Extending the chemical space of CAZymes: how and why?

<none>

Programme Social programme Plenary speakers Keynote speakers 1st EuroCarb Young Researcher (ECYR) Workshop CarboMet Workshop Mini symposium: Glycobiology at the LUMC and beyond Favourites/Agenda

Social programme

Plenary speakers

Keynote speakers

1st EuroCarb Young Researcher (ECYR) Workshop

CarboMet Workshop

Mini symposium: Glycobiology at the LUMC and beyond

Favourites/Agenda

Photos

Venue & Travel Venue Accommodation City of Leiden Travel directions

Venue

Accommodation

City of Leiden

Travel directions

Committees

Home

Extending the chemical space of CAZymes: how and why?

Régis Fauré 1 , Nuria Ramos 1 , Donna-Joe Bigot 1 , Virginie Ramillon-Delvolve 1 , iGEM Toulouse INSA-UPS team 1,2 , Cédric Montanier 1 , Gilles Truan 1 , Sébastien Nouaille 1

1 LISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France, 2 LBME, CBI, Université de Toulouse, CNRS, UPS, Toulouse, France

Standard protein engineering usually involves the substitution of one or more amino acids by other amino acids chosen from the remaining nineteen common alternatives. While this approach has a proven track record, it is nevertheless extremely limited by the chemical space offered by the 20 canonical amino acids.

Over the last 25 years, techniques have been developed to site specifically introduce non-canonical amino acids (ncAA) into proteins, while using the existing genetic code [1,2]. Advantageously, these approaches provide a means to explore chemical space, create new catalytic opportunities 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, we are studying the production of nCAA-bearing glycoside hydrolases and carbohydrate-binding modules [3]. In this presentation, we will describe current progress towards this goal, focussing both on the methodological aspects and on prospects for the future creation of artificial enzymes displaying new functions or architectures.

This research was supported by the pre-competitive program of Toulouse White Biotechnology (TWB), the Institut National de la Recherche Agronomique (INRA) and the 3BCAR Carnot Institute, through the project INSEREE (2015-2018), the ANS CHIMZYM (2016 & 2017) and the project i-INSEREE (2018-2019) respectively. The iGEM Toulouse INSA-UPS team 2018 (http://2018.igem.org/Team:Toulouse-INSA-UPS) is composed of G. Bordes, A. Pelus, Y. Bouchiba, C. Burnard, J. Delhomme, J. Pérochon, M. Toanen, A. Verdier, C. Wagner, S. Barbe, B. Enjalbert, J. Esque, M.-P. Escudié, R. Fauré, M. Guionnet, A. Henras, S. Heux, P. Millard, C. Montanier, and Y. Romeo.

Noren C.J.; Anthony-Cahill S.J.; Griffith M.C.; Schultz P.G. Science 1989, 244, 182-188.

Liu C.C.; Schultz P.G. Ann. Rev. Biochem. 2010, 79, 413-444.

Ramos N.; Bigot D.-J.; Ramillon-Devolve V.; Hebra T.; Montanier C.; Truan G.; Fauré R.; Nouaille S. In preparation

Contact eurocarb@eurocarb2019.com for general questions about EUROCARB2019, or codee@eurocarb2019.com for scientific questions.

Leiden University / Leiden Institute of Chemistry lic.leidenuniv.nl

European Carbohydrate Organisation

Congress by Design www.congressbydesign.com