title: A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases.
abstract: An in silico survey of the -1 subsite of all known 3D-structures of O-glycoside hydrolases containing a suitably positioned ligand has led to the recognition -- apparently without exceptions -- of a transition state stabilising hydrophobic platform which is complementary to a crucial hydrophobic patch of the ligand. This platform is family-specific and highly conserved. A comprehensive list is given with examples of enzymes belonging to 33 different families. Several typical constellations of platform - protein residues are described.
authors.affiliation: Department of Biochemistry, Physiology and Microbiology, Ghent University, K L Ledeganckstraat 35, B-9000 Gent, Belgium. wim.nerinckx@rug.ac.be
authors.forename: W
authors.initials: W
authors.lastname: Nerinckx
authors.forename: T
authors.initials: T
authors.lastname: Desmet
authors.forename: M
authors.initials: M
authors.lastname: Claeyssens
mesh_terms: D000818:Animals; D001665:Binding Sites; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism*; D013045:Species Specificity
chemical_list: D006026:Glycoside Hydrolases