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dc.contributor.author
Mokhtari, Abdelhamid
dc.contributor.author
Blancato, Victor Sebastian
dc.contributor.author
Repizo, Guillermo Daniel
dc.contributor.author
Henry, Céline
dc.contributor.author
Pikis, Andreas
dc.contributor.author
Bourand, Alexa
dc.contributor.author
Alvarez, Maria de Fatima
dc.contributor.author
Immel, Stefan
dc.contributor.author
Mechakra Maza, Aicha
dc.contributor.author
Hartke, Axel
dc.contributor.author
Thompson, John
dc.contributor.author
Magni, Christian
dc.contributor.author
Deutscher, Josef
dc.date.available
2016-03-21T14:20:50Z
dc.date.issued
2013-04
dc.identifier.citation
Mokhtari, Abdelhamid; Blancato, Victor Sebastian; Repizo, Guillermo Daniel; Henry, Céline; Pikis, Andreas; et al.; Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose-6-P phosphatase (MapP); Wiley; Molecular Microbiology; 88; 2; 4-2013; 234-253
dc.identifier.issn
0950-382X
dc.identifier.uri
http://hdl.handle.net/11336/4874
dc.description.abstract
Similar to Bacillus subtilis, Enterococcus faecalis transports and phosphorylates maltose via a phosphoenolpyruvate (PEP):maltose phosphotransferase system (PTS). The maltose-specific PTS permease is encoded by the malT gene. However, E. faecalis lacks a malA gene encoding a 6-phospho-a-glucosidase, which in B. subtilis hydrolyses maltose 6-P into glucose and glucose 6-P. Instead, an operon encoding a maltose phosphorylase (MalP), a phosphoglucomutase and a mutarotase starts upstream from malT. MalP was suggested to split maltose 6-P into glucose 1-P and glucose 6-P. However, purified MalP phosphorolyses maltose but not maltose 6-P. We discovered that the gene downstream from malT encodes a novel enzyme (MapP) that dephosphorylates maltose 6-P formed by the PTS. The resulting intracellular maltose is cleaved by MalP into glucose and glucose 1-P. Slow uptake of maltose probably via a maltodextrin ABC transporter allows poor growth for the mapP but not the malP mutant. Synthesis of MapP in a B. subtilis mutant accumulating maltose 6-P restored growth on maltose. MapP catalyses the dephosphorylation of intracellular maltose 6-P, and the resulting maltose is converted by the B. subtilis maltose phosphorylase into glucose and glucose 1-P. MapP therefore connects PTS-mediated maltose uptake to maltose phosphorylase-catalysed metabolism. Dephosphorylation assays with a wide variety of phosphosubstrates revealed that MapP preferably dephosphorylates disaccharides containing an O-aglycosyl linkage
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Maltose Metabolism
dc.subject
Enterococcus Faecalis
dc.subject
Maltose 6-Phosphate Phosphatase (Mapp)
dc.subject
Lactic Acid Bacterium
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose-6-P phosphatase (MapP)
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
88
dc.journal.number
2
dc.journal.pagination
234-253
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Hoboken
dc.description.fil
Fil: Mokhtari, Abdelhamid. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia. University Mentouri. Faculty of Natural Science and Life. Department of Biochemistry-Microbiology. Laboratory of Environmental Biology; Argelia
dc.description.fil
Fil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. 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 Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil
Fil: Henry, Céline. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia
dc.description.fil
Fil: Pikis, Andreas. Center for Drug Evaluation and Research. Food and Drug Administration; Estados Unidos
dc.description.fil
Fil: Bourand, Alexa. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia
dc.description.fil
Fil: Alvarez, Maria de Fatima. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Immel, Stefan. Technische Universität Darmstad. Institut für Organische Chemie; Alemania
dc.description.fil
Fil: Mechakra Maza, Aicha. University Mentouri. Faculty of Natural Science and Life. Department of Biochemistry-Microbiology. Laboratory of Environmental Biology; Argelia
dc.description.fil
Fil: Hartke, Axel. Universite de Caen Basse Normandie; Francia
dc.description.fil
Fil: Thompson, John. National Institutes of Health. Laboratory of Cell and Developmental Biology. Microbial Biochemistry and Genetics Section; Estados Unidos
dc.description.fil
Fil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil
Fil: Deutscher, Josef. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia
dc.journal.title
Molecular Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/mmi.12183/abstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/mmi.12183
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/10.1111/mmi.12183
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/pmid/PMC3633101
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3633101/
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