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dc.contributor.author
Ebrecht, Ana Cristina
dc.contributor.author
Orlof, Agnieszka M.
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Sasoni, Natalia
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Figueroa, Carlos Maria
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Iglesias, Alberto Alvaro
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Ballicora, Miguel A.
dc.date.available
2018-03-22T18:51:21Z
dc.date.issued
2015-11
dc.identifier.citation
Ebrecht, Ana Cristina; Orlof, Agnieszka M.; Sasoni, Natalia; Figueroa, Carlos Maria; Iglesias, Alberto Alvaro; et al.; On the ancestral UDP-glucose pyrophosphorylase activity of GalF from Escherichia coli; Frontiers Research Foundation; Frontiers in Microbiology; 6; 1253; 11-2015; 1-13
dc.identifier.issn
1664-302X
dc.identifier.uri
http://hdl.handle.net/11336/39726
dc.description.abstract
In bacteria, UDP-glucose is a central intermediate in carbohydrate metabolism. The enzyme responsible for its synthesis is encoded by the galU gene and its deletion generates cells unable to ferment galactose. In some bacteria, there is a second gene, galF, encoding for a protein with high sequence identity to GalU. However, the role of GalF has been contradictory regarding its catalytic capability and not well understood. In this work we show that GalF derives from a catalytic (UDP-glucose pyrophosphorylase) ancestor, but its activity is very low compared to GalU. We demonstrated that GalF has some residual UDP-glucose pyrophosphorylase activity by in vitro and in vivo experiments in which the phenotype of a galU- strain was reverted by the over-expression of GalF and its mutant. To demonstrate its evolutionary path of "enzyme inactivation" we enhanced the catalysis by mutagenesis and showed the importance of the quaternary structure. This study provides important information to understand the structural and functional evolutionary origin of the protein GalF in enteric bacteria.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Frontiers Research Foundation
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
Catalytic Residues
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Enzyme Evolution
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Enzyme Inactivation
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Enzyme Resurrection
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Galactose Metabolism
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Nucleotidyltransferase
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
On the ancestral UDP-glucose pyrophosphorylase activity of GalF from Escherichia coli
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-21T16:53:20Z
dc.journal.volume
6
dc.journal.number
1253
dc.journal.pagination
1-13
dc.journal.pais
Suiza
dc.journal.ciudad
Lausana
dc.description.fil
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. Loyola University; Estados Unidos
dc.description.fil
Fil: Orlof, Agnieszka M.. Loyola University; Estados Unidos
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Fil: Sasoni, Natalia. 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: Figueroa, Carlos Maria. 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: 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
Fil: Ballicora, Miguel A.. Loyola University; Estados Unidos
dc.journal.title
Frontiers in Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fmicb.2015.01253/full
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fmicb.2015.01253
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