9 research outputs found
Analysis of MMP2-1306C/T and TIMP2G-418C polymorphisms with relapsing remitting multiple sclerosis
Effect of Clonidine Early in Life on Brain Morphofunctional Deficits Induced by Neonatal Malnutrition in the Rat
Early Malnutrition and Changes in the Induced Release of Noradrenaline in the Prefrontal Cortex of Adult Rats
Rational enzyme design without structural knowledge: a sequence-based approach for efficient generation of transglycosylases
International audienceGlycobiology 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