A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate

Autores
Asención Diez, Matías Damián; Aleanzi, Mabel C.; Iglesias, Alberto Alvaro; Ballicora, Miguel A.
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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
Materia
Allosteric regulation
Bacteria glycogen
ADP-glucose synthesis
Synergic regulation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/13167
Acceder
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network_name_str CONICET Digital (CONICET)
spelling A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvateAsención Diez, Matías DamiánAleanzi, Mabel C.Iglesias, Alberto AlvaroBallicora, Miguel A.Allosteric regulationBacteria glycogenADP-glucose synthesisSynergic regulationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Fructose-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 UnidosFil: Aleanzi, Mabel C.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Agrobiotecnologia del Litoral; ArgentinaFil: Ballicora, Miguel A.. Loyola University Chicago. Department of Chemistry; Estados UnidosPublic Library Of Science2014-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13167Asención Diez, Matías Damián; Aleanzi, Mabel C.; Iglesias, Alberto Alvaro; Ballicora, Miguel A.; A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate; Public Library Of Science; Plos One; 9; 8; 7-2014; e1038881932-6203enginfo:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0103888info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0103888info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:10:17Zoai:ri.conicet.gov.ar:11336/13167instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:10:18.282CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
title A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
spellingShingle A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
Asención Diez, Matías Damián
Allosteric regulation
Bacteria glycogen
ADP-glucose synthesis
Synergic regulation
title_short A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
title_full A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
title_fullStr A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
title_full_unstemmed A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
title_sort A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate
dc.creator.none.fl_str_mv Asención Diez, Matías Damián
Aleanzi, Mabel C.
Iglesias, Alberto Alvaro
Ballicora, Miguel A.
author Asención Diez, Matías Damián
author_facet Asención Diez, Matías Damián
Aleanzi, Mabel C.
Iglesias, Alberto Alvaro
Ballicora, Miguel A.
author_role author
author2 Aleanzi, Mabel C.
Iglesias, Alberto Alvaro
Ballicora, Miguel A.
author2_role author
author
author
dc.subject.none.fl_str_mv Allosteric regulation
Bacteria glycogen
ADP-glucose synthesis
Synergic regulation
topic Allosteric regulation
Bacteria glycogen
ADP-glucose synthesis
Synergic regulation
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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
description 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.
publishDate 2014
dc.date.none.fl_str_mv 2014-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/13167
Asención Diez, Matías Damián; Aleanzi, Mabel C.; Iglesias, Alberto Alvaro; Ballicora, Miguel A.; A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate; Public Library Of Science; Plos One; 9; 8; 7-2014; e103888
1932-6203
url http://hdl.handle.net/11336/13167
identifier_str_mv Asención Diez, Matías Damián; Aleanzi, Mabel C.; Iglesias, Alberto Alvaro; Ballicora, Miguel A.; A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-glucose Pyrophosphorylase: The role of pyruvate; Public Library Of Science; Plos One; 9; 8; 7-2014; e103888
1932-6203
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0103888
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0103888
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Public Library Of Science
publisher.none.fl_str_mv Public Library Of Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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