Differential activation of endopeptidase EC 3.4.24.15 toward natural and synthetic substrates by metal ions.

@article{Wolfson1996DifferentialAO,
  title={Differential activation of endopeptidase EC 3.4.24.15 toward natural and synthetic substrates by metal ions.},
  author={Adele J Wolfson and Corie N. Shrimpton and Robert Lew and Alexander Ian Smith},
  journal={Biochemical and biophysical research communications},
  year={1996},
  volume={229 1},
  pages={341-8}
}
The activity of endopeptidase EC 3.4.24.15 (thimet oligopeptidase, EP 24.15), as measured by cleavage of a quenched fluorescent substrate, 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys (2,4-dinitrophenyl), was increased 2-3 fold by the addition of 1 mM Mn2+ or of 10 mM Ca2+. The inhibitory capability of a specific EP. 24.15 inhibitor, N-[1-(R,S)-carboxy… CONTINUE READING