Non-ribosomal peptide synthetases (NRPSs) are a large family of modular multienzymes that catalyse the biosynthesis of many commercially important microbial natural products. Adenylation (A) domains within each NRPS module selectively bind and activate (by reaction with ATP) the amino acids constituting the peptide. Structure based models of A-domains have recently been developed, which identify potentially important residues for amino acid recognition and facilitate the prediction of new peptide natural pr oduct structures from genome sequence data. The accuracy of these structural predictions and the role played by putative recognition residues will be investigated using the Streptomyces coelicolor A3(2) coelichelin synthetase as a model.
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