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dc.contributor.author
Cereijo, Antonela Estefanía  
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Asención Diez, Matías Damián  
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Ballicora, Miguel A.  
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Iglesias, Alberto Alvaro  
dc.date.available
2019-10-21T18:36:57Z  
dc.date.issued
2018-09  
dc.identifier.citation
Cereijo, Antonela Estefanía; Asención Diez, Matías Damián; Ballicora, Miguel A.; Iglesias, Alberto Alvaro; Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus; American Society for Microbiology; Journal of Bacteriology; 200; 17; 9-2018  
dc.identifier.issn
0021-9193  
dc.identifier.uri
http://hdl.handle.net/11336/86691  
dc.description.abstract
ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes (glgC and glgD) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, Bacillales and Lactobacillales, present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from Clostridiales, the third group in Firmicutes, has been characterized. For this reason, we cloned the glgC and glgD genes from Ruminococcus albus. Different quaternary forms of the enzyme (GlgC, GlgD, and GlgC/GlgD) were purified to homogeneity and their kinetic parameters were analyzed. We observed that GlgD is an inactive monomer when expressed alone but increased the catalytic efficiency of the heterotetramer (GlgC/GlgD) compared to the homotetramer (GlgC). The heterotetramer is regulated by fructose-1,6-bisphosphate, phosphoenolpyruvate, and NAD(P)H. The first characterization of the Bacillales enzyme suggested that heterotetrameric ADP-glucose pyrophosphorylases from Firmicutes were unregulated. Our results, together with data from Lactobacillales, indicate that heterotetrameric Firmicutes enzymes are mostly regulated. Thus, the ADPglucose pyrophosphorylase from Bacillales seems to have distinctive insensitivity to regulation.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
American Society for Microbiology  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
ADP-GLUCOSE PYROPHOSPHORYLASE  
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ALLOSTERISM  
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FRUCTOSE-1,6-BISPHOSPHATE  
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GLGC  
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GLGD  
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GLYCOGEN  
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GLYCOGEN METABOLISM  
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PHOSPHOENOLPYRUVATE  
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PYRUVATE  
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RUMINOCOCCUS ALBUS  
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Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-10-18T18:37:22Z  
dc.journal.volume
200  
dc.journal.number
17  
dc.journal.pais
Estados Unidos  
dc.description.fil
Fil: Cereijo, Antonela Estefanía. 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: Asención Diez, Matías Damián. 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.. University of Chicago; Estados Unidos  
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.journal.title
Journal of Bacteriology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://jb.asm.org/content/200/17/e00172-18  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1128/JB.00172-18