The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling.

@article{Uehara2004TheNK,
  title={The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling.},
  author={Tsuyoshi Uehara and James T. Park},
  journal={Journal of bacteriology},
  year={2004},
  volume={186 21},
  pages={7273-9}
}
N-acetyl-D-glucosamine (GlcNAc) is a major component of bacterial cell wall murein and the lipopolysaccharide of the outer membrane. During growth, over 60% of the murein of the side wall is degraded, and the major products, GlcNAc-anhydro-N-acetylmuramyl peptides, are efficiently imported into the cytoplasm and cleaved to release GlcNAc, anhydro-N-acetylmuramic acid, murein tripeptide (L-Ala-D-Glu-meso-diaminopimelic acid), and D-alanine. Like murein tripeptide, GlcNAc is readily recycled, and… CONTINUE READING
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Identification of a dedicated recycling pathway for anhydro- N-acetylmuramic acid and N-acetylglucosamine derived from Escherichia coli cell wall murein

  • J. T. Park
  • J. Bacteriol
  • 2001
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