title: Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis.
abstract: The Michaelis complex of the beta-mannosidase Man2A shows distortion to a (1)S(5) conformation adding to the growing body of evidence supporting catalysis through a boat conformation.
authors.affiliation: Department of Chemistry, The University of York, Heslington, UK.
authors.forename: Wendy A
authors.initials: WA
authors.lastname: Offen
authors.forename: David L
authors.initials: DL
authors.lastname: Zechel
authors.forename: Stephen G
authors.initials: SG
authors.lastname: Withers
authors.forename: Harry J
authors.initials: HJ
authors.lastname: Gilbert
authors.forename: Gideon J
authors.initials: GJ
authors.lastname: Davies
mesh_terms: D001439:Bacteroides / Q000201:enzymology; D006868:Hydrolysis; D008362:Mannosides / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D013816:Thermodynamics; D044902:beta-Mannosidase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D008362:Mannosides; D044902:beta-Mannosidase