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Pathways of disulfide bond formation in Escherichia coli

Publication Type:

Journal Article

Authors:

Messens,J.; Collet,J.F.

Source:

Int. J. Biochem. Cell Biol., Volume 38, Issue 7, p.1050 - 1062 (2006)

URL:

PM:16446111

Keywords:

Amino Acid Sequence; Animals; Bacterial Proteins; genetics; metabolism; Catalysis; Cysteine; chemistry; Dimerization; Disulfides; Endoplasmic Reticulum; Escherichia coli; Membrane Proteins; Models; Molecular; Molecular Structure; Oxidation-Reduction; Prote

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

Notes:

DA - 20060403
IS - 1357-2725 (Print)
LA - eng
PT - Journal Article
PT - Review
RN - 0 (Bacterial Proteins)
RN - 0 (Disulfides)
RN - 0 (DsbB protein, Bacteria)
RN - 0 (Membrane Proteins)
RN - 52-90-4 (Cysteine)
RN - 52500-60-4 (Thioredoxins)
RN - EC 5.3.4.1 (Protein Disulfide-Isomerase)
SB - IM