Document Type
Article
Publication Date
8-2014
Publication Title
PLOS One
Volume
9
Issue
8
Pages
1-8
Publisher Name
PLOS
Abstract
Fructose-1,6-bisphosphate activates ADP-glucose pyrophosphorylase and the synthesis of glycogen in Escherichia coli. Here, we show that although pyruvate is a weak activator by itself, it synergically enhances the fructose-1,6-bisphosphate activation. They increase the enzyme affinity for each other, and the combination increases Vmax, substrate apparent affinity, and decreases AMP inhibition. Our results indicate that there are two distinct interacting allosteric sites for activation. Hence, pyruvate modulates E. coli glycogen metabolism by orchestrating a functional network of allosteric regulators. We postulate that this novel dual activator mechanism increases the evolvability of ADP-glucose pyrophosphorylase and its related metabolic control.
Recommended Citation
Asención Diez MD, Aleanzi MC, Iglesias AA, Ballicora MA (2014) A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-Glucose Pyrophosphorylase: The Role of Pyruvate. PLoS ONE 9(8): e103888. doi:10.1371/journal.pone.0103888
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Copyright Statement
© 2014 Asención Diez et al.
Comments
Author posting. © 2014 Asención Diez et al. This article is posted here by permission of the authors for personal use, not for redistribution. The article was published in PLOS One, Volume 9, Issue 8, August 2014, http://dx.doi.org/10.1371/journal.pone.0103888