title: Histidines, histamines and imidazoles as glycosidase inhibitors.
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.
authors.affiliation: School of Chemical Sciences, University of East Anglia, Norwich, U.K.
authors.forename: R A
authors.initials: RA
authors.lastname: Field
authors.forename: A H
authors.initials: AH
authors.lastname: Haines
authors.forename: E J
authors.initials: EJ
authors.lastname: Chrystal
authors.forename: M C
authors.initials: MC
authors.lastname: Luszniak
mesh_terms: D001665:Binding Sites; D001667:Binding, Competitive; D002384:Catalysis; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors*; D006632:Histamine / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D007093:Imidazoles / Q000737:chemistry*
chemical_list: D007093:Imidazoles; D006639:Histidine; D006632:Histamine; D006026:Glycoside Hydrolases