Glycosyl special

Science 200T,21(5512) 2263. (This issue contains a special section entitled Carbohydrates and Glycobiology. It contains articles on the synthesis, structural determination, and functions of sugar-containing molecules and the roles of glycosylation in the immune system). 

E. coli, Bacillus and Pseudomonas present quite a solid base for the production of non-glycosylated proteins. Nevertheless, a number of other prokaryotic expression hosts exist that are not as well established and which show features that are not present in the major expression organisms, and this could be extremely useful for special case proteins. 

Carbohydrate derivatives, in which one or more of the oxygen atoms bonded directly to the carbon skeleton have been replaced by sulfur, are termed thiosugars. The placement of the sulfur atom at the anomeric position constitutes a special case, because thioglycosides, alkyl, aryl and heterocyclic, occupy a very important place as versatile glycosyl donors in glycosidation methodology. Anomeric thiocarbonyl compounds, on the contrary, have been less explored, although their potential and scope is likely to be similar. 

High selectivity and substrate specificity of glycosyl transferases make them valuable catalysts for special linkages in polymer-supported synthesis. There is, however, still a rather limited set of enzymes available to date, and the need to synthesize a variety of natural and non-natural oligosaccharides prevails. Particularly with regard to combinatorial approaches, chemical solid-phase oligosaccharide synthesis promises to meet the demands most effectively. 

Special Applications of Glycosyl Phosphates in Oligosaccharide Synthesis... 

This book covers all of the most recent (at the time of writing) developments in the field of solid support oligosaccharide synthesis. Included are chapters discussing different synthetic strategies, glycosylation protocols, the use of solid supports versus soluble polymeric supports and on-resin analytical methods. Special topics such as the formation of [3-glycosidic linkages on solid support are also discussed. 

In transit through the ER and Golgi, the proteins acquire oligosaccharide side chains attached commonly at serine or threonine residues (O-linked) or at asparagine residues (N-linked). N-linked glycosylation requires participation of a special lipid called dolichol phosphate. 

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