title: Exploring the synthetic potency of the first furanothioglycoligase through original remote activation.
abstract: Thioglycosidic bonds are of utmost importance in biomolecules as their incorporation led to more stable glycomimetics with potential drug activities. Until now only chemical methods were available for their incorporation into glycofuranosyl conjugates. Herein, we wish to describe the use of the first furanothioglycoligase for the preparation of a great variety of thioaryl derivatives with moderate to excellent yields. Of great interest, a stable 1-thioimidoyl arabinofuranose, classically used in chemical glycosylation, was able to efficiently act as a donor through an original enzymatic remote activation mechanism. Study of the chemical structure as well as the nucleophilicity of the thiol allowed us to optimize this biocatalyzed process. As a consequence, this mutated enzyme constitutes an original, mild and eco-friendly method of thioligation.
authors: Ecole Nationale Supérieure de Chimie de Rennes, CNRS, UMR 6226, Avenue du Général Leclerc, CS 50837, 35708, Rennes Cedex 7, France.
authors: Mélanie
authors: M
authors: Almendros
authors: Dantcho
authors: D
authors: Danalev
authors: Marc
authors: M
authors: François-Heude
authors: Pascal
authors: P
authors: Loyer
authors: Laurent
authors: L
authors: Legentil
authors: Caroline
authors: C
authors: Nugier-Chauvin
authors: Richard
authors: R
authors: Daniellou
authors: Vincent
authors: V
authors: Ferrières
mesh_terms: D001089:Arabinose / Q000031:analogs & derivatives / Q000096:biosynthesis* / Q000737:chemistry; D055162:Biocatalysis; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D008958:Models, Molecular
chemical_list: D001089:Arabinose; D006026:Glycoside Hydrolases