1.8.5.9: protein dithiol:quinone oxidoreductase DsbB
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For detailed information about protein dithiol:quinone oxidoreductase DsbB, go to the full flat file.
Reaction
Synonyms
C. trachomatis disulfide bond protein B, CtDsbB, disulfide bond formation protein B, disulfide bond oxidoreductase B, disulfide bond protein B, disulfide-bond formation protein B, DsbB, membrane protein disulfide bond protein B, Rv2968c, thiol:disulfide oxidoreductase, VKOR homolog
ECTree
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Reference on EC 1.8.5.9 - protein dithiol:quinone oxidoreductase DsbB
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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
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
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
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
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
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)
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
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)
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
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)
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
Inaba, K.; Takahashi, Y.H.; Ito, K.
Reactivities of quinone-free DsbB from Escherichia coli
J. Biol. Chem.
280
33035-33044
2005
Escherichia coli
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
Inaba, K.
Protein disulfide bond generation in Escherichia coli DsbB-DsbA
J. Synchrotron Radiat.
15
199-201
2008
Escherichia coli
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
Collet, J.; Bardwell, J.
Oxidative protein folding in bacteria
Mol. Microbiol.
44
1-8
2002
Escherichia coli
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)
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
Proc. Natl. Acad. Sci. USA
103
287-292
2006
Escherichia coli
Dutton, R.; Boyd, D.; Berkmen, M.; Beckwith, J.
Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
Proc. Natl. Acad. Sci. USA
105
11933-11938
2008
Bacteroides fragilis, Escherichia coli, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Bacteroides fragilis NCTC9343
Guilhot, C.; Jander, G.; Martin, N.; Beckwith, J.
Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
Proc. Natl. Acad. Sci. USA
92
9895-9899
1995
Escherichia coli
Kobayashi, T.; Kishigami, S.; Sone, M.; Inokuchi, H.; Mogi, T.; Ito, K.
Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
Proc. Natl. Acad. Sci. USA
94
11857-11862
1997
Escherichia coli
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