A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvate

Autor: Mabel Cristina Aleanzi, Miguel A. Ballicora, Alberto A. Iglesias, Matías Damián Asención Diez
Jazyk: angličtina
Rok vydání: 2014
Předmět:
lcsh:Medicine
Glucose-1-Phosphate Adenylyltransferase
medicine.disease_cause
Biochemistry
Substrate Specificity
purl.org/becyt/ford/1 [https]
chemistry.chemical_compound
Fructosediphosphates
Enzyme Chemistry
lcsh:Science
2. Zero hunger
chemistry.chemical_classification
Multidisciplinary
Glycogen
Bioquímica y Biología Molecular
Allosteric regulation
Recombinant Proteins
Enzymes
Carbohydrate Metabolism
CIENCIAS NATURALES Y EXACTAS
Allosteric Site
Research Article
Bacteria glycogen
Biology
Ciencias Biológicas
Enzyme Regulation
Enzyme activator
medicine
Escherichia coli
Enzyme kinetics
Pyruvates
purl.org/becyt/ford/1.6 [https]
Enzyme Kinetics
Activator (genetics)
lcsh:R
Synergic regulation
Biology and Life Sciences
Proteins
Enzyme Activation
Kinetics
Enzyme
Metabolism
chemistry
Enzymology
Biocatalysis
lcsh:Q
ADP-glucose synthesis
Zdroj: PLoS ONE, Vol 9, Iss 8, p e103888 (2014)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS ONE
ISSN: 1932-6203
Popis: 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. Fil: Asención Diez, Matías Damián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina. Loyola University Chicago. Department of Chemistry; Estados Unidos Fil: Aleanzi, Mabel C.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina Fil: Ballicora, Miguel A.. Loyola University Chicago. Department of Chemistry; Estados Unidos
Databáze: OpenAIRE