Enzyme I facilitates reverse flux from pyruvate to phosphoenolpyruvate in Escherichia coli
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.
Saved in:
Main Authors: | Christopher P. Long, Jennifer Au, Nicholas R. Sandoval, Nikodimos A. Gebreselassie, Maciek R. Antoniewicz |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2017
|
Subjects: | |
Online Access: | https://doaj.org/article/6fd908c06d0a4f18ad7fd23a269a9807 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Identification of a High-Affinity Pyruvate Receptor in Escherichia coli
by: Stefan Behr, et al.
Published: (2017) -
Programmable biomolecular switches for rewiring flux in Escherichia coli
by: Cong Gao, et al.
Published: (2019) -
Extensive regulation of enzyme activity by phosphorylation in Escherichia coli
by: Evgeniya Schastnaya, et al.
Published: (2021) -
Imaging mitochondrial flux in single cells with a FRET sensor for pyruvate.
by: Alejandro San Martín, et al.
Published: (2014) -
Author Correction: Palmitate and pyruvate carbon flux in response to choline and methionine in bovine neonatal hepatocytes
by: T. L. Chandler, et al.
Published: (2021)