title: Glycosidase mechanisms.
abstract: The three-dimensional structure of glycosidases and of their complexes and the study of transition-state mimics reveal structural details that correlate with mechanism. Of particular interest are the transition-state conformations harnessed by individual enzymes and the substrate distortion observed in enzyme-ligand complexes. 3D-structure in synergy with transition-state mimicry opens the way for mechanistic interpretation of enzyme inhibition and for the development of therapeutic agents.
authors.affiliation: Laboratorium für Organische Chemie, ETH Hönggerberg, HCI H317, CH-8093 Zürich, Switzerland.
authors.forename: Andrea
authors.initials: A
authors.lastname: Vasella
authors.forename: Gideon J
authors.initials: GJ
authors.lastname: Davies
authors.forename: Matthias
authors.initials: M
authors.lastname: Böhm
mesh_terms: D002384:Catalysis; D004791:Enzyme Inhibitors / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D006868:Hydrolysis; D008024:Ligands; D015394:Molecular Structure; D016296:Mutagenesis; D011487:Protein Conformation; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D004791:Enzyme Inhibitors; D008024:Ligands; D006026:Glycoside Hydrolases