Enkephalin convertase: Potent, selective, and irreversible inhibitors

Lloyd D. Fricker, Thomas H. Plummer, Solomon H. Snyder

Research output: Contribution to journalArticlepeer-review

63 Scopus citations


Biproduct analogs of lysine and arginine are potent inhibitors of enkephalin convertase, a carboxypeptidase B-like enzyme which appears to be physiologically associated with enkephalin biosynthesis. The most effective derivatives are guanidinoethylmercaptosuccinic acid and guanidinopropylsuccinic acid with respective Ki's of 8.8 and 7.5 nM. These dicarboxylic acid analogs of arginine are several hundred fold more potent towards enkephalin convertase than towards carboxypeptidase B or N. Kinetic analysis indicates the pure competitive nature of the inhibition. Bromoacetyl-D-arginine, an irreversible inhibitor of carboxypeptidase B and N, is also an efficient irreversible inhibitor of enkephalin convertase.

Original languageEnglish (US)
Pages (from-to)994-1000
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Mar 29 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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