5MAN

Switching enzyme specificity from phosphate to resveratrol glucosylation.

(2017) Chem Commun (Camb) 53: 12181-12184

• PubMed: 29057405 Search on PubMed
• DOI: https://doi.org/10.1039/c7cc05993k
• Primary Citation of Related Structures:  
  5M9X, 5MAN


• PubMed 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.

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Organizational Affiliation: 

Department of Organic Chemistry, Universit?t Würzburg, Am Hubland, 97074 Würzburg, Germany. seibel@chemie.uni-wuerzburg.de.