Recent developments in the enzymatic O-glycosylation of flavonoids
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The glycosylation of bioactive compounds, such as flavonoids, is of particular relevance, as it modulates many of their pharmacokinetic parameters. This article reviews the literature between 2010 and the end of 2015 that deals with the enzymatic O-glycosylation of this class of compounds. Enzymes of glycosyltransferase family 1 remain the biocatalysts of choice for glycodiversification of flavonoids, in spite of relatively low yields. Transfers of 14 different sugars, in addition to glucose, were reported. Several Escherichia coli strains were metabolically engineered to enable a (more efficient) synthesis of the required donor during in vivo glycosylations. For the transfer of glucose, enzymes of glycoside hydrolase families 13 and 70 were successfully assayed with several flavonoids. The number of acceptor substrates and of regiospecificities characterized so far is smaller than for glycosyltransferases. However, their glycosyl donors are much cheaper and yields are considerably higher. A few success stories of enzyme engineering were reported. These improved the catalytic efficiency as well as donor, acceptor, or product ranges. Currently, the development of appropriate high-throughput screening systems appears to be the major bottleneck for this powerful technology.
KeywordsFlavonoid Glycosylation Glycosyltransferase Glycoside hydrolase
The author thanks the Bundesministerium für Forschung und Technologie for repeated funding of the work carried out in his laboratory.
Compliance with ethical standards
Conflict of interest
The author declares that he has no conflict of interest.
This article does not contain any studies with human participants or animals performed by the author.
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