Enzyme-catalyzed formation of glycosidic linkages.
Significant progress has recently been achieved in the use of glycosidases and glycosyltransferases as synthetic tools. Glycosidases have been used to synthesize trisaccharides with a reasonable overall yield, as well as high-mannose neoglycoconjugates. Studies on glycosyltransferases have defined reaction mechanisms and demonstrated reasonable substrate tolerance of these enzymes. Effective methodology for the synthesis of defined glycoproteins has also been demonstrated.
Watt
G M
GM
Edinburgh Centre for Protein Technology, Department of Chemistry, University of Edinburgh, UK.
Lowden
P A
PA
Flitsch
S L
SL
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006001:Glycoconjugates / Q000096:biosynthesis; D006023:Glycoproteins / Q000096:biosynthesis*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006027:Glycosides / Q000096:biosynthesis*; D016695:Glycosyltransferases / Q000378:metabolism*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009844:Oligosaccharides / Q000096:biosynthesis*; D013379:Substrate Specificity
D006001:Glycoconjugates; D006023:Glycoproteins; D006027:Glycosides; D009844:Oligosaccharides; D016695:Glycosyltransferases; D006026:Glycoside Hydrolases