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dc.contributor.author
Asención Diez, Matías Damián
dc.contributor.author
Ebrecht, Ana Cristina
dc.contributor.author
Martínez, Lucila Inés
dc.contributor.author
Aleanzi, Mabel Cristina
dc.contributor.author
Guerrero, Sergio Adrian
dc.contributor.author
Ballicora, Miguel A.
dc.contributor.author
Iglesias, Alberto Alvaro
dc.date.available
2015-08-11T20:43:08Z
dc.date.issued
2013-05
dc.identifier.citation
Asención Diez, Matías Damián; Ebrecht, Ana Cristina; Martínez, Lucila Inés; Aleanzi, Mabel Cristina; Guerrero, Sergio Adrian; et al.; A Chimeric UDP-Glucose Pyrophosphorylase Produced by Protein Engineering Exhibits Sensitivity to Allosteric Regulators; Molecular Diversity Preservation International; International Journal Of Molecular Sciences; 14; 5; 5-2013; 9703-9721
dc.identifier.issn
1422-0067
dc.identifier.uri
http://hdl.handle.net/11336/1621
dc.description.abstract
In bacteria, glycogen or oligosaccharide accumulation involves glucose-1-phosphate partitioning into either ADP-glucose (ADP-Glc) or UDP-Glc. Their respective synthesis is catalyzed by allosterically regulated ADP-Glc pyrophosphorylase (EC 2.7.7.27, ADP-Glc PPase) or unregulated UDP-Glc PPase (EC 2.7.7.9). In this work, we characterized the UDP-Glc PPase from Streptococcus mutans . In addition, we constructed a chimeric protein by cutting the C-terminal domain of the ADP-Glc PPase from Escherichia coli and pasting it to the entire S. mutans UDP-Glc PPase. Both proteins were fully active as UDP-Glc PPases and their kinetic parameters were measured. The chimeric enzyme had a slightly higher affinity for substrates than the native S. mutans UDP-Glc PPase, but the maximal activity was four times lower. Interestingly, the chimeric protein was sensitive to regulation by pyruvate, 3-phosphoglyceric acid and fructose-1,6-bis-phosphate, which are known to be effectors of ADP-Glc PPases from different sources. The three compounds activated the chimeric enzyme up to three-fold, and increased the affinity for substrates. This chimeric protein is the first reported UDP-Glc PPase with allosteric regulatory properties. In addition, this is a pioneer work dealing with a chimeric enzyme constructed as a hybrid of two pyrophosphorylases with different specificity toward nucleoside-diphospho-glucose and our results turn to be relevant for a deeper understanding of the evolution of allosterism in this family of enzymes.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Molecular Diversity Preservation International
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Protein Engineering
dc.subject
Allosteric Regulation
dc.subject
Pyrophosphorylases Evolution
dc.subject
Udp-Glucose
dc.subject
Adp-Glucose
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
A Chimeric UDP-Glucose Pyrophosphorylase Produced by Protein Engineering Exhibits Sensitivity to Allosteric Regulators
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-03-30 10:35:44.97925-03
dc.journal.volume
14
dc.journal.number
5
dc.journal.pagination
9703-9721
dc.journal.pais
Suiza
dc.journal.ciudad
Basel
dc.description.fil
Fil: Asención Diez, Matías Damián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.description.fil
Fil: Ebrecht, Ana Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.description.fil
Fil: Martínez, Lucila Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.description.fil
Fil: Aleanzi, Mabel Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.description.fil
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.description.fil
Fil: Ballicora, Miguel A.. University Of Chicago; Estados Unidos de América;
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina;
dc.journal.title
International Journal Of Molecular Sciences
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/ijms14059703
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/14/5/9703


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