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Enzyme design and engineering by implementation of non-canonical amino acids in protein scaffolds

Total Cost €


EC-Contrib. €






 THIAZOLIUMenzyme project word cloud

Explore the words cloud of the THIAZOLIUMenzyme project. It provides you a very rough idea of what is the project "THIAZOLIUMenzyme" about.

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Project "THIAZOLIUMenzyme" data sheet

The following table provides information about the project.


Organization address
address: Raemistrasse 101
postcode: 8092

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Switzerland [CH]
 Total cost 191˙149 €
 EC max contribution 191˙149 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2018
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2019
 Duration (year-month-day) from 2019-09-15   to  2021-09-14


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 Project objective

The design of enzymatic catalysts and protein therapeutics with tailored, new-to-nature properties is a long-standing goal in enzymology and cell biology. Nature generally uses 20 amino acids as building blocks for protein synthesis. However, this portfolio limits the options for engineering proteins with ‘un-natural’ activities. Recent developments in the expansion of the genetic code have the potential to revolutionise the design of novel enzymes; by reprogramming the genetic code, we could convey novel functionality into proteins and extend their properties. This project aims at incorporating thiazolium amino acids into the active site of a promiscuous and highly evolvable de novo enzyme, namely the RA95 (retro)-aldolase, for orchestrating organocatalytic transformations of clinical and industrial interest. Such reactions, conventionally mediated by non-enzymatic, small molecule N-heterocyclic carbene (NHC) catalysts require high temperature and catalyst loading. An engineered enzyme with the ability to catalyse such chemistry may overcome the drawbacks of these abiological catalysts, serving as a ‘greener’ biocatalytic alternative, and also perform the desired reactions in cells for medicinal purposes. This initiative will pave the way for development of general strategies for creating enzymes with unique properties and provide a tool-box for efficient, environmentally-friendly and bioorthogonal organocatalysed reactions. It is anticipated that the generated artificial biocatalysts will have attractive applications in research, medicine and industry.

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