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dc.contributor.author
Bejar, Clarisa M.
dc.contributor.author
Ballicora, Miguel
dc.contributor.author
Gomez Casati, Diego Fabian
dc.contributor.author
Iglesias, Alberto Alvaro
dc.contributor.author
Preiss, Jack
dc.date.available
2020-01-03T17:58:32Z
dc.date.issued
2004-08-27
dc.identifier.citation
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
dc.identifier.issn
0014-5793
dc.identifier.uri
http://hdl.handle.net/11336/93434
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
ADP-GLC PPASE, ADP-GLUCOSE PYROPHOSPHORYLASE
dc.subject
ADP-GLC, ADP-GLUCOSE
dc.subject
FBP, FRUCTOSE 1,6-BISPHOSPHATE
dc.subject
GLC1P, GLUCOSE 1-PHOSPHATE
dc.subject
NDP-SUGAR PPASE, NUCLEOTIDE-DIPHOSPHATE-SUGAR PYROPHOSPHORYLASE
dc.subject
PEP, PHOSPHOENOLPYRUVATE
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-10T19:33:54Z
dc.journal.volume
573
dc.journal.number
1-3
dc.journal.pagination
99-104
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Bejar, Clarisa M.. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
dc.description.fil
Fil: Ballicora, Miguel. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
dc.description.fil
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
dc.description.fil
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
dc.description.fil
Fil: Preiss, Jack. Michigan State University. Department of Biochemistry and Molecular Biology; Estados Unidos
dc.journal.title
FEBS Letters
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0014579304009433
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.febslet.2004.07.060


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