Skip to main content

Re-Evolution of a Non Ribosomal Protein Synthethase

Objective

Many peptide-based natural products of therapeutic importance are synthesised by nonribosomal peptide synthetases (NRPSs), large, multifunctional enzymes that operate as molecular assembly lines, by coupling and processing an extending chain of amino acid monomers. They are composed of numerous enzyme domains that carry out the steps of the bio-synthesis and provide an efficient route to natural products that are not easily accessible by synthetic chemistry. An efficient exploitation, however, still requires a much deeper understanding of the molecular basis of activity and specificity in NRPS enzymes. A set of approaches dealing with neutral drift, directed evolution and selective enzyme modification will be carried out on the model system TycA, taking advantage of knowledge and technologies available at the host institution as well as through a number of international collaborations and participation in the training programme of the FP7 network ENEFP (dealing with directed evolution of functional proteins).

Field of science

  • /natural sciences/chemical sciences/organic chemistry/amines
  • /natural sciences/biological sciences/biochemistry/biomolecules/proteins
  • /natural sciences/biological sciences/biochemistry/biomolecules/proteins/enzymes

Call for proposal

FP7-PEOPLE-IEF-2008
See other projects for this call

Funding Scheme

MC-IEF - Intra-European Fellowships (IEF)

Coordinator

THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE
Address
Trinity Lane The Old Schools
CB2 1TN Cambridge
United Kingdom
Activity type
Higher or Secondary Education Establishments
EU contribution
€ 171 867,63
Administrative Contact
Edna Murphy (Ms.)