Protein disulfide isomerases from C. elegans are equally efficient at thiol-disulfide exchange in simple peptide-based systems but show differences in reactivity towards protein substrates.

@article{Karala2007ProteinDI,
  title={Protein disulfide isomerases from C. elegans are equally efficient at thiol-disulfide exchange in simple peptide-based systems but show differences in reactivity towards protein substrates.},
  author={Anna-Riikka Karala and Panagiotis Psarrakos and Lloyd W Ruddock and Peter Klappa},
  journal={Antioxidants & redox signaling},
  year={2007},
  volume={9 11},
  pages={1815-23}
}
Although the formation of disulfide bonds is an essential process in every living organism, only little is known about the mechanisms in multicellular eukaryotic systems. The reason for this uncertainty is that in addition to the well-known key enzyme protein disulfide isomerase (PDI), several PDI-like proteins are present in the ER of metazoans. In total, there are now 18 PDI-family members in the human endoplasmic reticulum, with different domain architectures and active site chemistries. To… CONTINUE READING