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Open AccessArticle

Hydrolysis of Glycosyl Thioimidates by Glycoside Hydrolase Requires Remote Activation for Efficient Activity

1
Institut de Chimie Organique et Analytique, ICOA, Université d’Orléans, CNRS, UMR 7311, BP6759 Rue de Chartres, F-45067 Orléans CEDEX 2, France
2
Department of Chemistry and Biochemistry, University of Missouri-St. Louis, One University Boulevard, St. Louis, MO 63121, USA
*
Author to whom correspondence should be addressed.
Catalysts 2019, 9(10), 826; https://doi.org/10.3390/catal9100826
Received: 18 September 2019 / Revised: 27 September 2019 / Accepted: 30 September 2019 / Published: 1 October 2019
(This article belongs to the Special Issue Novel Enzyme and Whole-Cell Biocatalysts)
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. View Full-Text
Keywords: glycoside hydrolase; thioglycosides; biocatalysis glycoside hydrolase; thioglycosides; biocatalysis
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MDPI and ACS Style

Guillotin, L.; Assaf, Z.; Pistorio, S.G.; Lafite, P.; Demchenko, A.V.; Daniellou, R. Hydrolysis of Glycosyl Thioimidates by Glycoside Hydrolase Requires Remote Activation for Efficient Activity. Catalysts 2019, 9, 826.

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