Reprogramming nonribosomal peptide synthetases for "clickable" amino acids.

@article{Kries2014ReprogrammingNP,
  title={Reprogramming nonribosomal peptide synthetases for "clickable" amino acids.},
  author={Hajo Kries and Rudolf Wachtel and Anja Pabst and Benedikt Wanner and David L Niquille and Donald Hilvert},
  journal={Angewandte Chemie},
  year={2014},
  volume={53 38},
  pages={10105-8}
}
Nonribosomal peptide synthetases (NRPSs) are multifunctional enzymes that produce a wide array of bioactive peptides. Here we show that a single tryptophan-to-serine mutation in phenylalanine-specific NRPS adenylation domains enables the efficient activation of non-natural aromatic amino acids functionalized with azide and alkyne groups. The resulting 10(5)-fold switch in substrate specificity was achieved without appreciable loss of catalytic efficiency. Moreover, the effective communication… CONTINUE READING
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