Opendata, web and dolomites

NetMoDEzyme SIGNED

Network models for the computational design of proficient enzymes

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 NetMoDEzyme project word cloud

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

reduce    biology    magnitude    predictions    mutations    economic    billions    netmodezyme    assays    technique    regions    industries    benefits    models    will    paradigm    withdrawn    blocker    characterizes    socio    principles    chemoinformatic    rules    residues    pure    routine    groundbreaking    chemical    natural    reactions    unviable    catalytic    costly    mimicking    synthesis    lag    easily    network    superb    beta    active    complexity    physical    conformational    treating    debated    cardiovascular    made    tremendous    power    completely    modern    accurately    confer    customizes    drugs    nature    strategy    advantages    directed    dynamics    enzymatic    elucidate    protocol    accelerating    reformulate    economically    movement    alteration    computational    efficiencies    counterparts    site    alternatives    correlated    genuinely    evolution    functionalities    guidelines    underlying    mutation    experimental    relies    environmentally    synthetically    catalysts    enzyme    enzymes    orders    extraordinary    proficient    enantiomerically    distal   

Project "NetMoDEzyme" data sheet

The following table provides information about the project.

Coordinator
UNIVERSITAT DE GIRONA 

Organization address
address: PLACA SANT DOMENEC 3
city: GIRONA
postcode: 17004
website: www.udg.es

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 Spain [ES]
 Project website https://silviaosuna.wordpress.com
 Total cost 1˙445˙587 €
 EC max contribution 1˙445˙587 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2015-STG
 Funding Scheme ERC-STG
 Starting year 2016
 Duration (year-month-day) from 2016-05-01   to  2021-04-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITAT DE GIRONA ES (GIRONA) coordinator 1˙445˙587.00

Map

 Project objective

Billions of years of evolution have made enzymes superb catalysts capable of accelerating reactions by several orders of magnitude. The underlying physical principles of their extraordinary catalytic power still remains highly debated, which makes the alteration of natural enzyme activities towards synthetically useful targets a tremendous challenge for modern chemical biology. The routine design of enzymes will, however, have large socio-economic benefits, as because of the enzymatic advantages the production costs of many drugs will be reduced and will allow industries to use environmentally friendly alternatives. The goal of this project is to make the routine design of proficient enzymes possible. Current computational and experimental approaches are able to confer natural enzymes new functionalities but are economically unviable and the catalytic efficiencies lag far behind their natural counterparts. The groundbreaking nature of NetMoDEzyme relies on the application of network models to reduce the complexity of the enzyme design paradigm and completely reformulate previous computational design approaches. The new protocol proposed accurately characterizes the enzyme conformational dynamics and customizes the included mutations by exploiting the correlated movement of the enzyme active site residues with distal regions. The guidelines for mutation are withdrawn from the costly directed evolution experimental technique, and the most proficient enzymes are easily identified via chemoinformatic models. The new strategy will be applied to develop proficient enzymes for the synthesis of enantiomerically pure β-blocker drugs for treating cardiovascular problems at a reduced cost. The experimental assays of our computational predictions will finally elucidate the potential of this genuinely new approach for mimicking Nature’s rules of evolution.

 Publications

year authors and title journal last update
List of publications.
2017 Miguel A. Maria-Solano, Adrian Romero-Rivera, Sílvia Osuna
Exploring the reversal of enantioselectivity on a zinc-dependent alcohol dehydrogenase
published pages: 4122-4129, ISSN: 1477-0520, DOI: 10.1039/c7ob00482f
Organic & Biomolecular Chemistry 15/19 2020-04-06
2017 Guangyue Li, Miguel A. Maria-Solano, Adrian Romero-Rivera, Sílvia Osuna, Manfred T. Reetz
Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution
published pages: 9454-9457, ISSN: 1359-7345, DOI: 10.1039/C7CC05377K
Chemical Communications 53/68 2020-04-06
2017 Eila Serrano-Hervás, Marc Garcia-Borràs, Sílvia Osuna
Exploring the origins of selectivity in soluble epoxide hydrolase from Bacillus megaterium
published pages: 8827-8835, ISSN: 1477-0520, DOI: 10.1039/C7OB01847A
Organic & Biomolecular Chemistry 15/41 2020-04-06
2017 Adrian Romero-Rivera, Marc Garcia-Borràs, Sílvia Osuna
Role of Conformational Dynamics in the Evolution of Retro-Aldolase Activity
published pages: 8524-8532, ISSN: 2155-5435, DOI: 10.1021/acscatal.7b02954
ACS Catalysis 7/12 2020-04-06
2019 Christian Curado-Carballada, Ferran Feixas, Javier Iglesias-Fernández, Sílvia Osuna
Hidden Conformations in Aspergillus niger Monoamine Oxidase are Key for Catalytic Efficiency
published pages: 3097-3101, ISSN: 1433-7851, DOI: 10.1002/anie.201812532
Angewandte Chemie International Edition 58/10 2020-04-06
2018 Miguel A. Maria-Solano, Eila Serrano-Hervás, Adrian Romero-Rivera, Javier Iglesias-Fernández, Sílvia Osuna
Role of conformational dynamics in the evolution of novel enzyme function
published pages: 6622-6634, ISSN: 1359-7345, DOI: 10.1039/c8cc02426j
Chemical Communications 54/50 2020-04-06
2018 Eila Serrano-Hervás, Guillem Casadevall, Marc Garcia-Borràs, Ferran Feixas, Sílvia Osuna
Epoxide Hydrolase Conformational Heterogeneity for the Resolution of Bulky Pharmacologically Relevant Epoxide Substrates
published pages: 12254-12258, ISSN: 0947-6539, DOI: 10.1002/chem.201801068
Chemistry - A European Journal 24/47 2020-04-06
2017 Adrian Romero-Rivera, Marc Garcia-Borràs, Sílvia Osuna
Computational tools for the evaluation of laboratory-engineered biocatalysts
published pages: 284-297, ISSN: 1359-7345, DOI: 10.1039/C6CC06055B
Chem. Commun. 53/2 2020-04-06
2018 Miguel A. Maria-Solano, Eila Serrano-Hervás, Adrian Romero-Rivera, Javier Iglesias-Fernández, Sílvia Osuna
Role of conformational dynamics in the evolution of novel enzyme function
published pages: 6622-6634, ISSN: 1359-7345, DOI: 10.1039/c8cc02426j
Chemical Communications 54/50 2020-04-06
2018 Eila Serrano-Hervás, Guillem Casadevall, Marc Garcia-Borràs, Ferran Feixas, Sílvia Osuna
Epoxide Hydrolase Conformational Heterogeneity for the Resolution of Bulky Pharmacologically Relevant Epoxide Substrates
published pages: 12254-12258, ISSN: 0947-6539, DOI: 10.1002/chem.201801068
Chemistry - A European Journal 24/47 2020-04-06

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "NETMODEZYME" 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 "NETMODEZYME" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.1.)

DISINTEGRATION (2019)

The Mass Politics of Disintegration

Read More  

SUExp (2018)

Strategic Uncertainty: An Experimental Investigation

Read More  

PROGRESS (2019)

The Enemy of the Good: Towards a Theory of Moral Progress

Read More