Jump to main content
Jump to site search

Issue 90, 2017
Previous Article Next Article

Switching enzyme specificity from phosphate to resveratrol glucosylation

Author affiliations

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 glucosylation. 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.

Graphical abstract: Switching enzyme specificity from phosphate to resveratrol glucosylation

Back to tab navigation

Supplementary files

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., 2017,53, 12181-12184
  •   Request permissions

    Switching enzyme specificity from phosphate to resveratrol glucosylation

    M. Kraus, C. Grimm and J. Seibel, Chem. Commun., 2017, 53, 12181
    DOI: 10.1039/C7CC05993K

Search articles by author

Spotlight

Advertisements