The C-terminal region of the proprotein convertase 1/3 (PC1/3) exerts a bimodal regulation of the enzyme activity in vitro.

@article{Rabah2007TheCR,
  title={The C-terminal region of the proprotein convertase 1/3 (PC1/3) exerts a bimodal regulation of the enzyme activity in vitro.},
  author={Nadia Rabah and D. Ludovic Gauthier and Jimmy D. Dikeakos and Timothy L. Reudelhuber and Claude Lazure},
  journal={The FEBS journal},
  year={2007},
  volume={274 13},
  pages={3482-91}
}
The proprotein convertase PC1/3 preferentially cleaves its substrates in the dense core secretory granules of endocrine and neuroendocrine cells. Similar to most proteinases synthesized first as zymogens, PC1/3 is synthesized as a larger precursor that undergoes proteolytic processing of its signal peptide and propeptide. The N-terminally located propeptide has been shown to be essential for folding and self-inhibition. Furthermore, PC1/3 also possesses a C-terminal region (CT-peptide) which… CONTINUE READING