During oxidative protein folding, efficient catalysis of disulfide rearrangements by protein-disulfide isomerase is found to involve an escape mechanism that prevents the enzyme from becoming trapped in covalent complexes with substrates that fail to rearrange in a timely fashion. Protein-disulfide isomerase mutants with only a single active-site cysteine catalyze slow disulfide rearrangements ...

The formation of native intramolecular disulfide bonds is critical for the folding and stability of many secreted proteins. This process involves oxidation of protein thiols to form disulfide bonds as well as rearrangement of any non-native disulfide bonds that might form. Protein disulfide isomerase (PDI) is an abundant catalyst for native disulfide bond formation in the lumen of endoplasmic r...

PLANTS ARE UNIQUE AMONG EUKARYOTES IN HAVING EVOLVED ORGANELLES the protein storage vacuole, protein body, and chloroplast. Disulfide transfer pathways that function in the endoplasmic reticulum (ER) and chloroplasts of plants play critical roles in the development of protein storage organelles and the biogenesis of chloroplasts, respectively. Disulfide bond formation requires the cooperative f...