Histidines, histamines and imidazoles as glycosidase inhibitors

Field, R. A., Haines, A. H., Chrystal, E. J.T. and Luszniak, M. C. (1991) Histidines, histamines and imidazoles as glycosidase inhibitors. Biochemical Journal, 274 (3). pp. 885-889. ISSN 0264-6021

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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 β-glucosidase, yeast α-glucosidase, and Escherichia coli β-galactosidase. The addition of a hydrophobic group to the basic imidazole nucleus greatly enhances binding to both the α- and β-glucosidases. L-Histidine β-naphthylamide (K(i) 17 μM) is a potent competitive inhibitor of sweet-almond β-glucosidase as is ω-N-acetylhistamine (K(i) 35 μM), which inhibits the sweet-almond β-glucosidase at least 700 times more strongly than either yeast α-glucosidase or Escherichia coli β-galactosidase, and suggests potential for the development of selective reversible β-glucosidase inhibitors. A range of hydrophobic ω-N-acylhistamines were synthesized and shown to be among the most potent inhibitors of sweet-almond β-glucosidase reported to date.

Item Type:	Article
Uncontrolled Keywords:	biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School:	Faculty of Science > School of Chemistry, Pharmacy and Pharmacology Faculty of Science > School of Chemistry (former - to 2024)
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	11 Sep 2024 14:30
Last Modified:	06 Feb 2025 12:15
URI:	https://ueaeprints.uea.ac.uk/id/eprint/96728
DOI:	10.1042/bj2740885

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