Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling.

@article{Cheng2000MolecularCO,
  title={Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling.},
  author={Qiaomei Cheng and Hongchuan Li and Keith D. Merdek and James T. Park},
  journal={Journal of bacteriology},
  year={2000},
  volume={182 17},
  pages={4836-40}
}
The beta-N-acetylglucosaminidase of Escherichia coli was found to have a novel specificity and to be encoded by a gene (nagZ) that maps at 25.1 min. It corresponds to an open reading frame, ycfO, whose predicted amino acid sequence is 57% identical to that of Vibrio furnissii ExoII. NagZ hydrolyzes the beta-1,4 glycosidic bond between N-acetylglucosamine and anhydro-N-acetylmuramic acid in cell wall degradation products following their importation into the cell during the process for recycling… CONTINUE READING
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