title: Mechanism of catalysis by retaining beta-glycosyl hydrolases.
abstract: Recent structural studies provide a fresh look at the catalytic mechanism of polysaccharide hydrolysis by retaining beta-glycosyl hydrolases. Highlights include insights into saccharide ring distortion, both upon binding and during the course of catalysis, and evidence for the regulation of the pKa of key catalytic residues.
authors.affiliation: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254-9110, USA. awhite@auriga.rose.brandeis.edu
authors.forename: A
authors.initials: A
authors.lastname: White
authors.forename: D R
authors.initials: DR
authors.lastname: Rose
mesh_terms: D000345:Affinity Labels / Q000737:chemistry / Q000378:metabolism; D002236:Carbohydrate Conformation; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry*; D002384:Catalysis; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D004852:Epoxy Compounds / Q000378:metabolism / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D006027:Glycosides / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D000345:Affinity Labels; D002241:Carbohydrates; D004791:Enzyme Inhibitors; D004852:Epoxy Compounds; D006027:Glycosides; D006026:Glycoside Hydrolases; D009113:Muramidase