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Rational enzyme design without structural knowledge: a sequence-based approach for efficient generation of transglycosylases

Abstract : Glycobiology is dogged by the relative scarcity of synthetic, defined oligosaccharides. Enzyme-catalysed glycosylation using glycoside hydrolases is feasible but is hampered by the innate hydrolytic activity of these enzymes. Protein engineering is useful to remedy this, but it usually requires prior structural knowledge of the target enzyme, and/or relies on extensive, time-consuming screening and analysis. Here we describe a straightforward strategy that involves rational rapid in silico analysis of protein sequences. The method pinpoints 6‒12 single mutant candidates to improve transglycosylation yields. Requiring very little prior knowledge of the target enzyme other than its sequence, the method is generic and procures catalysts for the formation of glycosidic bonds involving various D/L-, α/β-pyranosides or furanosides, and exo- and endoaction. Moreover, mutations validated in one enzyme can be transposed to others, even distantly related enzymes.
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https://hal.inrae.fr/hal-02906907
Contributor : Insa Toulouse Scd <>
Submitted on : Friday, June 25, 2021 - 11:08:16 AM
Last modification on : Tuesday, September 21, 2021 - 4:06:13 PM

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David Teze, Jiao Zhao, Mathias Wiemann, Kazi Zubaida Gulshan Ara, Rossana Lupo, et al.. Rational enzyme design without structural knowledge: a sequence-based approach for efficient generation of transglycosylases. Chemistry - A European Journal, Wiley-VCH Verlag, In press, ⟨10.1002/chem.202100110⟩. ⟨hal-02906907v2⟩

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