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Switching enzyme specificity from phosphate to resveratrol glucosylation

Abstract

Here we present a point mutation-triggered domain shift which switches the acceptor preference of a sucrose phosphorylase from phosphate to a variety of large polyphenolic compounds including resveratrol and quercetin, enabling their efficient glycosylation. The variant possesses a high affinity for aromatic substrates due to newly introduced π-π- and hydrophobic interactions in the altered active site. The domain shift brings about a substantially enlarged and multifunctional active site for polyphenol glucosylation and rare disaccharide production. The crystal structure of the variant with its product resveratrol-3-α-D-glucoside allows the prediction of the substrate scope and regioselectivity of the aromatic compounds’ glucosylation sites.

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Publication details

The article was received on 31 Jul 2017, accepted on 13 Oct 2017 and first published on 13 Oct 2017


Article type: Communication
DOI: 10.1039/C7CC05993K
Citation: Chem. Commun., 2017, Accepted Manuscript
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    Switching enzyme specificity from phosphate to resveratrol glucosylation

    M. Kraus, C. Grimm and J. Seibel, Chem. Commun., 2017, Accepted Manuscript , DOI: 10.1039/C7CC05993K

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