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Field, R. A. 
ORCID: https://orcid.org/0000-0001-8574-0275, 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
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: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 11 Sep 2024 14:30 |
| Last Modified: | 25 Sep 2024 18:09 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96728 |
| DOI: | 10.1042/bj2740885 |
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