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Article

An in vivo pathway for disulfide bond isomerization in Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America - 12 Nov 1996

Rietsch A, Belin D, Martin N, Beckwith J

Abstract excerpt

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 roles in the cell in disulfide bond formation and isomerization, respectively. We have shown that mutants in dsbC...

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Identifiers

PMID: 8917542
DOI: 10.1073/pnas.93.23.13048
PMCID: PMC24044

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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