Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase

Autores
Ebrecht, Ana Cristina; Solamen, Ligin; Hill, Benjamin L.; Iglesias, Alberto Alvaro; Olsen, Kenneth W.; Ballicora, Miguel A.
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 catalytic efficiency of the enzyme toward the use of ATP rather than other nucleotides. In the presence of fructose-1,6-bisphosphate, the kcat/S0.5 for ATP was near ~600-fold higher that other nucleotides, whereas in the absence of activator was only ~3-fold higher. We propose that the allosteric regulation of certain enzymes is an evolutionary mechanism of adaptation for the selection of specific substrates.
Fil: Ebrecht, Ana Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. Loyola University Chicago; Estados Unidos
Fil: Solamen, Ligin. Loyola University Chicago; Estados Unidos
Fil: Hill, Benjamin L.. Loyola University Chicago; Estados Unidos
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Olsen, Kenneth W.. Loyola University Chicago; Estados Unidos
Fil: Ballicora, Miguel A.. Loyola University Chicago; Estados Unidos
Materia
ALLOSTERIC REGULATION
EFFECTORS INTERACTION
GLYCOGEN BIOSYNTHESIS
SUBSTRATE PROMISCUITY
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:11336/63641
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylaseEbrecht, Ana CristinaSolamen, LiginHill, Benjamin L.Iglesias, Alberto AlvaroOlsen, Kenneth W.Ballicora, Miguel A.ALLOSTERIC REGULATIONEFFECTORS INTERACTIONGLYCOGEN BIOSYNTHESISSUBSTRATE PROMISCUITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 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 catalytic efficiency of the enzyme toward the use of ATP rather than other nucleotides. In the presence of fructose-1,6-bisphosphate, the kcat/S0.5 for ATP was near ~600-fold higher that other nucleotides, whereas in the absence of activator was only ~3-fold higher. We propose that the allosteric regulation of certain enzymes is an evolutionary mechanism of adaptation for the selection of specific substrates.Fil: Ebrecht, Ana Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. Loyola University Chicago; Estados UnidosFil: Solamen, Ligin. Loyola University Chicago; Estados UnidosFil: Hill, Benjamin L.. Loyola University Chicago; Estados UnidosFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Olsen, Kenneth W.. Loyola University Chicago; Estados UnidosFil: Ballicora, Miguel A.. Loyola University Chicago; Estados UnidosFrontiers Research Foundation2017-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/63641Ebrecht, Ana Cristina; Solamen, Ligin; Hill, Benjamin L.; Iglesias, Alberto Alvaro; Olsen, Kenneth W.; et al.; Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase; Frontiers Research Foundation; Frontiers in Chemistry; 5; JUN; 6-2017; Article 412296-2646CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3389/fchem.2017.00041info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fchem.2017.00041/fullinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:15:37Zoai:ri.conicet.gov.ar:11336/63641instacron: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:34982025-10-22 12:15:37.569CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
title Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
spellingShingle Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
Ebrecht, Ana Cristina
ALLOSTERIC REGULATION
EFFECTORS INTERACTION
GLYCOGEN BIOSYNTHESIS
SUBSTRATE PROMISCUITY
title_short Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
title_full Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
title_fullStr Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
title_full_unstemmed Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
title_sort Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase
dc.creator.none.fl_str_mv Ebrecht, Ana Cristina
Solamen, Ligin
Hill, Benjamin L.
Iglesias, Alberto Alvaro
Olsen, Kenneth W.
Ballicora, Miguel A.
author Ebrecht, Ana Cristina
author_facet Ebrecht, Ana Cristina
Solamen, Ligin
Hill, Benjamin L.
Iglesias, Alberto Alvaro
Olsen, Kenneth W.
Ballicora, Miguel A.
author_role author
author2 Solamen, Ligin
Hill, Benjamin L.
Iglesias, Alberto Alvaro
Olsen, Kenneth W.
Ballicora, Miguel A.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv ALLOSTERIC REGULATION
EFFECTORS INTERACTION
GLYCOGEN BIOSYNTHESIS
SUBSTRATE PROMISCUITY
topic ALLOSTERIC REGULATION
EFFECTORS INTERACTION
GLYCOGEN BIOSYNTHESIS
SUBSTRATE PROMISCUITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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 catalytic efficiency of the enzyme toward the use of ATP rather than other nucleotides. In the presence of fructose-1,6-bisphosphate, the kcat/S0.5 for ATP was near ~600-fold higher that other nucleotides, whereas in the absence of activator was only ~3-fold higher. We propose that the allosteric regulation of certain enzymes is an evolutionary mechanism of adaptation for the selection of specific substrates.
Fil: Ebrecht, Ana Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. Loyola University Chicago; Estados Unidos
Fil: Solamen, Ligin. Loyola University Chicago; Estados Unidos
Fil: Hill, Benjamin L.. Loyola University Chicago; Estados Unidos
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Olsen, Kenneth W.. Loyola University Chicago; Estados Unidos
Fil: Ballicora, Miguel A.. Loyola University Chicago; Estados Unidos
description 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 catalytic efficiency of the enzyme toward the use of ATP rather than other nucleotides. In the presence of fructose-1,6-bisphosphate, the kcat/S0.5 for ATP was near ~600-fold higher that other nucleotides, whereas in the absence of activator was only ~3-fold higher. We propose that the allosteric regulation of certain enzymes is an evolutionary mechanism of adaptation for the selection of specific substrates.
publishDate 2017
dc.date.none.fl_str_mv 2017-06
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/11336/63641
Ebrecht, Ana Cristina; Solamen, Ligin; Hill, Benjamin L.; Iglesias, Alberto Alvaro; Olsen, Kenneth W.; et al.; Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase; Frontiers Research Foundation; Frontiers in Chemistry; 5; JUN; 6-2017; Article 41
2296-2646
CONICET Digital
CONICET
url http://hdl.handle.net/11336/63641
identifier_str_mv Ebrecht, Ana Cristina; Solamen, Ligin; Hill, Benjamin L.; Iglesias, Alberto Alvaro; Olsen, Kenneth W.; et al.; Allosteric control of substrate specificity of the Escherichia coli ADP-glucose pyrophosphorylase; Frontiers Research Foundation; Frontiers in Chemistry; 5; JUN; 6-2017; Article 41
2296-2646
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3389/fchem.2017.00041
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fchem.2017.00041/full
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
dc.publisher.none.fl_str_mv Frontiers Research Foundation
publisher.none.fl_str_mv Frontiers Research Foundation
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
_version_ 1846782571040473088
score 12.982451

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