Abstract
Enzymatic glycosylation catalyzed by glycosyltransferases has great potential for creating bioactive glycosylated small-molecule compounds. Here, we highlight the aglycon promiscuity of a new glycosyltransferase (PlGT7) from Pueraria lobata. PlGT7 exhibited the capability to glycosylate 26 structurally diverse drug-like scaffolds and simple phenolics with UDP-glucose to form O-, S-, and N-glycosides. The reversibility of PlGT7 coupled with its substrate flexibility was also exploited to generate bioactive glucosides with simple sugar donor. These studies indicate the significant potential of an enzymatic approach to the glycosylation of bioactive natural and unnatural products in drug discovery.
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