Histidines, histamines and imidazoles as glycosidase inhibitors

R.A. Field, A.H. Haines, E.J.T. Chrystal, M.C. Luszniak

Research output: Contribution to journalArticlepeer-review

Abstract

This present study reports the ability of a range of derivatives of L-histidine, histamine and imidazole to act as inhibitors of sweet-almond beta-glucosidase, yeast alpha-glucosidase and Escherichia coli beta-galactosidase. The addition of a hydrophobic group to the basic imidazole nucleus greatly enhances binding to both the alpha- and beta-glucosidases. L-Histidine (beta-naphthylamide (Ki 17 microM) is a potent competitive inhibitor of sweet-almond beta-glucosidase as is omega-N-acetylhistamine (K1 35 microM), which inhibits the sweet-almond beta-glucosidase at least 700 times more strongly than either yeast alpha-glucosidase or Escherichia coli beta-galactosidase, and suggests potential for the development of selective reversible beta-glucosidase inhibitors. A range of hydrophobic omega-N-acylhistamines were synthesized and shown to be among the most potent inhibitors of sweet-almond beta-glucosidase reported to date.

Original languageUndefined
Pages (from-to)885-889
Number of pages5
JournalBiochemical Journal
Volume274
Issue numberPt 3
DOIs
Publication statusPublished - 1991

Research Beacons, Institutes and Platforms

  • Manchester Institute of Biotechnology

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