Enkephalin-degrading dipeptidylaminopeptidase: characterization of the active site and selective inhibition.

@article{Chrot1986EnkephalindegradingDC,
  title={Enkephalin-degrading dipeptidylaminopeptidase: characterization of the active site and selective inhibition.},
  author={P Ch{\'e}rot and Jeanne Devin and Marie Claude Fourni{\'e}-Zaluski and Bernard Pierre Roques},
  journal={Molecular pharmacology},
  year={1986},
  volume={30 4},
  pages={
          338-44
        }
}
The enkephalins are degraded in vitro by three types of metallopeptidases including a dipeptidylaminopeptidase (DAP) which releases Tyr-Gly. In order to test the physiological significance of this enzyme in enkephalin metabolism, a membrane-bound DAP from porcine brain was purified. The structural characteristics of the active site of this enzyme were studied using several enkephalin-related fragments as substrates and various peptides as inhibitors. The active site possesses an anionic moiety… CONTINUE READING