Influence of charge differences in the C-terminal part of nisin on antimicrobial activity and signaling capacity.

@article{Kraaij1997InfluenceOC,
  title={Influence of charge differences in the C-terminal part of nisin on antimicrobial activity and signaling capacity.},
  author={C van Kraaij and Eefjan Breukink and Harry S. Rollema and Roland J. Siezen and Rudy A. Demel and Ben de Kruijff and Oscar P. Kuipers},
  journal={European journal of biochemistry},
  year={1997},
  volume={247 1},
  pages={114-20}
}
Three mutants of the antibiotic nisin Z, in which the Val32 residue was replaced by a Glu, Lys or Trp residue, were produced and characterized for the purpose of establishing the role of charge differences in the C-terminal part of nisin on antimicrobial activity and signaling properties. 1H-NMR analyses showed that all three mutants harbor an unmodified serine residue at position 33, instead of the usual dehydroalanine. Apparently, the nature of the residue preceding the serine to be… CONTINUE READING

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