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Publication Abstract from PubMed

Retaining LeLoir glycosyltransferases catalyze the formation of glycosidic bonds between nucleotide sugar donors and carbohydrate acceptors. The anomeric selectivity of trehalose transferase from Thermoproteus uzoniensis was investigated for both d- and l-glycopyranose acceptors. The enzyme couples a wide range of carbohydrates, yielding trehalose analogues with conversion and enantioselectivity of >98%. The anomeric selectivity inverts from alpha,alpha-(1 --> 1)-glycosidic bonds for d-glycopyranose acceptors to alpha,beta-(1 --> 1)-glycosidic bonds for l-glycopyranose acceptors, while (S)-selectivity was retained for both types of sugar acceptors. Comparison of protein crystal structures of trehalose transferase in complex with alpha,alpha-trehalose and an unnatural alpha,beta-trehalose analogue highlighted the mechanistic rationale for the observed inversion of anomeric selectivity.

Anomeric Selectivity of Trehalose Transferase with Rare l-Sugars.,Mestrom L, Marsden SR, van der Eijk H, Laustsen JU, Jeffries CM, Svergun DI, Hagedoorn PL, Bento I, Hanefeld U ACS Catal. 2020 Aug 7;10(15):8835-8839. doi: 10.1021/acscatal.0c02117. Epub 2020 , Jul 22. PMID:32953231^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.