dTDP-deoxysugars are an essential element in the biosynthesis of many natural products produced through secondary metabolism. Through deletion and overexpression of various wild type E. coli enzymes, zuChem is able to accumulate dTDP-4-keto- 6-deoxy-D-glucose (TKDG) in the wild-type strain AB707, creating a production chassis for dTDP- deoxysugars. We reported the successful scalable production of a variety of dTDP-activated deoxysugars and their use in glycodiversification. Because of its promiscuity toward a variety of aglycones, the glycosyltransferase YjiC from Bacillus licheniformis (BlYjiC) was chosen to glycosylate 4-methylumbelliforone. However, we also reported limitations of this enzyme with-respect-to the donor dTDP-activated deoxysugars. This prompted us to express and purify homologues of BlYjiC from other organisms in order to uncover enzymes with enhanced deoxysugar promiscuity. Reported here is an examination of the ability to transfer select dTDP-activated deoxysugars to 4-methylumbelliforone.

Glycosylation of 4-methylumbelliforone with dTDP-deoxysugars by homologues of Bacillus licheniformis YjiC

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.