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

Christopher P. Long; Jennifer Au; Nicholas R. Sandoval; Nikodimos A. Gebreselassie; Maciek R. Antoniewicz

doi:10.1038/ncomms14316

Nature Communications (Jan 2017)

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

Christopher P. Long,
Jennifer Au,
Nicholas R. Sandoval,
Nikodimos A. Gebreselassie,
Maciek R. Antoniewicz

Affiliations

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

DOI: https://doi.org/10.1038/ncomms14316
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 8

Abstract

Read online

Enzyme I, a component of the phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS), converts phosphoenolpyruvate to pyruvate. Here, the authors show that Enzyme I facilitates also the reverse reaction during both gluconeogenic and glycolytic growth inE. coli.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal