Structure of microcin C51, a new antibiotic with a broad spectrum of activity.

@article{Metlitskaya1995StructureOM,
  title={Structure of microcin C51, a new antibiotic with a broad spectrum of activity.},
  author={Anastasia Z. Metlitskaya and Genrikh S. Katrukha and Alexander S. Shashkov and Dmitry A. Zaitsev and Ts. A. Egorov and Inessa Khmel},
  journal={FEBS letters},
  year={1995},
  volume={357 3},
  pages={
          235-8
        }
}
The structure of microcin C51, a new antibiotic produced by E. coli, has been determined. This antibiotic was shown to be a 1.18 kDa nucleotide peptide. It consists of a heptapeptide with formylmethionine as the N-terminus and a C-terminal asparagine linked with nebularin-5'-monophosphate through the three-methylene bridge. The OH-group of threonine is substituted. The peptide chain of microcin C51 synthesized on ribosomes is the longest among the known biologically active nucleotide peptides. 
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