Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum

@article{Becker2008MetabolicRT,
  title={Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum},
  author={Judith Becker and Corinna Klopprogge and Christoph Wittmann},
  journal={Microbial Cell Factories},
  year={2008},
  volume={7},
  pages={8 - 8}
}
BACKGROUND Pyruvate kinase is an important element in flux control of the intermediate metabolism. It catalyzes the irreversible conversion of phosphoenolpyruvate into pyruvate and is under allosteric control. In Corynebacterium glutamicum, this enzyme was regarded as promising target for improved production of lysine, one of the major amino acids in animal nutrition. In pyruvate kinase deficient strains the required equimolar ratio of the two lysine precursors oxaloacetate and pyruvate can be… CONTINUE READING

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