N-acylation during glidobactin biosynthesis by the tridomain nonribosomal peptide synthetase module GlbF.

@article{Imker2010NacylationDG,
  title={N-acylation during glidobactin biosynthesis by the tridomain nonribosomal peptide synthetase module GlbF.},
  author={Heidi J Imker and Daniel Krahn and J{\'e}r{\^o}me Clerc and Markus Kaiser and Christopher T Walsh},
  journal={Chemistry & biology},
  year={2010},
  volume={17 10},
  pages={1077-83}
}
Glidobactins are hybrid NRPS-PKS natural products that function as irreversible proteasome inhibitors. A variety of medium chain 2(E),4(E)-diene fatty acids N-acylate the peptidolactam core and contribute significantly to the potency of proteasome inhibition. We have expressed the initiation NRPS module GlbF (C-A-T) in Escherichia coli and observe soluble active protein only on coexpression with the 8 kDa MbtH-like protein, GlbE. Following adenylation and installation of Thr as a T-domain… CONTINUE READING

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