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dc.contributor.author
Ballicora, Miguel A.
dc.contributor.author
Erben, Esteban Daniel
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Yazaki, Terutaka
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Bertolo, Ana L.
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Demonte, Ana María Magdalena
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Schmidt, Jennifer R.
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Aleanzi, Mabel Cristina
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Bejar, Clarisa M.
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Figueroa, Carlos Maria
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Fusari, Corina M.
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Iglesias, Alberto Alvaro
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Preiss, Jack
dc.date.available
2019-07-17T14:14:42Z
dc.date.issued
2007-07
dc.identifier.citation
Ballicora, Miguel A.; Erben, Esteban Daniel; Yazaki, Terutaka; Bertolo, Ana L.; Demonte, Ana María Magdalena; et al.; Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis; American Society for Microbiology; Journal of Bacteriology; 189; 14; 7-2007; 5325-5333
dc.identifier.issn
0021-9193
dc.identifier.uri
http://hdl.handle.net/11336/79729
dc.description.abstract
ADP-glucose pyrophosphorylase (ADP-Glc PPase) is the enzyme responsible for the regulation of bacterial glycogen synthesis. To perform a structure-function relationship study of the Escherichia coli ADP-Glc PPase enzyme, we studied the effects of pentapeptide insertions at different positions in the enzyme and analyzed the results with a homology model. We randomly inserted 15 bp in a plasmid with the ADP-Glc PPase gene. We obtained 140 modified plasmids with single insertions of which 21 were in the coding region of the enzyme. Fourteen of them generated insertions of five amino acids, whereas the other seven created a stop codon and produced truncations. Correlation of ADP-Glc PPase activity to these modifications validated the enzyme model. Six of the insertions and one truncation produced enzymes with sufficient activity for the E. coli cells to synthesize glycogen and stain in the presence of iodine vapor. These were in regions away from the substrate site, whereas the mutants that did not stain had alterations in critical areas of the protein. The enzyme with a pentapeptide insertion between Leu102 and Pro103 was catalytically competent but insensitive to activation. We postulate this region as critical for the allosteric regulation of the enzyme, participating in the communication between the catalytic and regulatory domains.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Microbiology
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Adp-Glucose Pyrophosphorylase
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-07-15T14:22:01Z
dc.journal.volume
189
dc.journal.number
14
dc.journal.pagination
5325-5333
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
Fil: Ballicora, Miguel A.. Loyola University; Estados Unidos
dc.description.fil
Fil: Erben, Esteban Daniel. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Enzimología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
dc.description.fil
Fil: Yazaki, Terutaka. Michigan State University; Estados Unidos
dc.description.fil
Fil: Bertolo, Ana L.. Michigan State University; Estados Unidos
dc.description.fil
Fil: Demonte, Ana María Magdalena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Enzimología Molecular; Argentina
dc.description.fil
Fil: Schmidt, Jennifer R.. Michigan State University; Estados Unidos
dc.description.fil
Fil: Aleanzi, Mabel Cristina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Enzimología Molecular; Argentina
dc.description.fil
Fil: Bejar, Clarisa M.. Michigan State University; Estados Unidos
dc.description.fil
Fil: Figueroa, Carlos Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Enzimología Molecular; Argentina
dc.description.fil
Fil: Fusari, Corina M.. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Enzimología Molecular; Argentina
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Laboratorio de Enzimología Molecular; Argentina
dc.description.fil
Fil: Preiss, Jack. Michigan State University; Estados Unidos
dc.journal.title
Journal of Bacteriology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/17496097
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1128/JB.00481-07
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://jb.asm.org/content/189/14/5325


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