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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/93434
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/93434 |
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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 Técnicas2025-09-29T09:59:54Zoai: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:34982025-09-29 09:59:55.262CONICET 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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1844613774572519424 |
score |
13.070432 |