Stereoselective synthesis of conformationally constrained glycosylated amino acids using an enzyme-catalyzed desymmetrization.
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.
Lane
Jonathan W
JW
Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309-0215, USA.
Halcomb
Randall L
RL
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
D000596:Amino Acids; D006020:Glycopeptides; D007202:Indicators and Reagents; D009844:Oligosaccharides; D016695:Glycosyltransferases