Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.

@article{Hirel1989ExtentON,
  title={Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.},
  author={Philippe Herve Hirel and M. Schmitter and Philippe Dessen and Guy Fayat and Sylvain Blanquet},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1989},
  volume={86 21},
  pages={
          8247-51
        }
}
  • P. Hirel, M. Schmitter, +2 authors S. Blanquet
  • Published 1989
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
In a significant fraction of the Escherichia coli cytosolic proteins, the N-terminal methionine residue incorporated during the translation initiation step is excised. The N-terminal methionine excision is catalyzed by methionyl-aminopeptidase (MAP). Previous studies have suggested that the action of this enzyme could depend mainly on the nature of the second amino acid residue in the polypeptide chain. In this study, to achieve a systematic analysis of the specificity of MAP action, each of… Expand
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