Expanding the catalytic potential of CAZymes using non-canonical amino Acids

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Fauré, Régis | Ramos, Nuria | Bigot, Donna-Joe | Ramillon-Delvolve, Virginie | Montanier, Cédric | Truan, Gilles | Nouaille, Sébastien

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International audience. Standard protein engineering usually involves the substitution of one or more amino acids byother amino acids chosen from the remaining nineteen common alternatives. While this ap-proach has a proven track record, it is nevertheless extremely limited by the chemical spaceoffered by the 20 canonical amino acids.Over the last 30 years, techniques have been developed to site specifically introduce non-canonical amino acids (ncAA) into proteins, while using the existing genetic code [1,2]. Ad-vantageously, these approaches provide a means to explore chemical space, create new catalyticopportunities and perform bioorthogonal conjugate reactions or assemblies.Despite the increasing use of ncAA, this approach has rarely been used to engineer carbohydrate-active enzymes (CAZymes). In work aimed at extending the chemical space of CAZymes, andthus their catalytic potential, we are studying the production of nCAA-bearing glycoside hy-drolases and carbohydrate-binding modules [3]. In this presentation, we will describe currentprogress towards this goal, focusing both on the methodological aspects and on prospects forthe future creation of artificial enzymes displaying new functions or architectures.

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