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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 + quinone
[DsbA protein] carrying a disulfide bond + quinol
[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
additional information
?
-
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 + quinone
[DsbA protein] carrying a disulfide bond + quinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + 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 + 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
?
-
-
membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation
-
-
-
additional information
?
-
membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation
-
-
-
additional information
?
-
membranes containing CtDsbB can sustain CtDsbA catalysed oxidation of a model substrate. Detergent solubilised, purified CtDsbB partially oxidises reduced CtDsbA, the active site CSAC thiols are the likely target for CtDsbB mediated oxidation
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + quinone
[DsbA protein] carrying a disulfide bond + quinol
[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
additional information
?
-
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 + quinone
[DsbA protein] carrying a disulfide bond + quinol
overall reaction
-
-
?
[DsbA protein] with reduced L-cysteine residues + quinone
[DsbA protein] carrying a disulfide bond + 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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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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C41S/C44S/C102S/C130S
inactive
C41S/C44S/C102S/C130S
-
inactive
-
R118H
-
missense mutation
-
T73I
-
missense mutation
-
V16M
-
missense mutation
-
V56A
-
missense mutation
-
C41A/C44A
-
the mutant has two cysteine residues at Cys104 and Cys130 compared to the wild type enzyme with Cys41, Cys44, Cys104 and Cys130
R48A
-
the mutant shows strongly reduced DsbA protein oxidation activity
R48K
-
the mutant shows strongly reduced DsbA protein oxidation activity
Y46A
-
the mutant shows strongly reduced DsbA protein oxidation activity
Y46P
-
the mutant shows strongly reduced DsbA protein oxidation activity
Y46P/E47P
-
the mutant shows strongly reduced DsbA protein oxidation activity
R48H
-
the mutant shows reduced activity compared to the wild type enzyme
R48H
-
the mutant shows reduced affinity for ubiquinone
R48H
-
the mutant shows strongly reduced DsbA protein oxidation activity
additional information
-
construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
additional information
construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
additional information
-
construction of mutant CtDsbB-CCSS, in which periplasmic loop 2 Cys98 and Cys104 are mutated to serines. In the presence of CtDsbB-CCSS or CtDsbB-SSCC, CtDsbA catalysed oxidation of the peptide substrate is markedly reduced relative to wild-type CtDsbB, although oxidation proceeds more rapidly than observed for negative controls containing only buffer, or the wild-type CtDsbB variant alone. The disulfide bonds present in periplasmic loops P1 and P2 of CtDsbB are each required for complete oxidation of CtDsbA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
DsbA-DsbB interaction through their active site cysteines Evidence from an odd cysteine mutant of DsbA
J. Biol. Chem.
270
17072-17074
1995
Escherichia coli
brenda
Inaba, K.; Takahashi, Y.H.; Ito, K.
Reactivities of quinone-free DsbB from Escherichia coli
J. Biol. Chem.
280
33035-33044
2005
Escherichia coli
brenda
Yazawa, K.; Furusawa, H.; Okahata, Y.
Real-time monitoring of intermediates reveals the reaction pathway in the thiol-disulfide exchange between disulfide bond formation protein A (DsbA) and B (DsbB) on a membrane-immobilized quartz crystal microbalance (QCM) system
J. Biol. Chem.
288
35969-35981
2013
Escherichia coli
brenda
Inaba, K.
Protein disulfide bond generation in Escherichia coli DsbB-DsbA
J. Synchrotron Radiat.
15
199-201
2008
Escherichia coli
brenda
Hayashi, S.; Mitsuko, A.; Kimoto, M.; Furukawa, S.; Nakazawa, T.
The dsbA-dsbB disulfide bond formation system of Burkholderia cepacia is involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance
Microbiol. Immunol.
44
41-50
2000
Burkholderia cepacia, Burkholderia cepacia KF1
brenda
Collet, J.; Bardwell, J.
Oxidative protein folding in bacteria
Mol. Microbiol.
44
1-8
2002
Escherichia coli
brenda
Christensen, S.; Halili, M.; Strange, N.; Petit, G.; Huston, W.; Martin, J.; McMahon, R.
Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development
PLoS ONE
14
e0222595
2019
Chlamydia trachomatis, Chlamydia trachomatis (G4NNC5), Chlamydia trachomatis A2497 (G4NNC5)
brenda
Inaba, K.; Takahashi, Y.; Ito, K.; Hayashi, S.
Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB
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