Explore the words cloud of the MDRZYMES project. It provides you a very rough idea of what is the project "MDRZYMES" about.
The following table provides information about the project.
Coordinator |
RIJKSUNIVERSITEIT GRONINGEN
Organization address contact info |
Coordinator Country | Netherlands [NL] |
Total cost | 165˙598 € |
EC max contribution | 165˙598 € (100%) |
Programme |
1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility) |
Code Call | H2020-MSCA-IF-2016 |
Funding Scheme | MSCA-IF-EF-ST |
Starting year | 2017 |
Duration (year-month-day) | from 2017-03-01 to 2019-02-28 |
Take a look of project's partnership.
# | ||||
---|---|---|---|---|
1 | RIJKSUNIVERSITEIT GRONINGEN | NL (GRONINGEN) | coordinator | 165˙598.00 |
Enzymes are remarkable catalysts. The unmatched rate accelerations and exacting selectivities that these protein molecules achieve have whetted the appetite of chemists to harness the prowess of enzyme catalysis for industrial applications. However, natural enzymes can only catalyze a small fraction of the reactions routinely employed by synthetic chemists. As a result, creating designer biocatalysts with the ability to efficiently catalyze transformations not found in nature’s repertoire is a long-standing goal in chemical biology. To meet this challenge, this proposal describes our plans to generate proficient enzymes for palladium-catalyzed cross-coupling reactions. Specifically, we will create hybrid catalysts by recruiting active palladium complexes to the promiscuous binding sites of multidrug resistance gene regulators. We will validate productive assemblies by a rigorous biophysical characterization and evaluate the resulting artificial metalloenzymes for their ability to catalyze model Suzuki-Miyaura cross-coupling reactions. To refine the activities and selectivities of these primitive catalysts we will explore directed evolution protocols to identify mutations in the protein scaffolds that are beneficial for catalysis. In one strategy, we will establish a fluorescence-based screening approach that allows for testing libraries of hybrid catalysts in multi-well format. Another strategy will evaluate the possibility of performing cross-coupling reaction in vivo. Toward this end, artificial metalloenzymes will be assembled in the periplasm and utilized for the synthesis of a non-standard amino acid, which subsequently can be incorporated into a selection marker. As a result, bacteria producing improved variants will outgrow those with less efficient catalysts under selection conditions. Overall, our efforts will generate proficient designer enzymes that could prove valuable for applications in sustainable chemical processes.
year | authors and title | journal | last update |
---|---|---|---|
2018 |
Ivana Drienovská, Clemens Mayer, Christopher Dulson, Gerard Roelfes A designer enzyme for hydrazone and oxime formation featuring an unnatural catalytic aniline residue published pages: 946-952, ISSN: 1755-4330, DOI: 10.1038/s41557-018-0082-z |
Nature Chemistry 10/9 | 2019-06-11 |
Are you the coordinator (or a participant) of this project? Plaese send me more information about the "MDRZYMES" project.
For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.
Send me an email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.
Thanks. And then put a link of this page into your project's website.
The information about "MDRZYMES" are provided by the European Opendata Portal: CORDIS opendata.