Glycosidases: a key to tailored carbohydrates.
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-beta-N-acetylglucosaminidase. A thorough selection of enzyme strains and aptly modified substrates have resulted in rare glycostructures, such as N-acetyl-beta-galactosaminuronates, beta1,4-linked mannosides and alpha1,4-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.
Bojarová
Pavla
P
Institute of Microbiology, Academy of Sciences of the Czech Republic, Center of Biocatalysis and Biotransformation, Vídenská 1083, CZ-142 20, Praha 4, Czech Republic.
Kren
Vladimír
V
D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000096:biosynthesis*; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D050505:Mutant Proteins / Q000378:metabolism; D015202:Protein Engineering; D040901:Proteomics; D013379:Substrate Specificity
D002241:Carbohydrates; D050505:Mutant Proteins; D006026:Glycoside Hydrolases