|Title||Pathways of disulfide bond formation in Escherichia coli.|
|Publication Type||Journal Article|
|Year of Publication||2006|
|Authors||Messens, J., and J-F. Collet|
|Journal||Int J Biochem Cell Biol|
|Type of Article||redox|
|Keywords||Amino Acid Sequence, Animals, Bacterial Proteins, Catalysis, Cysteine, Dimerization, Disulfides, Endoplasmic Reticulum, Escherichia coli, Membrane Proteins, Models, Molecular, Molecular Structure, Oxidation-Reduction, Protein Conformation, Protein Disulfide-Isomerases, Protein Folding, Thioredoxins|
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.
|Alternate Journal||Int. J. Biochem. Cell Biol.|
Pathways of disulfide bond formation in Escherichia coli.