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ENZYME MECHANISMS

The substrate lends a hand

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Duramycin is a small post-translationally modified peptide with antibody-like affinity for phosphatidylethanolamine. As it turns out, the same functionality that is essential for duramycin activity helps to catalyze the formation of its conformationally constrained and compact polycyclic architecture.

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Fig. 1: Structure and mechanism of DurN-catalyzed lysinoalanine formation.

References

  1. Arnison, P. G. et al. Nat. Prod. Rep. 30, 108–160 (2013).

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  2. An, L. et al. Nat. Chem. Biol. https://doi.org/10.1038/s41589-018-0122-4 (2018).

  3. Makino, A. et al. J. Biol. Chem. 278, 3204–3209 (2003).

    Article  CAS  PubMed  Google Scholar 

  4. Hosoda, K. et al. J. Biochem. 119, 226–230 (1996).

    Article  CAS  PubMed  Google Scholar 

  5. Ökesli, A., Cooper, L. E., Fogle, E. J. & van der Donk, W. A. J. Am. Chem. Soc. 133, 13753–13760 (2011).

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  6. Dall’Acqua, W. & Carter, P. Protein Sci. 9, 1–9 (2000).

    Article  PubMed Central  PubMed  Google Scholar 

  7. Carter, P. & Wells, J. A. Science 237, 394–399 (1987).

    Article  CAS  PubMed  Google Scholar 

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Authors and Affiliations

  1. Division of Chemical Biology and Medicinal Chemistry, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA

    Albert A. Bowers

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  1. Albert A. Bowers
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Correspondence to Albert A. Bowers.

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The author declares no competing interests.

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Bowers, A.A. The substrate lends a hand. Nat Chem Biol 14, 907–908 (2018). https://doi.org/10.1038/s41589-018-0135-z

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  • DOI: https://doi.org/10.1038/s41589-018-0135-z

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