Allosteric Control of Substrate Specificity of the Escherichia coli ADP-Glucose Pyrophosphorylase.

ABSTRACT: The substrate specificity of enzymes is crucial to control the fate of metabolites to different pathways. However, there is growing evidence that many enzymes can catalyze alternative reactions. This promiscuous behavior has important implications in protein evolution and the acquisition of new functions. The question is how the undesirable outcomes of in vivo promiscuity can be prevented. ADP-glucose pyrophosphorylase from Escherichia coli is an example of an enzyme that needs to select the correct substrate from a broad spectrum of alternatives. This selection will guide the flow of carbohydrate metabolism toward the synthesis of reserve polysaccharides. Here, we show that the allosteric activator fructose-1,6-bisphosphate plays a role in such selection by increasing the ca

SUBMITTER: Ebrecht AC 

PROVIDER: S-EPMC5474683 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature