Thioester hydrolysis by matrix metalloproteinases.

@article{Stein1994ThioesterHB,
  title={Thioester hydrolysis by matrix metalloproteinases.},
  author={Ross L. Stein and M Izquierdo-Martin},
  journal={Archives of biochemistry and biophysics},
  year={1994},
  volume={308 1},
  pages={274-7}
}
Substrate specificity studies from this laboratory suggested that Ac-Pro-Leu-Ala-Nva-TrpNH2, and its thioester derivative, Ac-Pro-Leu-Ala-SNva-TrpNH2, would be substrates for stromelysin (SLN). In this paper, we report that both peptides are efficiently hydrolyzed not only by SLN but also by two other matrix metalloproteinases, collagenase and gelatinase, and by the bacterial metalloproteinase thermolysin. The pH-dependence of kc/Km for the SLN-catalyzed hydrolysis of Ac-Pro-Leu-Ala-SNva-TrpNH2… CONTINUE READING