Biochemical characterisation of an α1,4 galactosyltransferase from Neisseria weaveri for the synthesis of α1,4-linked galactosides

Kun Huang, Andrea Marchesi, Kristian Hollingsworth, Peter Both, Ashley P Mattey, Edward Pallister, Helene Ledru, Simon Charnock, M. Carmen Galan, W Bruce Turnbull, Fabio Parmeggiani, Sabine L. Flitsch

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Abstract

The human cell surface trisaccharide motifs globotriose and P1 antigen play key roles in infections by pathogenic bacteria, which makes them important synthetic targets as antibacterial agents. Enzymatic strategies to install the terminal α1,4-galactosidic linkage are very attractive but have only been demonstrated for a limited set of analogues. Herein, a new bacterial α1,4 galactosyltransferase from N. weaveri was cloned and produced recombinantly in E. coli BL21 (DE3) cells, followed by investigation of its substrate specificity. We demonstrate that the enzyme can tolerate galactosamine (GalN) and also 6-deoxygalactose and 6-deoxy-6-fluorogalactose as donors, and lactose and N-acetyllactosamine as acceptors, leading directly to analogues of Gb3 and P1 that are valuable chemical probes and showcase how biocatalysis can provide fast access to a number of unnatural carbohydrate analogues.
Original languageEnglish
JournalOrganic & biomolecular chemistry
Early online date30 Mar 2020
DOIs
Publication statusE-pub ahead of print - 30 Mar 2020

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