earticle

영어

The biological activity of many natural products and pharmaceutically used drugs are attributed by the glycosidic residues attached to it. Generally, the glycosylation determines the competence of the most of the molecules as a drug. Therefore, engineering the sugar moiety in the natural products is one of the most efficient ways of generating novel compounds with diverse pharmacological properties. The screening and engineering of flexible glycosyltransferases from different sources and applying those enzymes for the biosynthesis of novel small molecule glycosides is still significantly demanding. In this context, we have identified a novel glycosyltransferase (YjiC) from Bacillus licheniformis and applied to glycosylate small molecule natural products like, flavonoids, isoflavonoids, chalcones, stillbenes, curcuminoids etc. The substrate flexibility of thus identified glycosyltaransferase is found to have broad, which resulted to generate a number of natural product glycosides including novel compounds. The enzyme glycosylates non-regiospecifically at suitable hydroxyl groups to produce O-glucosides of compounds. Moreover, this glycosyltransferase has shown flexibility towards NDP-sugar donors. This property of the enzyme would help to engineer the sugar moiety of most of the small molecules which might exhibit potentially different biological activities. The exchange of sugar moiety might help to modulate the biological application of the parent bioactive compounds. Plenty of biologically active aglycones and their glycoside derivatives are characterized to have diverse biological activities against wide-range of diseases. The production of such pharmaceutically important glycoside compounds and their glyco-engineering to alter biological function would be noteworthy in scientific world to develop a novel drug for future use.