Enzyme I facilitates reverse flux from pyruvate to phosphoenolpyruvate in Escherichia coli
Author(s) | Long, Christopher P | |
Author(s) | Au, Jennifer | |
Author(s) | Sandoval, Nicholas R | |
Author(s) | Gebreselassie, Nikodimos A | |
Author(s) | Antoniewicz, Maciek R | |
Ordered Author | Christopher P. Long | en_US |
Ordered Author | Jennifer Au | en_US |
Ordered Author | Nicholas R. Sandoval | en_US |
Ordered Author | Nikodimos A. Gebreselassie | en_US |
Ordered Author | Maciek R. Antoniewicz | en_US |
UD Author | Antoniewicz, Maciej Robert | en_US |
Date Accessioned | 2017-03-09T01:52:43Z | |
Date Available | 2017-03-09T01:52:43Z | |
Copyright Date | The Author(s) 2017 | en_US |
Publication Date | 2017-01-27 | |
Description | Publisher's PDF | en_US |
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. | en_US |
Department | University of Delaware, Department of Chemical and Biomolecular Engineering | en_US |
Citation | : Long, C. P. et al. Enzyme I facilitates reverse flux from pyruvate to phosphoenolpyruvate in Escherichia coli. Nat. Commun. 8, 14316 doi: 10.1038/ncomms14316 (2017) | en_US |
DOI | 10.1038/ncomms14316 | en_US |
ISSN | 2041-1723 | en_US |
URL | http://udspace.udel.edu/handle/19716/21126 | |
Language | English | en_US |
Publisher | Nature Publishing Group | en_US |
dc.rights | CC BY 4.0 | en_US |
dc.source | Nature Communications | en_US |
dc.source.uri | http://www.nature.com/ncomms/ | en_US |
Title | Enzyme I facilitates reverse flux from pyruvate to phosphoenolpyruvate in Escherichia coli | en_US |
Type | Article | en_US |