Bioconjugate Chemistry · 2015 · 43 citations · 23 references
Life SciencesBiochemistryBiotechnologyBiocatalysisCarbohydrate ChemistryEnzymologyBiocatalytic GlycosylationGlycan-protein InteractionsGlycosidic Bond HydrolysisProtein GlycosylationCarbohydrate-active EnzymesGlycosidase InhibitionGlycosidase InhibitorsGlycosidase-mediated ActivationGlycosidasesMultivalent InhibitorsPhosphorylase ActivationSmall-molecule Activators
Multivalent iminosugars have recently emerged as powerful tools to inhibit the activities of specific glycosidases. In this work, biocompatible dextrans were coated with iminosugars to form linear and ramified polymers with unprecedently high valencies (from 20 to 900) to probe the evolution of the multivalent inhibition as a function of ligand valency. This study led to the discovery that polyvalent iminosugars can also significantly enhance, not only inhibit, the enzymatic activity of specific glycoside-hydrolase, as observed on two galactosidases, a fucosidase, and a bacterial mannoside phosphorylase for which an impressive 70-fold activation was even reached. The concept of glycosidase activation is largely unexplored, with a unique recent example of small-molecules activators of a bacterial O-GlcNAc hydrolase. The possibility of using these polymers as "artificial enzyme effectors" may therefore open up new perspectives in therapeutics and biocatalysis.
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Crystal Structure of Thermotoga maritima α-l-Fucosidase
Gerlind Sulzenbacher, Christophe Bignon, Takeshi Nishimura et al. · Journal of Biological Chemistry · 2004 · 166 citations · Full text
Human liver glycogen phosphorylase inhibitors bind at a new allosteric site
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