Publication: Glycogen phosphorylase, the product of the glgP Gene, catalyzes glycogen breakdown by removing glucose units from the nonreducing ends in Escherichia coli
| dc.contributor.author | Alonso Casajús, Nora | |
| dc.contributor.author | Dauvillee, David | |
| dc.contributor.author | Viale Bailone, Alejandro M. | |
| dc.contributor.author | Muñoz Pérez, Francisco José | |
| dc.contributor.author | Baroja Fernández, Edurne | |
| dc.contributor.author | Morán Zorzano, María Teresa | |
| dc.contributor.author | Eydallin, Gustavo | |
| dc.contributor.author | Ball, Steven | |
| dc.contributor.author | Pozueta Romero, Javier | |
| dc.contributor.department | IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua | es_ES |
| dc.contributor.funder | Universidad Pública de Navarra / Nafarroako Unibertsitate Publikoa | es |
| dc.date.accessioned | 2019-01-23T11:16:23Z | |
| dc.date.available | 2019-01-23T11:16:23Z | |
| dc.date.issued | 2006 | |
| dc.description.abstract | To understand the biological function of bacterial glycogen phosphorylase (GlgP), we have produced and characterized Escherichia coli cells with null or altered glgP expression. glgP deletion mutants (ΔglgP) totally lacked glycogen phosphorylase activity, indicating that all the enzymatic activity is dependent upon the glgP product. Moderate increases of glycogen phosphorylase activity were accompanied by marked reductions of the intracellular glycogen levels in cells cultured in the presence of glucose. In turn, both glycogen content and rates of glycogen accumulation in ΔglgP cells were severalfold higher than those of wild-type cells. These defects correlated with the presence of longer external chains in the polysaccharide accumulated by ΔglgP cells. The overall results thus show that GlgP catalyzes glycogen breakdown and affects glycogen structure by removing glucose units from the polysaccharide outer chains in E. coli. | en |
| dc.description.sponsorship | This research was partially supported by grants BIO2001-1080 and BIO2004-01922 from the Consejo Interministerial de Ciencia y Tecnología and Fondo Europeo de Desarrollo Regional (Spain). A.M.V. expresses his most sincere gratitude to the Spanish Ministry of Culture and Education, to the Consejo Superior de Investigaciones Cientificas, and to the Public University of Navarra for their generous support. | en |
| dc.format.extent | 7 p. | |
| dc.format.mimetype | application/pdf | en |
| dc.identifier.doi | 10.1128/jb.01566-05 | |
| dc.identifier.issn | 0021-9193(Print) | |
| dc.identifier.issn | 1098-5530 (Electronic) | |
| dc.identifier.uri | https://academica-e.unavarra.es/handle/2454/32088 | |
| dc.language.iso | eng | en |
| dc.publisher | American Society for Microbiology | en |
| dc.relation.ispartof | Journal of Bacteriology, vol. 188, nº 14, july 2006, p. 5266–5272 | en |
| dc.relation.publisherversion | https://doi.org/10.1128/jb.01566-05 | |
| dc.rights | © 2006, American Society for Microbiology. All Rights Reserved. | en |
| dc.rights.accessRights | info:eu-repo/semantics/openAccess | en |
| dc.rights.accessRights | Acceso abierto / Sarbide irekia | es |
| dc.subject | Bacterial glycogen phosphorylase (GlgP) | en |
| dc.subject | Escherichia coli | en |
| dc.title | Glycogen phosphorylase, the product of the glgP Gene, catalyzes glycogen breakdown by removing glucose units from the nonreducing ends in Escherichia coli | en |
| dc.type | info:eu-repo/semantics/article | en |
| dc.type | Artículo / Artikulua | es |
| dc.type.version | info:eu-repo/semantics/publishedVersion | en |
| dc.type.version | Versión publicada / Argitaratu den bertsioa | es |
| dspace.entity.type | Publication | |
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