Comparison of the sequences of the nagE operons from Klebsiella pneumoniae and Escherichia colt K12: Enhanced variability of the enzyme IIN-acetylglucosamine in regions connecting functional domains

@article{Vogler2004ComparisonOT,
  title={Comparison of the sequences of the nagE operons from Klebsiella pneumoniae and Escherichia colt K12: Enhanced variability of the enzyme IIN-acetylglucosamine in regions connecting functional domains},
  author={A. Vogler and J. Lengeler},
  journal={Molecular and General Genetics MGG},
  year={2004},
  volume={230},
  pages={270-276}
}
SummaryThe nagE operon, encoding the enzyme II specific for N-acetylglucosamine (EIINag), and adjacent DNA from the chromosome of Klebsiella pneumoniae were sequenced and compared with the corresponding sequence from Escherichia colt K12. The deduced EIINag sequences differ in 72 out of 651 amino acids, the K. pneumoniae sequence being three residues longer. The amino acid differences were distributed unevenly, and were most frequent in regions connecting the three functional domains of the… Expand
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TLDR
Cloning and analysis of the gene nagE encoding Enzyme IINag (EIINag) from Klebsiella pneumoniae revealed strong similarities with the corresponding gene from Escherichia coli K12, indicating that truncated proteins lacking a C-terminal domain homologous to the soluble Enzyme III (crr gene) could be complemented by this molecule to nearly wild-type activity. Expand
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