Enkephalin convertase: Potent, selective, and irreversible inhibitors

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

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

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
Volume111
Issue number3
DOIs
StatePublished - Mar 29 1983
Externally publishedYes

Fingerprint

Carboxypeptidase H
Carboxypeptidase B
Lysine Carboxypeptidase
Arginine
Dicarboxylic Acids
Enkephalins
Biosynthesis
Lysine
Derivatives
Kinetics
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Enkephalin convertase : Potent, selective, and irreversible inhibitors. / Fricker, Lloyd D.; Plummer, Thomas H.; Snyder, Solomon H.

In: Biochemical and Biophysical Research Communications, Vol. 111, No. 3, 29.03.1983, p. 994-1000.

Research output: Contribution to journalArticle

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