Substrate requirements of human rhinovirus 3C protease for peptide cleavage in vitro.

@article{Cordingley1990SubstrateRO,
  title={Substrate requirements of human rhinovirus 3C protease for peptide cleavage in vitro.},
  author={Michael G. Cordingley and Peggy Callahan and Vinod Sardana and Victor M. Garsky and R. J. Colonno},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 16},
  pages={9062-5}
}
A series of synthetic peptides representing authentic proteolytic cleavage sites of human rhinovirus type 14 were assayed as substrates for purified 3C protease. Competition cleavage assays were employed to determine the relative specificity constants (Kcat/Km) for substrates with sequences related to the viral 2C-3A cleavage site. Variable length peptides representing the 2C-3A cleavage site were cleaved with comparable efficiency. These studies defined a minimum substrate of 6 amino acids… CONTINUE READING