Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 18, Issue 16, Pages 3142-3148Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0ob00407c
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Funding
- BBSRC [BB/M029034/1, BB/M028836/1, BB/M028976/1, BB/M028747/1]
- EPSRC [BB/M029034/1, BB/M028836/1, BB/M028976/1, BB/M028747/1]
- Innovate UK: IBCatalyst programme [BB/M029034/1, BB/M028836/1, BB/M028976/1, BB/M028747/1]
- Marie Sklodowska-Curie Innovative Training Network [H2020-MSCA-ITN-2014-ETN-642870]
- European Research Council (ERC) [ProgrES-DVL-788231, COG-648239]
- BBSRC [BB/M028976/1, BB/M028836/1, BB/M028747/1, BB/M029034/1] Funding Source: UKRI
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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 alpha 1,4-galactosidic linkage are very attractive but have only been demonstrated for a limited set of analogues. Herein, a new bacterial alpha 1,4 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.
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