NPTAILORINGENZYMES

Tailoring Enzymes for Natural Product Synthesis

 Coordinatore GOTTFRIED WILHELM LEIBNIZ UNIVERSITAET HANNOVER 

 Organization address address: Welfengarten 1
city: HANNOVER
postcode: 30167

contact info
Titolo: Ms.
Nome: Monika
Cognome: Griese
Email: send email
Telefono: +49 511 762 4612
Fax: +49 511 762 3011

 Nazionalità Coordinatore Germany [DE]
 Totale costo 100˙000 €
 EC contributo 100˙000 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-2011-CIG
 Funding Scheme MC-CIG
 Anno di inizio 2011
 Periodo (anno-mese-giorno) 2011-10-01   -   2015-09-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    GOTTFRIED WILHELM LEIBNIZ UNIVERSITAET HANNOVER

 Organization address address: Welfengarten 1
city: HANNOVER
postcode: 30167

contact info
Titolo: Ms.
Nome: Monika
Cognome: Griese
Email: send email
Telefono: +49 511 762 4612
Fax: +49 511 762 3011

DE (HANNOVER) coordinator 100˙000.00

Mappa


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biocatalysts    enzymes    parts    ambruticin    natural    jerangolid    syntheses    assays    total    biosynthetic    tailoring    pathways    studied    gain    steps    polyketide   

 Obiettivo del progetto (Objective)

'The aim of the project is to translate the knowledge from biosynthetic pathways of natural products into Organic Chemistry, achieved by developing novel chemoenzymatic total syntheses of the polyketide natural products ambruticin and jerangolid. In both biosynthetic pathways, large parts of the molecular complexity are set up by tailoring enzymes. These enzymes will be studied regarding their potential to act as biocatalysts that can substitute late and crucial steps in total syntheses. The project divides into two parts. At first, the biosynthesis of ambruticin and jerangolid will be studied with a focus on allocating particular steps to individual tailoring enzymes. These enzymes will be characterised in in vitro assays and these assays will be optimised in order to find out if the candidate enzymes can be applied as efficient biocatalysts. After this, total syntheses will be developed, which integrate these enzymatic steps. This approach promises to gain several advantages. The overall efficiency of the syntheses could be drastically improved and the access to derivatives could also be considerably facilitated. Furthermore, the project will gain substantial knowledge about tailoring processes of complex polyketide pathways.'

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