The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains

Autores
Bejar, Clarisa M.; Ballicora, Miguel; Gomez Casati, Diego Fabian; Iglesias, Alberto Alvaro; Preiss, Jack
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Computational analysis of ADP-glucose pyrophosphorylases predicts a fold with two domains. Co-expression of two polypeptides comprising residues 1-323 and 328-431 from the Escherichia coli ADP-glucose pyrophosphorylase yielded an enzyme form as active as the wild type. The only difference from the wild type was a slightly modified affinity for allosteric effectors. The two polypeptides could not be separated by chromatographic procedures. Separate expression of these polypeptides produced inactive unstable forms. All these results indicated that the ADP-glucose pyrophosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability.
Fil: Bejar, Clarisa M.. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Ballicora, Miguel. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Iglesias, Alberto Alvaro. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos. 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: Preiss, Jack. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
Materia
ADP-GLC PPASE, ADP-GLUCOSE PYROPHOSPHORYLASE
ADP-GLC, ADP-GLUCOSE
FBP, FRUCTOSE 1,6-BISPHOSPHATE
GLC1P, GLUCOSE 1-PHOSPHATE
NDP-SUGAR PPASE, NUCLEOTIDE-DIPHOSPHATE-SUGAR PYROPHOSPHORYLASE
PEP, PHOSPHOENOLPYRUVATE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/93434
Acceder
id CONICETDig_35665c51d1f40e213df4769424d3c50c
oai_identifier_str oai:ri.conicet.gov.ar:11336/93434
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domainsBejar, Clarisa M.Ballicora, MiguelGomez Casati, Diego FabianIglesias, Alberto AlvaroPreiss, JackADP-GLC PPASE, ADP-GLUCOSE PYROPHOSPHORYLASEADP-GLC, ADP-GLUCOSEFBP, FRUCTOSE 1,6-BISPHOSPHATEGLC1P, GLUCOSE 1-PHOSPHATENDP-SUGAR PPASE, NUCLEOTIDE-DIPHOSPHATE-SUGAR PYROPHOSPHORYLASEPEP, PHOSPHOENOLPYRUVATEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Computational analysis of ADP-glucose pyrophosphorylases predicts a fold with two domains. Co-expression of two polypeptides comprising residues 1-323 and 328-431 from the Escherichia coli ADP-glucose pyrophosphorylase yielded an enzyme form as active as the wild type. The only difference from the wild type was a slightly modified affinity for allosteric effectors. The two polypeptides could not be separated by chromatographic procedures. Separate expression of these polypeptides produced inactive unstable forms. All these results indicated that the ADP-glucose pyrophosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability.Fil: Bejar, Clarisa M.. Michigan State University. Department of Biochemistry and Molecular Biology; Estados UnidosFil: Ballicora, Miguel. Michigan State University. Department of Biochemistry and Molecular Biology; Estados UnidosFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Iglesias, Alberto Alvaro. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos. 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: Preiss, Jack. Michigan State University. Department of Biochemistry and Molecular Biology; Estados UnidosElsevier Science2004-08-27info: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/11336/93434Bejar, Clarisa M.; Ballicora, Miguel; Gomez Casati, Diego Fabian; Iglesias, Alberto Alvaro; Preiss, Jack; The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains; Elsevier Science; FEBS Letters; 573; 1-3; 27-8-2004; 99-1040014-5793CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0014579304009433info:eu-repo/semantics/altIdentifier/doi/10.1016/j.febslet.2004.07.060info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:29:22Zoai:ri.conicet.gov.ar:11336/93434instacron: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 11:29:22.845CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
title The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
spellingShingle The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
Bejar, Clarisa M.
ADP-GLC PPASE, ADP-GLUCOSE PYROPHOSPHORYLASE
ADP-GLC, ADP-GLUCOSE
FBP, FRUCTOSE 1,6-BISPHOSPHATE
GLC1P, GLUCOSE 1-PHOSPHATE
NDP-SUGAR PPASE, NUCLEOTIDE-DIPHOSPHATE-SUGAR PYROPHOSPHORYLASE
PEP, PHOSPHOENOLPYRUVATE
title_short The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
title_full The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
title_fullStr The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
title_full_unstemmed The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
title_sort The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
dc.creator.none.fl_str_mv Bejar, Clarisa M.
Ballicora, Miguel
Gomez Casati, Diego Fabian
Iglesias, Alberto Alvaro
Preiss, Jack
author Bejar, Clarisa M.
author_facet Bejar, Clarisa M.
Ballicora, Miguel
Gomez Casati, Diego Fabian
Iglesias, Alberto Alvaro
Preiss, Jack
author_role author
author2 Ballicora, Miguel
Gomez Casati, Diego Fabian
Iglesias, Alberto Alvaro
Preiss, Jack
author2_role author
author
author
author
dc.subject.none.fl_str_mv ADP-GLC PPASE, ADP-GLUCOSE PYROPHOSPHORYLASE
ADP-GLC, ADP-GLUCOSE
FBP, FRUCTOSE 1,6-BISPHOSPHATE
GLC1P, GLUCOSE 1-PHOSPHATE
NDP-SUGAR PPASE, NUCLEOTIDE-DIPHOSPHATE-SUGAR PYROPHOSPHORYLASE
PEP, PHOSPHOENOLPYRUVATE
topic ADP-GLC PPASE, ADP-GLUCOSE PYROPHOSPHORYLASE
ADP-GLC, ADP-GLUCOSE
FBP, FRUCTOSE 1,6-BISPHOSPHATE
GLC1P, GLUCOSE 1-PHOSPHATE
NDP-SUGAR PPASE, NUCLEOTIDE-DIPHOSPHATE-SUGAR PYROPHOSPHORYLASE
PEP, PHOSPHOENOLPYRUVATE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Computational analysis of ADP-glucose pyrophosphorylases predicts a fold with two domains. Co-expression of two polypeptides comprising residues 1-323 and 328-431 from the Escherichia coli ADP-glucose pyrophosphorylase yielded an enzyme form as active as the wild type. The only difference from the wild type was a slightly modified affinity for allosteric effectors. The two polypeptides could not be separated by chromatographic procedures. Separate expression of these polypeptides produced inactive unstable forms. All these results indicated that the ADP-glucose pyrophosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability.
Fil: Bejar, Clarisa M.. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Ballicora, Miguel. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Iglesias, Alberto Alvaro. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos. 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: Preiss, Jack. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
description Computational analysis of ADP-glucose pyrophosphorylases predicts a fold with two domains. Co-expression of two polypeptides comprising residues 1-323 and 328-431 from the Escherichia coli ADP-glucose pyrophosphorylase yielded an enzyme form as active as the wild type. The only difference from the wild type was a slightly modified affinity for allosteric effectors. The two polypeptides could not be separated by chromatographic procedures. Separate expression of these polypeptides produced inactive unstable forms. All these results indicated that the ADP-glucose pyrophosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability.
publishDate 2004
dc.date.none.fl_str_mv 2004-08-27
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/11336/93434
Bejar, Clarisa M.; Ballicora, Miguel; Gomez Casati, Diego Fabian; Iglesias, Alberto Alvaro; Preiss, Jack; The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains; Elsevier Science; FEBS Letters; 573; 1-3; 27-8-2004; 99-104
0014-5793
CONICET Digital
CONICET
url http://hdl.handle.net/11336/93434
identifier_str_mv Bejar, Clarisa M.; Ballicora, Miguel; Gomez Casati, Diego Fabian; Iglesias, Alberto Alvaro; Preiss, Jack; The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains; Elsevier Science; FEBS Letters; 573; 1-3; 27-8-2004; 99-104
0014-5793
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0014579304009433
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.febslet.2004.07.060
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier 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 12.982451

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