Posttranslational conversion of L-serines to D-alanines is vital for optimal production and activity of the lantibiotic lacticin 3147.

@article{Cotter2005PosttranslationalCO,
  title={Posttranslational conversion of L-serines to D-alanines is vital for optimal production and activity of the lantibiotic lacticin 3147.},
  author={Paul D Cotter and Paula M O'connor and Lorraine A. Draper and Elaine M. Lawton and Lucy H. Deegan and C. Ray Hill and R Paul Ross},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 51},
  pages={18584-9}
}
As a general rule, ribosomally synthesized polypeptides contain amino acids only in the L-isoform in an order dictated by the coding DNA/RNA. Two of a total of only four examples of L to D conversions in prokaryotic systems occur in posttranslationally modified antimicrobial peptides called lantibiotics. In both examples (lactocin S and lacticin 3147), ribosomally encoded L-serines are enzymatically converted to D-alanines, giving rise to an apparent mistranslation of serine codons to alanine… CONTINUE READING

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