Mostrar el registro sencillo del ítem
dc.contributor.author
Espariz, Martin
dc.contributor.author
Repizo, Guillermo Daniel
dc.contributor.author
Blancato, Victor Sebastian
dc.contributor.author
Mortera, Pablo
dc.contributor.author
Alarcon, Sergio Hugo
dc.contributor.author
Magni, Christian
dc.date.available
2021-06-16T12:02:43Z
dc.date.issued
2011-06
dc.identifier.citation
Espariz, Martin; Repizo, Guillermo Daniel; Blancato, Victor Sebastian; Mortera, Pablo; Alarcon, Sergio Hugo; et al.; Identification of malic and soluble oxaloacetate decarboxylase enzymes in Enterococcus faecalis; Wiley Blackwell Publishing, Inc; Febs Journal; 278; 12; 6-2011; 2140-2151
dc.identifier.issn
1742-464X
dc.identifier.uri
http://hdl.handle.net/11336/133972
dc.description.abstract
Two paralogous genes, maeE and citM, that encode putative malic enzyme family members were identified in the Enterococcus faecalis genome. MaeE (41 kDa) and CitM (42 kDa) share a high degree of homology between them (47% identities and 68% conservative substitutions). However, the genetic context of each gene suggested that maeE is associated with malate utilization whereas citM is linked to the citrate fermentation pathway. In the present work, we focus on the biochemical characterization and physiological contribution of these enzymes in E. faecalis. With this aim, the recombinant versions of the two proteins were expressed in Escherichia coli, affinity purified and finally their kinetic parameters were determined. This approach allowed us to establish that MaeE is a malate oxidative decarboxylating enzyme and CitM is a soluble oxaloacetate decarboxylase. Moreover, our genetic studies in E. faecalis showed that the citrate fermentation phenotype is not affected by citM deletion. On the other hand, maeE gene disruption resulted in a malate fermentation deficient strain indicating that MaeE is responsible for malate metabolism in E. faecalis. Lastly, it was demonstrated that malate fermentation in E. faecalis is associated with cytoplasmic and extracellular alkalinization which clearly contributes to pH homeostasis in neutral or mild acidic conditions. In the present study, we performed a biochemical characterization of two members of the malic enzyme family from Enterococcus faecalis. It was stated that MaeE is a malate oxidative decarboxylating enzyme whereas CitM is a soluble oxaloacetate decarboxylase. Our genetic studies showed that the citrate fermentation phenotype is not affected by citM deletion. Conversely, maeE gene disruption resulted in a malate deficient strain.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CITRATE METABOLISM
dc.subject
ENTEROCOCCUS FAECALIS
dc.subject
MALATE METABOLISM
dc.subject
MALIC ENZYME
dc.subject
OXALOACETATE DECARBOXYLASE
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Identification of malic and soluble oxaloacetate decarboxylase enzymes in Enterococcus faecalis
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-12-22T15:49:55Z
dc.journal.volume
278
dc.journal.number
12
dc.journal.pagination
2140-2151
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Espariz, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil
Fil: Repizo, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil
Fil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil
Fil: Mortera, Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina
dc.description.fil
Fil: Alarcon, Sergio Hugo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina
dc.description.fil
Fil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.journal.title
Febs Journal
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1111/j.1742-4658.2011.08131.x
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2011.08131.x
Archivos asociados