Document Type

Article

Publication Date

8-2014

Publication Title

PLOS One

Volume

9

Issue

8

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.

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

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Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

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Chemistry Commons

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