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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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書誌詳細
出版年:Proc Natl Acad Sci U S A
主要な著者: Rietsch, Arne, Belin, Dominique, Martin, Nancy, Beckwith, Jonathan
フォーマット: Artigo
言語:Inglês
出版事項: National Academy of Sciences 1996
主題:
オンライン・アクセス: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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