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.

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

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.)

EngPTC2 (2019)

Exploring new technologies for the next generation pulse tube cryocooler below 2K

Read More  

NSTree (2020)

Understanding substrate delivery for cell wall biosynthesis in plants

Read More  

ReproMech (2019)

The Molecular Mechanisms of Cell Fate Reprogramming in Vertebrate Eggs

Read More