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).
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