PMID:15546661

Citation	Nakamoto, H and Bardwell, JC (2004) Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim. Biophys. Acta 1694:111-9
Abstract	Disulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of cysteine pairs is achieved by the transfer of disulfides from the highly oxidizing DsbA/DsbB catalytic machinery to substrate proteins. The oxidizing power utilized by this system comes from the membrane-embedded electron transport system, which utilizes molecular oxygen as a final oxidant. Proofreading of disulfide bond formation is performed by the DsbC/DsbD system, which has the ability to rearrange non-native disulfides to their native configuration. These disulfide isomerization reactions are sustained by a constant supply of reducing power provided by the cytoplasmic thioredoxin system, utilizing NADPH as the ultimate electron source.
Links	PubMed Online version:10.1016/j.bbamcr.2004.02.012
Keywords	Catalysis; Cysteine/chemistry; Cysteine/metabolism; Disulfides/metabolism; Escherichia coli/enzymology; Periplasm/enzymology; Periplasm/metabolism; Protein Disulfide-Isomerases/metabolism; Protein Engineering; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.