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.
MeSH terms
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Amino Acid Sequence
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Animals
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Catalysis
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Cysteine / chemistry*
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Dimerization
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Disulfides / chemistry*
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Disulfides / metabolism*
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Endoplasmic Reticulum / metabolism
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Escherichia coli / metabolism*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Models, Molecular
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Molecular Structure
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Oxidation-Reduction
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Protein Conformation
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Protein Disulfide-Isomerases / chemistry
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Protein Disulfide-Isomerases / metabolism*
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Protein Folding
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Thioredoxins / chemistry
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Thioredoxins / metabolism
Substances
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Bacterial Proteins
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Disulfides
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DsbB protein, Bacteria
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Membrane Proteins
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Thioredoxins
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Protein Disulfide-Isomerases
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Cysteine