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MDRZYMES

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

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 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.

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

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

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