New enkephalinase inhibitors as probes to differentiate "enkephalinase" and angiotensin-converting-enzyme active sites.

@article{Roques1982NewEI,
  title={New enkephalinase inhibitors as probes to differentiate "enkephalinase" and angiotensin-converting-enzyme active sites.},
  author={B. Roques and Marie Claude Fourni{\'e}-Zaluski and Dominique Florentin and Gilles Waksman and A Sassi and P. Chaillet and H Collado and Jean Costentin},
  journal={Life sciences},
  year={1982},
  volume={31 16-17},
  pages={
          1749-52
        }
}
Abstract Thiorphan, N-[(R,S)-3-mercapto-2-benzylpropanoyl]-glycine the first described inhibitor (1) of the peptidyldipeptide hydrolase “enkephalinase” (2) was rationally synthesized taking into account the occurence in the Zn metallopeptidase of a S 1 ′ subsite specific for aromatic or hydrophobic residues (3,4), a feature lacking in angiotensin-converting-enzyme (ACE). In this work, we report new results concerning the differences between “enkephalinase” and ACE at the level of : i) their S 1… Expand
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The enkephalinase inhibitor thiorphan shows antinociceptive activity in mice
TLDR
Thiorphan is reported here that this compound, thiorphan [(DL-3-mercapto-2-benzylpropanoyl)-glycine; patent no. 8008601] protects the enkephalins from the action of enkephalinase in vitro in nanomolar concentration and in vivo after either intracerebroventricular or systemic administration. Expand
High-affinity enkephalin-degrading peptidase in brain is increased after morphine
TLDR
The presence of a high-affinity peptidase in a particulate fraction of mouse striatum splitting the Leu-enkephalin molecule with release of a tripeptide fragment and exhibiting definite substrate specificity suggests that it might be associated with enkphalinergic transmission. Expand
Rational design of enkephalinase inhibitors: substrate specificity of enkephalinase studied from inhibitory potency of various dipeptides.
Abstract The inhibitory potency (IC 50 ) of a variety of dipeptides regarding enkephalinase (enkephalin carboxydipeptidase) activity from mouse striatum indicates that the substrate specificity ofExpand
Angiotensin‐converting enzyme inhibitors: Medicinal chemistry and biological actions
TLDR
Pharmacological and clinical studies on ACE inhibitors of novel chemical structure will establish their utility as antihypertensive agents and may lead to greater understanding of the mechanism of action of all ACE inhibitors. Expand