title: Stereoselective synthesis of conformationally constrained glycosylated amino acids using an enzyme-catalyzed desymmetrization.
abstract: As part of an effort to probe the mechanism by which glycosyltransferases recognize glycoproteins and assemble the core structures of O-linked oligosaccharides, constrained glycopeptides, compounds 2 and 3, based on the alpha-N-acetylgalactosaminyl serine substructure 1, were designed. In this paper we describe a stereoselective preparation of protected versions of these compounds. A pig liver esterase-catalyzed enzymatic desymmetrization of a diacetate substrate, 10, was employed as a key component in the synthesis.
authors.affiliation: Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309-0215, USA.
authors.forename: Jonathan W
authors.initials: JW
authors.lastname: Lane
authors.forename: Randall L
authors.initials: RL
authors.lastname: Halcomb
mesh_terms: D000596:Amino Acids / Q000138:chemical synthesis*; D002384:Catalysis; D006020:Glycopeptides / Q000138:chemical synthesis*; D006031:Glycosylation; D016695:Glycosyltransferases / Q000378:metabolism*; D007202:Indicators and Reagents; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D009844:Oligosaccharides / Q000737:chemistry*; D013237:Stereoisomerism
chemical_list: D000596:Amino Acids; D006020:Glycopeptides; D007202:Indicators and Reagents; D009844:Oligosaccharides; D016695:Glycosyltransferases