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Article

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.

Journal of molecular biology - 11 Apr 2008

Pan Jonathan L, Sliskovic Inga, Bardwell James C A

Abstract excerpt

Disulfide bond formation occurs in secreted proteins in Escherichia coli when the disulfide oxidoreductase DsbA, a soluble periplasmic protein, nonspecifically transfers a disulfide to a substrate protein. The catalytic disulfide of DsbA is regenerated by the inner-membrane protein DsbB. To help identify the specificity determinants in DsbB and to understand the nature of the kinetic barrier preventing direct...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 18325532
DOI: 10.1016/j.jmb.2008.01.058
PMCID: PMC2391272

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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