Glycosyltransferase and its application to glycodiversification of natural products
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摘要
Glycosyltransferase (GT) catalyzes the transfer of a sugar moiety to acceptor substrates such as secondary metabolites. The majority of GTs has two structural folds, GT-A and GT-B based on 3-D structural analysis. The limited structural fold diversity is compensated by a highly divergent acceptor binding domain for conferring sufficient substrate promiscuity. Various GTs have been engineered to further enhance the glucose transfer activity and expand substrate promiscuity by error-prone PCR and site-directed mutagenesis. Engineered GT-catalyzed glycosylation will certainly play a key role in the generation of scaffold for new drug discovery and control of drug pharmacokinetics.

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