Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.

@article{Araki2011FunctionalIV,
  title={Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.},
  author={Kazutaka Araki and Kazuhiro Nagata},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 37},
  pages={32705-12}
}
Oxidative protein folding in the endoplasmic reticulum is supported by efficient electron relays driven by enzymatic reactions centering on the ERO1-protein-disulfide isomerase (PDI) pathway. A controlled in vitro oxygen consumption assay was carried out to analyze the ERO1-PDI reaction. The results showed the pH-dependent oxidation of PDI by ERO1α. Among several possible disulfide bonds regulating ERO1α activity, Cys(94)-Cys(131) and Cys(99)-Cys(104) disulfide bonds are dominant regulators by… CONTINUE READING