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Hydrolysis of Glycosyl Thioimidates by Glycoside Hydrolase Requires Remote Activation for Efficient Activity
Catalysts (2019)
  • Alexei Demchenko, University of Missouri-St. Louis
  • Laure Guillotin
  • Zeinab Assaf
  • Salvatore G. Pistorio, University of Missouri–St. Louis
  • Pierre Lafite
  • Richard Daniellou
Chemoenzymatic synthesis of glycosides relies on efficient glycosyl donor substrates able to react rapidly and efficiently, yet with increased stability towards chemical or enzymatic hydrolysis. In this context, glycosyl thioimidates have previously been used as efficient donors, in the case of hydrolysis or thioglycoligation. In both cases, the release of the thioimidoyl aglycone was remotely activated through a protonation driven by a carboxylic residue in the active site of the corresponding enzymes. A recombinant glucosidase (DtGly) from Dictyoglomus themophilum, previously used in biocatalysis, was also able to use such glycosyl thioimidates as substrates. Yet, enzymatic kinetic values analysis, coupled to mutagenesis and in silico modelling of DtGly/substrate complexes demonstrated that the release of the thioimidoyl moiety during catalysis is only driven by its leaving group ability, without the activation of a remote protonation. In the search of efficient glycosyl donors, glycosyl thioimidates are attractive and efficient. Their utility, however, is limited to enzymes able to promote leaving group release by remote activation.
  • glycoside hydrolase; thioglycosides; biocatalysis
Publication Date
October 1, 2019
Citation Information
Alexei Demchenko, Laure Guillotin, Zeinab Assaf, Salvatore G. Pistorio, et al.. "Hydrolysis of Glycosyl Thioimidates by Glycoside Hydrolase Requires Remote Activation for Efficient Activity" Catalysts Vol. 9 Iss. 10 (2019)
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This work is licensed under a Creative Commons CC_BY International License.