Extending the chemical space of enzymes through genetic code expansion

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Vernhes, Emeline | Bigot, Donna-Joe | Lemoine, Elsa | Cioci, Gianluca | Esque, Jérémy | Pradeau, Stéphanie | André, Isabelle | Montanier, Cédric | Fort, Sébastien | Nouaille, Sébastien | Fauré, Régis

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International audience. The incorporation into proteins of non-canonical amino acids is a powerful way tosurmount the limited chemical diversity of natural amino acids.1 Advantageously, thisapproach provides a means to explore chemical space, create new catalytic functionsand biorthogonal conjugates. Despite this promise, the success of this approach ishampered by highly variable and often low amino acid incorporation efficiency. In thiswork we describe methodological improvements that enhance the incorporation of non-canonical amino acids and discuss prospects for creation of artificial enzymesdisplaying designed metal ion-binding sites, or targeted sites for further post-translational glycosylation and labelling.[1] Shandell M. A.; Tan Z.; Cornish V. W. Biochemistry 2021 60(46), 3455-3469.

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