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Review
. 2006;38(7):1050-62.
doi: 10.1016/j.biocel.2005.12.011. Epub 2006 Jan 11.

Pathways of disulfide bond formation in Escherichia coli

Joris Messens  1 , Jean-François Collet
Affiliations
Review

Pathways of disulfide bond formation in Escherichia coli

Joris Messens et al. Int J Biochem Cell Biol. 2006.

Abstract

Disulfide bond formation is required for the correct folding of many secreted proteins. Cells possess protein-folding catalysts to ensure that the correct pairs of cysteine residues are joined during the folding process. These enzymatic systems are located in the endoplasmic reticulum of eukaryotes or in the periplasm of Gram-negative bacteria. This review focuses on the pathways of disulfide bond formation and isomerization in bacteria, taking Escherichia coli as a model.

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