t-DsbD, in turn reduces the disulfide bond in c-DsbD, which then reduces n-DsbD. Lastly, n-DsbD transfers electrons to periplasmic substrates including the isomerases DsbC and DsbG, which reshuffle non-native disulfide bonds in multi-cysteine containing, as well as the reductases CcmG (DsbE), and CcmH which are involved in cytochrome c maturation
-
additional information
13Calpha and 13Cbeta chemical shift comparison of the two active site cysteine residues between n-NmDsbDOx and n-NmDsbDRed relative to the average BMRB shift values, overview
additional information
-
13Calpha and 13Cbeta chemical shift comparison of the two active site cysteine residues between n-NmDsbDOx and n-NmDsbDRed relative to the average BMRB shift values, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DSBD_ECOLI
Escherichia coli (strain K12)
565
8
61795
Swiss-Prot
other Location (Reliability: 1)
DSBD_NEIMB
Neisseria meningitidis serogroup B (strain MC58)
601
8
64925
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
DsbD is an integral membrane protein comprising two periplasmic domains, n-DsbD and c-DsbD, which flank a transmembrane region, t-DsbD. Two periplasmic domains of native cytoplasmic NmDsbD in the oxidized (n-NmDsbDOx, c-NmDsbDOx) and reduced (n-NmDsbDRed, c-NmDsbDRed) forms, structure analysis by NMR spectroscopy
additional information
-
DsbD is an integral membrane protein comprising two periplasmic domains, n-DsbD and c-DsbD, which flank a transmembrane region, t-DsbD. Two periplasmic domains of native cytoplasmic NmDsbD in the oxidized (n-NmDsbDOx, c-NmDsbDOx) and reduced (n-NmDsbDRed, c-NmDsbDRed) forms, structure analysis by NMR spectroscopy
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using 25% (w/v) poly(ethylene glycol) 4000, 0.1 M sodium acetate, pH 4.6, and 0.2 M NH4SO4
oxidized (ox) and reduced (red) periplasmic domains c-DsbD and n-DsbD, using 8-20% (w/v) PEG 6000, 100 mM MES (pH 6.4), and 20 mM ZnCl2 for n-DsbDox, 2.5 M ammonium sulfate and 0.1 M Tris (pH 9.1) for n-DsbDred, 5% (w/v) PEG 400 and 1.7-2.2 M citrate/citric acid (pH 7.0-7.8) for c-DsbDox, and 0.2 M zinc acetate dehydrate, 0.1 M sodium cacodylate trihydrate (pH 7.5), and 18% (w/v) PEG 8000 for c-DsbDred
-
periplasmic domains n-DsbD and c-DsbD in both redox states, hanging drop vapor diffusion method, using 18-20% (w/v) PEG 6000, 0.1 M MES pH 6.4, 0.02 M ZnCl2 (for the oxidized state of n-DsbD), 2.5 M ammonium sulfate, 0.1 M Tris pH 9.1 (for the reduced state of n-DsbD), 5% (w/v) PEG 400, 1.7-2.2 M citrate/citric acid pH 7.0-7.8 (for the oxidized state of c-DsbD), or 0.2 M zinc acetate dihydrate, 0.1 M sodium cacodylate trihydrate pH 7.5, 18% (w/v) PEG 8000 (for the reduced state of c-DsbD)
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C103A
C103A/C109A
C163A/C282A
Echerichia coli expressing the C163A and C282A mutations is Cu2+ resistant
C163A/C285A
C282A/C285A
Echerichia coli expressing the C282A and C285A mutations is Cu2+ resistant
C461A/C464A
Echerichia coli expressing the C461A and C464A mutations is Cu2+ sensitive
C464A
D455N/E468Q
-
in the double mutant of periplasmic C-terminal domain of the enzyme, the pK(a) value of Cys461 is lowered to 8.6, a value close to that expected for an unperturbed cysteine residue
P162A
-
the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
P166A
-
the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
P284A
-
the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
P289A
-
the mutation leads to less viability on copper and less susceptibility to air oxidation than wild type
C103S
C103A/C109A
Echerichia coli expressing the C103A and C109A mutations is Cu2+ sensitive and shows no enzymatic activity
C163A/C285A
Echerichia coli expressing the C163A and C285A mutations is Cu2+ sensitive and shows no enzymatic activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose column chromatography, HiTrap chelating column chromatography, and DEAE-Sepharose column chromatography
Q-Sepharose column chromatography, phenyl Sepharose column chromatography, and Econo-Pac 10 gel filtration
-
recombinant His6-tagged enzyme domains by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli DH5alpha cells
gene dsbD, recombinant individual expression of the C- and N-terminal domains of the enzyme with an N-terminal His6-tag followed by a tobacco etch virus (TEV) protease cleavage site in Escherichia coli strain BL21(DE3) pLysS
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of the enzyme is induced by dithiothreitol through the MisR/S regulatory system
transcription of the enzyme gene is decreased at 50°C, but not completely turned off
-
the expression of the enzyme is induced by dithiothreitol through the MisR/S regulatory system
-
the expression of the enzyme is induced by dithiothreitol through the MisR/S regulatory system
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Smith, R.; Whitten, A.; Paxman, J.; Kahler, C.; Scanlon, M.; Heras, B.
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis
Acta Crystallogr. Sect. F
74
31-38
2018
Neisseria meningitidis, Neisseria meningitidis NMB
brenda
Goulding, C.; Sawaya, M.; Parseghian, A.; Lim, V.; Eisenberg, D.; Missiakas, D.
Thiol-disulfide exchange in an immunoglobulin-like fold Structure of the N-terminal domain of DsbD
Biochemistry
41
6920-6927
2002
Escherichia coli (P36655)
brenda
Quinternet, M.; Tsan, P.; Selme, L.; Beaufils, C.; Jacob, C.; Boschi-Muller, S.; Averlant-Petit, M.; Branlant, G.; Cung, M.
Solution structure and backbone dynamics of the cysteine 103 to serine mutant of the N-terminal domain of DsbD from Neisseria meningitides
Biochemistry
47
12710-12720
2008
Neisseria meningitidis
brenda
Mavridou, D.; Stelzl, L.; Ferguson, S.; Redfield, C.
1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli
Biomol. NMR Assign.
6
163-167
2012
Escherichia coli
brenda
Katzen, F.; Beckwith, J.
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