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Ancestral SIGNED

Structural and biochemical studies of an ancestral enzyme with dual dehalogenase and luciferase activity

Total Cost €

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EC-Contrib. €

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Partnership

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 Ancestral project word cloud

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

spectrometry    haloalkane    history    simulations    carbon    lab    insights    dual    marine    hydrolases    prior    display    light    pave    mass    time    basis    software    remarkable    switchable    compounds    underlying    dioxide    gained    interesting    photo    reniformis    resolved    individual    invertebrate    promiscuous    cleavage    employed    complementary    complexes    similarity    dynamics    contributions    alpha    amino    biocatalytic    subjects    molecular    independent    rational    monooxygenase    site    existed    directed    rluc    halogen    catalyse    proof    emission    unobserved    industrial    substrate    coelenteramide    evolution    hld    dehalogenases    crystallography    coelenterazine    day    bond    probe    divergence    engineering    enzyme    followed    modern    beta    blue    uses    functional    catalytically    workings    acid    12    homologues    reaction    luciferase    techniques    hlds    generation    residues    biotechnology    biocatalysts    exhibits    tools    dissect    renilla    13    analogues    converts    inner    ray    data    biomedicine    mutagenesis    dehalogenase    ec    evolutionary    organization    structural    strikingly    function    reconstruction    mechanisms    biochemical    unusual    organohalogen    driving    feasibility    extend    poorly    ancestral    unlike    cofactor    reflects    sequence    explore    resurrected   

Project "Ancestral" data sheet

The following table provides information about the project.

Coordinator
Masarykova univerzita 

Organization address
address: Zerotinovo namesti 9
city: BRNO STRED
postcode: 60177
website: http://www.muni.cz

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 Czech Republic [CZ]
 Total cost 142˙720 €
 EC max contribution 142˙720 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2017
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2018
 Duration (year-month-day) from 2018-06-01   to  2020-05-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    Masarykova univerzita CZ (BRNO STRED) coordinator 142˙720.00

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 Project objective

Haloalkane dehalogenases (HLDs) catalyse the cleavage of the carbon-halogen bond of industrial organohalogen compounds and are interesting subjects to study molecular evolution. Strikingly, HLDs display remarkable sequence and structural similarity with luciferase from the marine invertebrate Renilla reniformis (RLuc), which reflects their common evolutionary history. Unlike HLDs, which are α/β hydrolases (EC 3.8.1.5), the RLuc luciferase is cofactor-independent monooxygenase (EC 1.13.12.5) that converts coelenterazine into coelenteramide and carbon dioxide, followed by an emission of blue light. Yet, the evolutionary steps driving their functional divergence remain poorly understood. Our proof-of-concept data show the feasibility of the reconstruction of an ancestral enzyme, which existed prior to the functional divergence of the modern-day HLD and RLuc homologues, and that this in-lab resurrected enzyme exhibits so-far unobserved dual dehalogenase/luciferase activity. This project aims to dissect structural and biochemical basis of this unusual biocatalytic behaviour of the ancestral enzyme. Specifically, X-ray crystallography, including time-resolved studies with photo-switchable substrate analogues, and advanced mass spectrometry techniques will be employed to probe enzyme-substrate complexes in order to get molecular insights into the inner organization and workings of the catalytically promiscuous enzyme. Complementary site-directed mutagenesis and molecular dynamics simulations will explore the contributions of individual amino acid residues to the dual-function activity. The gained knowledge will extend our in-depth understanding of the evolution of underlying biocatalytic reaction mechanisms. Furthermore, it will pave the way for the development of novel software tools for the rational engineering of next-generation biocatalysts for specific uses in biotechnology and biomedicine.

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