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

Christopher P. Long, Jennifer Au, Nicholas R. Sandoval, Nikodimos A. Gebreselassie and Maciek R. Antoniewicz ()
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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
Nikodimos A. Gebreselassie: Metabolic Engineering and Systems Biology Laboratory, University of Delaware
Maciek R. Antoniewicz: Metabolic Engineering and Systems Biology Laboratory, University of Delaware

Nature Communications, 2017, vol. 8, issue 1, 1-8

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms14316

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