In recent years, carbohydrate-processing enzymes have become the enzymes of choice in many applications thanks to their stereoselectivity and efficiency. This review presents recent developments in glycosidase-catalyzed synthesis via two complementary approaches: the use of wild-type enzymes with engineered substrates, and mutant glycosidases. Genetic engineering has recently produced glucuronyl synthases, an inverting xylosynthase and the first mutant endo-β-N-acetylglucosaminidase. A thorough selection of enzyme strains and aptly modified substrates have resulted in rare glycostructures, such as N-acetyl-β-galactosaminuronates, β1,4-linked mannosides and α1,4-linked galactosides. The efficient selection of mutant enzymes is facilitated by high-throughput screening assays involving the co-expression of coupled enzymes or chemical complementation. Selective glycosidase inhibitors and highly specific glycosidases are finding attractive applications in biomedicine, biology and proteomics. © 2008 Elsevier Ltd. All rights reserved.
Mendeley saves you time finding and organizing research
Choose a citation style from the tabs below