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Information on EC 1.8.5.9 - protein dithiol:quinone oxidoreductase DsbB
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EC Tree
1.8.5.9 protein dithiol:quinone oxidoreductase DsbBIUBMB Comments
DsbB is a protein found in Gram-negative bacteria that functions within a pathway for protein disulfide bond formation. The enzyme catalyses the oxidation of the DsbA protein by generating disulfide bonds de novo via the reduction of membrane quinones. cf. EC 1.8.4.15, protein dithiol oxidoreductase (disulfide-forming).
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
a [DsbA protein] with reduced L-cysteine residues
+
=
a [DsbA protein] carrying a disulfide bond
+
Synonyms
vkor homolog, disulfide bond formation protein b, disulfide bond protein b, disulfide-bond formation protein b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
disulfide bond oxidoreductase B
DsbB
membrane protein disulfide bond protein B
Rv2968c
VKOR homolog
DsbB
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [DsbA protein] with reduced L-cysteine residues + a quinone = a [DsbA protein] carrying a disulfide bond + a quinol
overall reaction
-
-
a [DsbA protein] with reduced L-cysteine residues + a [DsbB protein] carrying a disulfide bond = a [DsbA protein] carrying a disulfide bond + a [DsbB protein] with reduced L-cysteine residues
(1a)
-
-
a [DsbB protein] with reduced L-cysteine residues + a quinone = a [DsbB protein] carrying a disulfide bond + a quinol
(1b)
-
-
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SYSTEMATIC NAME
IUBMB Comments
protein dithiol:quinone oxidoreductase (disulfide-forming)
DsbB is a protein found in Gram-negative bacteria that functions within a pathway for protein disulfide bond formation. The enzyme catalyses the oxidation of the DsbA protein by generating disulfide bonds de novo via the reduction of membrane quinones. cf. EC 1.8.4.15, protein dithiol oxidoreductase (disulfide-forming).
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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 [DsbA protein] with reduced L-cysteine residues + a quinone
a [DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
a [DsbA protein] with reduced L-cysteine residues + a [DsbB protein] carrying a disulfide bond
a [DsbA protein] carrying a disulfide bond + a [DsbB protein] with reduced L-cysteine residues
-
-
-
?
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
a [DsbA protein] with reduced L-cysteine residues + menaquinone-8
a [DsbA protein] carrying a disulfide bond + menaquinol-8
-
overall reaction
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
a [DsbA protein] with reduced L-cysteine residues + ubiquinone-1
a [DsbA protein] carrying a disulfide bond + ubiquinol-1
-
overall reaction
-
?
a [DsbB protein] with reduced L-cysteine residues + a quinone
a [DsbB protein] carrying a disulfide bond + a quinol
-
-
-
?
a [DsbB protein] with reduced L-cysteine residues + ubiquinone
a [DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
[DsbA protein] with reduced L-cysteine residues + menaquinone
[DsbA protein] carrying a disulfide bond + menaquinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
[DsbA protein] with reduced L-cysteine residues + ubiquinone Q8
[DsbA protein] carrying a disulfide bond + ubiquinol Q8
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
[DsbA protein] with reduced L-cysteine residues + ubiquinone-8
[DsbA protein] carrying a disulfide bond + ubiquinol-8
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
[DsbB protein] with reduced L-cysteine residues + a quinone
[DsbB protein] carrying a disulfide bond + a quinol
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
-
overall reaction
-
?
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
-
under unaerobic conditions, overall reaction
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
under aerobic conditions, overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
-
overall reaction
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
?
additional information
?
-
-
reduced DsbA forms a complex with the enzyme in which Cys30 of DsbA is disulfide-bonded to Cys104 of the enzyme. Cys104 is rapidly replaced by Cys33 of DsbA to generate the oxidized form of this protein
-
-
additional information
?
-
-
the enzyme is initially oxidized (state A). Disulfide interaction between Cys30 of DsbA protein and Cys104 of the enzyme then triggers the recycling reaction of DsbA (state B), allowing over all electron transfer from newly secreted protein via DsbA (Cys30/Cys33) to the enzyme in which intra-chain electron flow from Cys104/Cys130 (state C) to Cys41/Cys44 (state D) may occur
-
-
additional information
?
-
-
enzyme-catalyzed DsbA protein oxidation is an entropy-driven reaction originating from delocalization of electrons among four cysteine residues in the enzyme, which proceeds independently of an oxidizing power of ubiquinone
-
-
additional information
?
-
-
mutant DsbA protein C33S preferentially forms mixed disulfides with the enzyme
-
-
additional information
?
-
-
the enzyme gains the ability to oxidize its specific substrate, DsbA protein, having very high redox potential, by undergoing a DsbA-induced rearrangement of cysteine residues. One of the enzyme cysteines that are now reduced then interacts with ubiquinone to form a charge transfer complex, leading to the regeneration of a disulfide at the enzyme active site
-
-
additional information
?
-
-
the enzyme uses its two pairs of cysteines in a coordinated reaction to accept electrons from the active cysteines in DsbA protein
-
-
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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 [DsbA protein] with reduced L-cysteine residues + a quinone
a [DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + a [DsbB protein] carrying a disulfide bond
a [DsbA protein] carrying a disulfide bond + a [DsbB protein] with reduced L-cysteine residues
-
-
-
-
?
a [DsbA protein] with reduced L-cysteine residues + menaquinone
a [DsbA protein] carrying a disulfide bond + menaquinol
-
under unaerobic conditions, overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
a [DsbB protein] with reduced L-cysteine residues + a quinone
a [DsbB protein] carrying a disulfide bond + a quinol
-
-
-
-
?
a [DsbB protein] with reduced L-cysteine residues + ubiquinone
a [DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
[DsbA protein] with reduced L-cysteine residues + menaquinone
[DsbA protein] carrying a disulfide bond + menaquinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
[DsbA protein] with reduced L-cysteine residues + ubiquinone Q8
[DsbA protein] carrying a disulfide bond + ubiquinol Q8
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
[DsbB protein] with reduced L-cysteine residues + a quinone
[DsbB protein] carrying a disulfide bond + a quinol
-
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
-
?
a [DsbA protein] with reduced L-cysteine residues + ubiquinone
a [DsbA protein] carrying a disulfide bond + ubiquinol
-
under aerobic conditions, overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + a quinone
[DsbA protein] carrying a disulfide bond + a quinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
-
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone
[DsbA protein] carrying a disulfide bond + ubiquinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + ubiquinone-1
[DsbA protein] carrying a disulfide bond + ubiquinol-1
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
-
?
[DsbA protein] with reduced L-cysteine residues + [DsbB protein] carrying a disulfide bond
[DsbA protein] carrying a disulfide bond + [DsbB protein] with reduced L-cysteine residues
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone
[DsbB protein] carrying a disulfide bond + ubiquinol
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
-
?
[DsbB protein] with reduced L-cysteine residues + ubiquinone-1
[DsbB protein] carrying a disulfide bond + ubiquinol-1
-
-
-
?
additional information
?
-
-
reduced DsbA forms a complex with the enzyme in which Cys30 of DsbA is disulfide-bonded to Cys104 of the enzyme. Cys104 is rapidly replaced by Cys33 of DsbA to generate the oxidized form of this protein
-
-
-
additional information
?
-
-
the enzyme is initially oxidized (state A). Disulfide interaction between Cys30 of DsbA protein and Cys104 of the enzyme then triggers the recycling reaction of DsbA (state B), allowing over all electron transfer from newly secreted protein via DsbA (Cys30/Cys33) to the enzyme in which intra-chain electron flow from Cys104/Cys130 (state C) to Cys41/Cys44 (state D) may occur
-
-
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-bromo-1-methyl-5-oxo[1,2,5,6-tetrahydro[1,1'-biphenyl]]-3-yl propanoate
-
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
the oxidation of DsbA by the enzyme strongly depends on the presence of oxygen
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
3'-bromo-1-methyl-5-oxo[1,2,5,6-tetrahydro[1,1'-biphenyl]]-3-yl propanoate
Escherichia coli
-
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
the enzyme facilitates the formation of disulfide bonds in periplasmic proteins but does not facilitate the formation of intramembraneous disulfides
physiological function
malfunction
-
mutation in the DsbA-enzyme system results in an increase in sensitivity to Cd2+ and Zn2+ as well as a variety of antibiotics including beta-lactams, kanamycin, erythromycin, novobiocin, ofloxacin and sodium dodecyl sulfate
malfunction
-
mutation in the DsbA-enzyme system results in an increase in sensitivity to Cd2+ and Zn2+ as well as a variety of antibiotics including beta-lactams, kanamycin, erythromycin, novobiocin, ofloxacin and sodium dodecyl sulfate
physiological function
the enzyme is required for virulence in Burkholderia pseudomallei
physiological function
the enzyme oxidizes DsbA for continuous protein disulfide bond formation in the cell
physiological function
-
the enzyme is required for virulence in Burkholderia pseudomallei
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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). DSBB_BURPS
Burkholderia pseudomallei (strain K96243)
169
0
18114
Swiss-Prot
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with ubiquinone Q8 and DsbA, sitting drop vapor diffusion method, using 30% (w/v) PEG 550MME, 0.3 M ammonium formate and 0.05 M Tris/HCl, pH 8.9
sitting drop vapor diffusion method, using 15% (w/v) PEG3350, 0.1M magnesium formate and 0.1M MOPS (pH 7.0)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C41A/C44A
-
the mutant has two cysteine residues at Cys104 and Cys130 compared to the wild type enzyme with Cys41, Cys44, Cys104 and Cys130
R48H
Y46P/E47P
-
the mutant shows strongly reduced DsbA protein oxidation activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap nickel affinity column chromatography and Superdex S200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed with the biotin carboxyl carrier protein tag in Escherichia coli C41 (DE3) cells
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borsetti, F.; Francia, F.; Turner, R.J.; Zannoni, D.
The thiol:disulfide oxidoreductase DsbB mediates the oxidizing effects of the toxic metalloid tellurite (TeO32-) on the plasma membrane redox system of the facultative phototroph Rhodobacter capsulatus
J. Bacteriol.
189
851-859
2007
Rhodobacter capsulatus
brenda
Halili, M.; Bachu, P.; Lindahl, F.; Bechara, C.; Mohanty, B.; Reid, R.; Scanlon, M.; Robinson, C.; Fairlie, D.; Martin, J.
Small molecule inhibitors of disulfide bond formation by the bacterial DsbA-DsbB dual enzyme system
ACS Chem. Biol.
10
957-964
2015
Escherichia coli
brenda
Yazawa, K.; Furusawa, H.
Entropy-driven mechanisms between disulfide-bond formation protein A (DsbA) and B (DsbB) in Escherichia coli
ACS Omega
4
8341-8349
2019
Escherichia coli
brenda
Inaba, K.; Ito, K.
Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine
Biochim. Biophys. Acta Mol. Cell Res.
1783
520-529
2008
Escherichia coli
brenda
Kadokura, H.; Beckwith, J.
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
EMBO J.
21
2354-2363
2002
Escherichia coli
brenda
Inaba, K.; Murakami, S.; Nakagawa, A.; Iida, H.; Kinjo, M.; Ito, K.; Suzuki, M.
Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB
EMBO J.
28
779-791
2009
Escherichia coli (P0A6M2)
brenda
Whitley, P.; von Heijne, G.
The DsbA-DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains
FEBS Lett.
332
49-51
1993
Escherichia coli
brenda
Malojcic, G.; Owen, R.; Grimshaw, J.; Glockshuber, R.
Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
FEBS Lett.
582
3301-3307
2008
Escherichia coli (P0A6M2)
brenda
Kishigami, S.; Ito, K.
Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli
Genes Cells
1
201-208
1996
Escherichia coli
brenda
McMahon, R.; Ireland, P.; Sarovich, D.; Petit, G.; Jenkins, C.; Sarkar-Tyson, M.; Currie, B.; Martin, J.
Virulence of the melioidosis pathogen Burkholderia pseudomallei requires the oxidoreductase membrane protein DsbB
Infect. Immun.
86
e00938-17
2018
Burkholderia pseudomallei (Q63RY4), Burkholderia pseudomallei K96243 (Q63RY4)
brenda
Kishigami, S.; Kanaya, E.; Kikuchi, M.; Ito, K.
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