General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability

Accessing large numbers of structurally diverse glycans and derivatives is essential to functional glycomics. We showed a general tolerance of galactosyltransferases toward uridine-diphosphate-galactosamine (UDP-GalN), which is not a commonly used sugar nucleotide donor. The property was harnessed to develop a two-step chemoenzymatic strategy for facile synthesis of novel and divergent N-acetylgalactosamine (GalNAc)-glycosides and derivatives in preparative scales. The discovery and the application of the new property of existing glycosyltransferases expand their catalytic capabilities in generating novel carbohydrate linkages, thus prompting the synthesis of diverse glycans and glycoconjugates for biological studies.

Automated summary

Accessing structurally diverse glycans is crucial for functional glycomics. Our study demonstrates the general tolerance of galactosyltransferases towards UDP-GalN, enabling the synthesis of novel GalNAc-glycosides. This discovery expands the catalytic capabilities of glycosyltransferases, facilitating the synthesis of diverse glycans and glycoconjugates for biological studies.