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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Bibliografiske detaljer

Udgivet i:	Proc Natl Acad Sci U S A
Principais autores:	Rietsch, Arne, Belin, Dominique, Martin, Nancy, Beckwith, Jonathan
Format:	Artigo
Sprog:	Inglês
Udgivet:	National Academy of Sciences 1996
Fag:	Biological Sciences
Online adgang:	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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