Fructose-1,6-bisphosphatase from Corynebacterium glutamicum: expression and deletion of the fbp gene and biochemical characterization of the enzyme

@article{Rittmann2003Fructose16bisphosphataseFC,
  title={Fructose-1,6-bisphosphatase from Corynebacterium glutamicum: expression and deletion of the fbp gene and biochemical characterization of the enzyme},
  author={Doris Rittmann and Steffen Schaffer and Volker F Wendisch and Hermann Sahm},
  journal={Archives of Microbiology},
  year={2003},
  volume={180},
  pages={285-292}
}
The class II fructose-1,6-bisphosphatase gene of Corynebacterium glutamicum, fbp, was cloned and expressed with a N-terminal His-tag in Escherichia coli. Purified, His-tagged fructose-1,6-bisphosphatase from C. glutamicum was shown to be tetrameric, with a molecular mass of about 140 kDa for the homotetramer. The enzyme displayed Michaelis-Menten kinetics for the substrate fructose 1,6-bisphosphate with a Km value of about 14 µM and a Vmax of about 5.4 µmol min−1 mg−1 and kcat of about 3.2 s−1… CONTINUE READING

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