Protein disulfide isomerase

B Wilkinson, HF Gilbert - Biochimica et biophysica acta (BBA)-proteins and …, 2004 - Elsevier
B Wilkinson, HF Gilbert
Biochimica et biophysica acta (BBA)-proteins and proteomics, 2004Elsevier
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link
specific cysteines are often added to stabilize a protein or to join it covalently to other
proteins. Disulfide formation, which requires a change in the covalent structure of the
protein, occurs as the protein folds into its three-dimensional structure. In the eukaryotic
endoplasmic reticulum and in the bacterial periplasm, an elaborate system of chaperones
and folding catalysts ensure that disulfides connect the proper cysteines and that the folding …
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure. In the eukaryotic endoplasmic reticulum and in the bacterial periplasm, an elaborate system of chaperones and folding catalysts ensure that disulfides connect the proper cysteines and that the folding protein does not make improper interactions. This review focuses specifically on one of these folding assistants, protein disulfide isomerase (PDI), an enzyme that catalyzes disulfide formation and isomerization and a chaperone that inhibits aggregation.
Elsevier