title: A potential fortuitous binding of inhibitors of an inverting family GH9 β-glycosidase derived from isofagomine.
abstract: Using structural insight, the binding mode of isofagomine-derived inhibitors with family GH9 glycosidases is achieved via the study of Alicyclobacillus acidocaldarius (AaCel9A) endoglucanase. In contrast to what was observed in the first report using these compounds with inverting glycosidases from family GH6, these inhibitors do not adopt a distorted conformation in the active site.
authors.affiliation: Laboratoire d'Enzymologie et Biochimie Structurales (LEBS), CNRS, Avenue de la Terrasse, 91198, Gif-sur-Yvette, France. morera@lebs.cnrs-gif.fr
authors.forename: Solange
authors.initials: S
authors.lastname: Moréra
authors.forename: Armelle
authors.initials: A
authors.lastname: Vigouroux
authors.forename: Keith A
authors.initials: KA
authors.lastname: Stubbs
mesh_terms: D056450:Alicyclobacillus / Q000201:enzymology*; D002480:Cellulase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D006026:Glycoside Hydrolases; D050112:Imino Pyranoses / Q000737:chemistry* / Q000494:pharmacology*; D008958:Models, Molecular; D011485:Protein Binding
chemical_list: D004791:Enzyme Inhibitors; D050112:Imino Pyranoses; C098432:isofagomine; D006026:Glycoside Hydrolases; D002480:Cellulase