Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Ebrecht, Ana Cristina | - |
| dc.creator | Solamen, Ligin | - |
| dc.creator | Hill, Benjamin L. | - |
| dc.creator | Iglesias, Alberto Alvaro | - |
| dc.creator | Olsen, Kenneth W. | - |
| dc.creator | Ballicora, Miguel A. | - |
| dc.date | 2018-06-08T20:46:59Z | - |
| dc.date | 2018-06-08T20:46:59Z | - |
| dc.date | 2017-06 | - |
| dc.date | 2018-05-31T18:14:16Z | - |
| dc.date.accessioned | 2019-04-29T15:50:28Z | - |
| dc.date.available | 2019-04-29T15:50:28Z | - |
| dc.date.issued | 2017-06 | - |
| dc.identifier | Ebrecht, Ana Cristina; Solamen, Ligin; Hill, Benjamin L.; Iglesias, Alberto Alvaro; Olsen, Kenneth W.; et al.; Allosteric Control of Substrate Specificity of the Escherichia coli ADP-Glucose Pyrophosphorylase; Frontiers Research Foundation; Frontiers in Chemistry; 5; 41; 6-2017; 1-11 | - |
| dc.identifier | http://hdl.handle.net/11336/48005 | - |
| dc.identifier | 2296-2646 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/303436 | - |
| dc.description | The substrate specificity of enzymes is crucial to control the fate of metabolites to different pathways. However, there is growing evidence that many enzymes can catalyze alternative reactions. This promiscuous behavior has important implications in protein evolution and the acquisition of new functions. The question is how the undesirable outcomes of in vivo promiscuity can be prevented. ADP-glucose pyrophosphorylase from Escherichia coli is an example of an enzyme that needs to select the correct substrate from a broad spectrum of alternatives. This selection will guide the flow of carbohydrate metabolism toward the synthesis of reserve polysaccharides. Here, we show that the allosteric activator fructose-1,6-bisphosphate plays a role in such selection by increasing the catalytic efficiency of the enzyme toward the use of ATP rather than other nucleotides. In the presence of fructose-1,6-bisphosphate, the kcat/S0.5 for ATP was near ~600-fold higher that other nucleotides, whereas in the absence of activator was only ~3-fold higher. We propose that the allosteric regulation of certain enzymes is an evolutionary mechanism of adaptation for the selection of specific substrates. | - |
| dc.description | Fil: Ebrecht, Ana Cristina. 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. University of Chicago; Estados Unidos | - |
| dc.description | Fil: Solamen, Ligin. University of Chicago; Estados Unidos | - |
| dc.description | Fil: Hill, Benjamin L.. University of Chicago; Estados Unidos | - |
| dc.description | 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.description | Fil: Olsen, Kenneth W.. University of Chicago; Estados Unidos | - |
| dc.description | Fil: Ballicora, Miguel A.. University of Chicago; Estados Unidos | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Frontiers Research Foundation | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.3389/fchem.2017.00041 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fchem.2017.00041/full | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by/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 | Allosteric regulation | - |
| dc.subject | Effectors interaction | - |
| dc.subject | Glycogen biosynthesis | - |
| dc.subject | Substrate promiscuity | - |
| dc.subject | Otras Ciencias Biológicas | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Allosteric Control of Substrate Specificity of the Escherichia coli ADP-Glucose Pyrophosphorylase | - |
| 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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