Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Asención Diez, Matías Damián | - |
| dc.creator | Ebrecht, Ana Cristina | - |
| dc.creator | Martínez, Lucila Inés | - |
| dc.creator | Aleanzi, Mabel Cristina | - |
| dc.creator | Guerrero, Sergio Adrian | - |
| dc.creator | Ballicora, Miguel A. | - |
| dc.creator | Iglesias, Alberto Alvaro | - |
| dc.date | 2015-08-11T20:43:08Z | - |
| dc.date | 2015-08-11T20:43:08Z | - |
| dc.date | 2013-05 | - |
| dc.date | 2016-03-30 10:35:44.97925-03 | - |
| dc.date.accessioned | 2019-04-29T15:34:42Z | - |
| dc.date.available | 2019-04-29T15:34:42Z | - |
| dc.date.issued | 2013-05 | - |
| dc.identifier | 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 | 1422-0067 | - |
| dc.identifier | http://hdl.handle.net/11336/1621 | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/296997 | - |
| dc.description | 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.description | 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: 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: 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: 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: 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: Ballicora, Miguel A.. University Of Chicago; Estados Unidos de América; | - |
| dc.description | Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico - CONICET - Santa Fe. Instituto de Agrobiotecnologia del Litoral; Argentina; | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Molecular Diversity Preservation International | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/ijms14059703 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/14/5/9703 | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.subject | protein engineering | - |
| dc.subject | allosteric regulation | - |
| dc.subject | pyrophosphorylases evolution | - |
| dc.subject | UDP-glucose | - |
| dc.subject | ADP-glucose | - |
| dc.subject | Bioquímica y Biología Molecular | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | 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:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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