From β-glucanase to β-glucansynthase: Glycosyl transfer to α-glycosyl fluorides catalyzed by a mutant endoglucanase lacking its catalytic nucleophile

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Abstract

Removal of the catalytic nucleophile Glu134 of the retaining 1,3-1,4-β-glucanase from Bacillus licheniformis by mutation to alanine yields an enzyme with no glycosidase activity. The mutant is able to catalyze the regio- and stereospecific glycosylation of α-laminaribiosyl fluoride with different glucoside acceptors through a single-step inverting mechanism. The main advantage of the mutant as glycosylation catalyst with respect to the kinetically controlled transglycosylation using the wild-type enzyme is that the reaction products cannot be hydrolyzed by the mutant enzyme, and glycosylation yields rise to 90%. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)208-212
Number of pages5
JournalFEBS Letters
Volume440
Issue number1-2
DOIs
Publication statusPublished - 27 Nov 1998

Keywords

  • Enzymatic glycosylation
  • Glycosyl fluoride
  • Glycosynthase
  • Nucleophile residue
  • β-Glucanase

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