Opendata, web and dolomites

MDRZYMES

Multidrug resistance gene regulators as scaffolds for the design and evolution of artificial metalloenzymes

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 MDRZYMES project word cloud

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

outgrow    fraction    assemblies    vivo    biophysical    synthetic    synthesis    accelerations    biocatalysts    meet    acid    ing    enzymes    proficient    rate    promiscuous    recruiting    mutations    appetite    refine    efforts    assembled    designer    format    libraries    beneficial    prowess    multidrug    incorporated    directed    fluorescence    standard    remarkable    possibility    suzuki    primitive    found    routinely    sites    whetted    strategy    chemists    palladium    protocols    valuable    reaction    repertoire    cross    variants    model    reactions    coupling    unmatched    enzyme    artificial    catalyze    biology    describes    active    molecules    evolution    gene    chemical    periplasm    generate    scaffolds    sustainable    resistance    catalysis    industrial    transformations    catalyzed    subsequently    metalloenzymes    small    producing    amino    bacteria    natural    performing    regulators    productive    screening    selectivities    employed    explore    prove    efficient    miyaura    complexes    validate    binding    nature    toward    hybrid    utilized    rigorous    catalysts    plans    marker    protein    create    characterization    exacting    harness   

Project "MDRZYMES" data sheet

The following table provides information about the project.

Coordinator
RIJKSUNIVERSITEIT GRONINGEN 

Organization address
address: Broerstraat 5
city: GRONINGEN
postcode: 9712CP
website: www.rug.nl

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 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

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    RIJKSUNIVERSITEIT GRONINGEN NL (GRONINGEN) coordinator 165˙598.00

Map

 Project objective

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.

 Publications

year authors and title journal last update
List of publications.
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.

More projects from the same programme (H2020-EU.1.3.2.)

ReproMech (2019)

The Molecular Mechanisms of Cell Fate Reprogramming in Vertebrate Eggs

Read More  

PHOTOCARBOX (2020)

Increasing the scope of CO2-utilising photoreactions: asymmetric photosynthesis of amino acids

Read More  

BB-SLM (2020)

Polychromatic digital optics for structured light

Read More