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Enzyme I facilitates reverse flux from pyruvate to phosphoenolpyruvate in Escherichia coli

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  • Christopher P. Long

    (Metabolic Engineering and Systems Biology Laboratory, University of Delaware)

  • Jennifer Au

    (Metabolic Engineering and Systems Biology Laboratory, University of Delaware)

  • Nicholas R. Sandoval

    (Metabolic Engineering and Systems Biology Laboratory, University of Delaware
    Present address: Department of Chemical and Biomolecular Engineering, Tulane University, New Orleans, LA 70188, USA)

  • Nikodimos A. Gebreselassie

    (Metabolic Engineering and Systems Biology Laboratory, University of Delaware)

  • Maciek R. Antoniewicz

    (Metabolic Engineering and Systems Biology Laboratory, University of Delaware)

Abstract

The bacterial phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) consists of cascading phosphotransferases that couple the simultaneous import and phosphorylation of a variety of sugars to the glycolytic conversion of phosphoenolpyruvate (PEP) to pyruvate. As the primary route of glucose uptake in E. coli, the PTS plays a key role in regulating central carbon metabolism and carbon catabolite repression, and is a frequent target of metabolic engineering interventions. Here we show that Enzyme I, the terminal phosphotransferase responsible for the conversion of PEP to pyruvate, is responsible for a significant in vivo flux in the reverse direction (pyruvate to PEP) during both gluconeogenic and glycolytic growth. We use 13C alanine tracers to quantify this back-flux in single and double knockouts of genes relating to PEP synthetase and PTS components. Our findings are relevant to metabolic engineering design and add to our understanding of gene-reaction connectivity in E. coli.

Suggested Citation

  • Christopher P. Long & Jennifer Au & Nicholas R. Sandoval & Nikodimos A. Gebreselassie & Maciek R. Antoniewicz, 2017. "Enzyme I facilitates reverse flux from pyruvate to phosphoenolpyruvate in Escherichia coli," Nature Communications, Nature, vol. 8(1), pages 1-8, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14316
    DOI: 10.1038/ncomms14316
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