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An in vivo pathway for disulfide bond isomerization in Escherichia coli

Biochemical studies have shown that the periplasmic protein disulfide oxidoreductase DsbC can isomerize aberrant disulfide bonds. Here we present the first evidence for an in vivo role of DsbC in disulfide bond isomerization. Furthermore, our data suggest that the enzymes DsbA and DsbC play distinct...

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Bibliografiset tiedot
Julkaisussa:Proc Natl Acad Sci U S A
Päätekijät: Rietsch, Arne, Belin, Dominique, Martin, Nancy, Beckwith, Jonathan
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 1996
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Linkit:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC24044/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8917542/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.93.23.13048
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