Anomeric Selectivity of Trehalose Transferase with Rare l-Sugars.
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ABSTRACT:
SUBMITTER: Mestrom L
PROVIDER: S-EPMC7493220 | biostudies-literature | 2020 Aug
REPOSITORIES: biostudies-literature
Publications
Anomeric Selectivity of Trehalose Transferase with Rare l-Sugars.
Mestrom Luuk L Marsden Stefan R SR van der Eijk Hessel H Laustsen Jesper U JU Jeffries Cy M CM Svergun Dmitri I DI Hagedoorn Peter-Leon PL Bento Isabel I Hanefeld Ulf U
ACS catalysis 20200722 15
Retaining LeLoir glycosyltransferases catalyze the formation of glycosidic bonds between nucleotide sugar donors and carbohydrate acceptors. The anomeric selectivity of trehalose transferase from <i>Thermoproteus uzoniensis</i> 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-glycopyranos ...[more]
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