Molecular characterization of glucokinase from Escherichia coli K-12.

@article{Meyer1997MolecularCO,
  title={Molecular characterization of glucokinase from Escherichia coli K-12.},
  author={Dominique Meyer and Christian Schneider-Fresenius and Reinhold Horlacher and Ralf Peist and Winfried Boos},
  journal={Journal of bacteriology},
  year={1997},
  volume={179 4},
  pages={1298-306}
}
glk, the structural gene for glucokinase of Escherichia coli, was cloned and sequenced. Overexpression of glk resulted in the synthesis of a cytoplasmic protein with a molecular weight of 35,000. The enzyme was purified, and its kinetic parameters were determined. Its Km values for glucose and ATP were 0.78 and 3.76 mM, respectively. Its Vmax was 158 U/mg of protein. A chromosomal glk-lacZ fusion was constructed and used to monitor glk expression. Under all conditions tested, only growth on… CONTINUE READING

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The maltose system of Escherichia coli, p. 201–229

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