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dc.contributor.author
Figueroa, Carlos Maria
dc.contributor.author
Esper, María Cecilia
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Bertolo, Ana
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Demonte, Ana María Magdalena
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Aleanzi, Mabel Cristina
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Iglesias, Alberto Alvaro
dc.contributor.author
Ballicora, Miguel A.
dc.date.available
2019-05-08T20:37:24Z
dc.date.issued
2011-10
dc.identifier.citation
Figueroa, Carlos Maria; Esper, María Cecilia; Bertolo, Ana; Demonte, Ana María Magdalena; Aleanzi, Mabel Cristina; et al.; Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli; Elsevier France-editions Scientifiques Medicales Elsevier; Biochimie; 93; 10; 10-2011; 1816-1823
dc.identifier.issn
0300-9084
dc.identifier.uri
http://hdl.handle.net/11336/75919
dc.description.abstract
ADP-glucose pyrophosphorylase is the enzyme responsible for the regulation of glycogen synthesis in bacteria. The enzyme N-terminal domain has a Rossmann-like fold with three neighbor loops facing the substrate ATP. In the Escherichia coli enzyme, one of those loops also faces the regulatory site containing Lys 39, a residue involved in binding of the allosteric activator fructose-1,6-bisphosphate and its analog pyridoxal-phosphate. The other two loops contain Trp 113 and Gln 74, respectively, which are highly conserved among all the ADP-glucose pyrophosphorylases. Molecular modeling of the E. coli enzyme showed that binding of ATP correlates with conformational changes of the latter two loops, going from an open to a closed (substrate-bound) form. Alanine mutants of Trp 113 or Gln 74 did not change apparent affinities for the substrates, but they became insensitive to activation by fructose-1,6-bisphosphate. By capillary electrophoresis we found that the mutant enzymes still bind fructose-1,6- bisphosphate, with similar affinity as the wild type enzyme. Since the mutations did not alter binding of the activator, they must have disrupted the communication between the regulatory and the substrate sites. This agrees with a regulatory mechanism where the interaction with the allosteric activator triggers conformational changes at the level of loops containing residues Trp 113 and Gln 74.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier France-editions Scientifiques Medicales Elsevier
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Activation Signal Propagation
dc.subject
Adp-Glucose Pyrophosphorylase
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Allosteric Mechanism
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Glycogen/Starch Metabolism
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Regulation Dynamics
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-04-26T15:38:04Z
dc.journal.volume
93
dc.journal.number
10
dc.journal.pagination
1816-1823
dc.journal.pais
Francia
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Figueroa, Carlos Maria. 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
dc.description.fil
Fil: Esper, María Cecilia. 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
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Fil: Bertolo, Ana. Cornell University; Estados Unidos
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Fil: Demonte, Ana María Magdalena. 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
dc.description.fil
Fil: Aleanzi, Mabel 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
dc.description.fil
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
dc.description.fil
Fil: Ballicora, Miguel A.. Loyola University Chicago; Estados Unidos
dc.journal.title
Biochimie
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0300908411002264
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.biochi.2011.06.029
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