earticle

영어

The glycosides are increasingly implicated in biological recognition and signalling mechanisms, thus further elevating their potential as therapeutics. This prominence creates a strong need for efficient and versatile methods for stereo- and regioselective glycoside synthesis. The enzymatic synthesis of glycosidic linkages with carbohydrate-active enzymes has been widely investigated to address this issue and is attractive in their abilities to circumvent often long-winded protection regimes. Glycosyltransferases have proven to be highly efficient in the synthesis of glycosidic linkages. However, the expense of the nucleotide sugar substrates, tight substrate specificity, and low enzyme availability limits their application. Glycosidases area attractive for large-scale application since they are more abundant, relatively inexpensive, exhibit broader acceptor-substrate specificity and use simpler substrates. However, stringent donor specificities and low yield can limit their use. In terms of reaction mechanism, transglycosidases and glycosidases belong to the same group. In this presentation we will focus on the use of transglycosidase and glycosidase for the synthesis of bioactive glycosides. The enzymes we chosen are levansucrase (transglycosidase) and β-glucosidase (glycosidase), respectively. The potential applications of newly made glycosides as well as the biochemical characteristics, substrate specificities, and transglycosylation properties of both enzymes can be discussed.