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Article

Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB.

The Journal of biological chemistry - 24 Feb 2006

Segatori Laura, Murphy Lori, Arredondo Silvia, Kadokura Hiroshi, Gilbert Hiram, Beckwith Jon, Georgiou George

Abstract excerpt

In the bacterial periplasm the co-existence of a catalyst of disulfide bond formation (DsbA) that is maintained in an oxidized state and of a reduced enzyme that catalyzes the rearrangement of mispaired cysteine residues (DsbC) is important for the folding of proteins containing multiple disulfide bonds. The kinetic partitioning of the DsbA/DsbB and DsbC/DsbD pathways partly depends on the ability of DsbB to...

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PMID: 16280324
DOI: 10.1074/jbc.M505453200

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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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