Switching between O- and C-Glycosyltransferase through Exchange of Active-Site Motifs

Authors

  • Alexander Gutmann,

    1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/1, 8010 Graz (Austria)
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  • Prof. Dr. Bernd Nidetzky

    Corresponding author
    1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/1, 8010 Graz (Austria)
    • Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/1, 8010 Graz (Austria)
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  • Financial support from the Austrian Science Fund (DK Molecular Enzymology W901-B05) is gratefully acknowledged. Prof. R. Edwards and Prof. K. Stich kindly provided the OsCGT and PcOGT gene, respectively.

Abstract

original image

Mechanistic implications: Distinct active-site motifs in plant aryl glucosyltransferases of the GT-1 family differentiate between C- and O-glycosylation activity on a phloretin acceptor. In the implicated protein design principle the exchange of active-site motifs results in reversible switch between C/O-glycoside specificity. The proposed mechanism of the C-glycosyltransferase involves direct nucleophilic displacement at the anomeric carbon.

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