Differences in the structural requirements for selective interaction with neutral metalloendopeptidase (enkephalinase) or angiotensin-converting enzyme. Molecular investigation by use of new thiol inhibitors.

@article{FourniZaluski1984DifferencesIT,
  title={Differences in the structural requirements for selective interaction with neutral metalloendopeptidase (enkephalinase) or angiotensin-converting enzyme. Molecular investigation by use of new thiol inhibitors.},
  author={Marie-Claude Fourni{\'e}-Zaluski and Edgar Lucas and Gabriel Waksman and B. Roques},
  journal={European journal of biochemistry},
  year={1984},
  volume={139 2},
  pages={267-74}
}
Despite the similarities in their mechanism of action, the structural requirements for selective interaction with angiotensin-converting enzyme or enkephalinase are different. Inhibitory potency of a series of new mercaptoalkanoyl amino acids were determined on pure angiotensin-converting enzyme (EC 3.4.15.1) from porcine plasma and on neutral metalloendopeptidase (EC 3.4.24.11) purified from rat brain. This latter enzyme, first designated as enkephalinase, seems to be synaptically involved in… CONTINUE READING