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

Autor: Fu X; Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA.; Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, 30303, USA., Gadi MR; Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA., Wang S; Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA., Han J; Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA., Liu D; Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA., Chen X; Department of Chemistry, University of California, Davis, Davis, CA, 95616, USA., Yin J; Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA.; Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, 30303, USA., Li L; Department of Chemistry, Georgia State University, Atlanta, GA, 30303, USA.
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2021 Dec 13; Vol. 60 (51), pp. 26555-26560. Date of Electronic Publication: 2021 Nov 09.
DOI: 10.1002/anie.202112574
Abstrakt: 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.
(© 2021 Wiley-VCH GmbH.)
Databáze: MEDLINE
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