Get access
Advertisement

Probing the Aglycon Promiscuity of an Engineered Glycosyltransferase

Authors

  • Richard W. Gantt,

    1. UW National Cooperative Drug Discovery Group, Laboratory for Biosynthetic Chemistry, School of Pharmacy, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705 (USA), Fax: (+1) 608-262-5345
    Search for more papers by this author
  • Randal D. Goff,

    1. UW National Cooperative Drug Discovery Group, Laboratory for Biosynthetic Chemistry, School of Pharmacy, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705 (USA), Fax: (+1) 608-262-5345
    Search for more papers by this author
  • Gavin J. Williams,

    1. UW National Cooperative Drug Discovery Group, Laboratory for Biosynthetic Chemistry, School of Pharmacy, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705 (USA), Fax: (+1) 608-262-5345
    Search for more papers by this author
  • Jon S. Thorson Prof.

    1. UW National Cooperative Drug Discovery Group, Laboratory for Biosynthetic Chemistry, School of Pharmacy, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705 (USA), Fax: (+1) 608-262-5345
    Search for more papers by this author

  • The authors thank the University of Wisconsin-Madison School of Pharmacy Analytical Facility for analytical support. This research was supported in part by National Institutes of Health Grants AI52218 and U19 CA113297.

Abstract

original image

A sweet library: Two variants (wild-type (WT) and a triple mutant) of glycosyltransferase (GT) OleD have been shown to catalyze glycosylation of over 70 substrates, formation of O-, S- and N-glycosidic bonds, and iterative glycosylation (see scheme). Identified substrates include nucleophiles not previously known to act in GT reactions and span numerous natural product and therapeutic drug classes.

Get access to the full text of this article

Ancillary