1.8.5.9: protein dithiol:quinone oxidoreductase DsbB
This is an abbreviated version!
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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General Information
General Information on EC 1.8.5.9 - protein dithiol:quinone oxidoreductase DsbB
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malfunction
metabolism
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the enzyme facilitates the formation of disulfide bonds in periplasmic proteins but does not facilitate the formation of intramembraneous disulfides
physiological function
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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
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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
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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
disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. The second disulfide of CtDsbA does not influence interaction with CtDsbB
physiological function
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the enzyme is required for virulence in Burkholderia pseudomallei
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physiological function
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disulfide bond protein A (DsbA) is the primary oxidase in the disulfide oxidative pathway of bacteria. DsbA catalyses the introduction of disulfide bonds into reduced and folding proteins in concert with a membrane protein partner DsbB. DsbB uses a quinone cofactor as an electron acceptor, and together the DsbA-DsbB pair ultimately shuttle electrons from a reduced protein substrate to molecular oxygen via the respiratory pathway. CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. The second disulfide of CtDsbA does not influence interaction with CtDsbB
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