Abstract
The chemoenzymatic synthesis of glycosaminoglycan (GAG) analogs is described. This chapter is divided into three main sections, each describing the use of one enzyme family in GAG synthesis. First, the polysaccharide lyase enzymes are described. These enzymes play crucial role in obtaining GAG oligosaccharides. Second, GAG synthases, bacterial enzymes that transfer UDP-monosaccharides to acceptor oligosaccharide are described, to obtain homogenous oligosaccahrides and polysaccharides. Finally, GAG sulfotransferases, that play a major role in the biosynthesis, are described for the introduction of sulfo groups to the appropriate positions on the polysaccharide backbone.The chemoenzymatic synthesis of glycosaminoglycan (GAG) analogs is described. This chapter is divided into three main sections, each describing the use of one enzyme family in GAG synthesis. First, the polysaccharide lyase enzymes are described. These enzymes play crucial role in obtaining GAG oligosaccharides. Second, GAG synthases, bacterial enzymes that transfer UDP-monosaccharides to acceptor oligosaccharide are described, to obtain homogenous oligosaccahrides and polysaccharides. Finally, GAG sulfotransferases, that play a major role in the biosynthesis, are described for the introduction of sulfo groups to the appropriate positions on the polysaccharide backbone.
Cite
CITATION STYLE
Avci Fikri Y., DeAngelis Paul L., Liu Jian, & Linhardt Robert J. (2007). Frontiers in Modern Carbohydrate Chemistry (Vol. 960, pp. 253–284). Retrieved from http://dx.doi.org/10.1021/bk-2007-0960.ch015
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.