Anomeric Selectivity of Trehalose Transferase with Rare l -Sugars

Luuk Mestrom, Stefan R. Marsden, Hessel Van Der Eijk, Jesper U. Laustsen, Cy M. Jeffries, Dmitri I. Svergun, Peter Leon Hagedoorn, Isabel Bento, Ulf Hanefeld

Research output: Contribution to journalArticleScientificpeer-review


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 α,α-(1 → 1)-glycosidic bonds for d-glycopyranose acceptors to α,β-(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 α,α-trehalose and an unnatural α,β-trehalose analogue highlighted the mechanistic rationale for the observed inversion of anomeric selectivity.

Original languageEnglish
Pages (from-to)8835-8839
JournalACS Catalysis
Issue number15
Publication statusPublished - 2020


  • glycosidic linkages
  • glycosyltransferase
  • Thermoproteus uzoniensis
  • transferase
  • trehalose

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