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dc.provenanceCONICET-
dc.creatorMokhtari, Abdelhamid-
dc.creatorBlancato, Victor Sebastian-
dc.creatorRepizo, Guillermo Daniel-
dc.creatorHenry, Céline-
dc.creatorPikis, Andreas-
dc.creatorBourand, Alexa-
dc.creatorAlvarez, Maria de Fatima-
dc.creatorImmel, Stefan-
dc.creatorMechakra Maza, Aicha-
dc.creatorHartke, Axel-
dc.creatorThompson, John-
dc.creatorMagni, Christian-
dc.creatorDeutscher, Josef-
dc.date2016-03-21T14:20:50Z-
dc.date2016-03-21T14:20:50Z-
dc.date2013-04-
dc.date2016-03-30 10:35:44.97925-03-
dc.date.accessioned2019-04-29T15:36:38Z-
dc.date.available2019-04-29T15:36:38Z-
dc.date.issued2013-04-
dc.identifierMokhtari, 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.identifier0950-382X-
dc.identifierhttp://hdl.handle.net/11336/4874-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/297688-
dc.descriptionSimilar 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.descriptionFil: 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.descriptionFil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina-
dc.descriptionFil: Repizo, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina-
dc.descriptionFil: Henry, Céline. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia-
dc.descriptionFil: Pikis, Andreas. Center for Drug Evaluation and Research. Food and Drug Administration; Estados Unidos-
dc.descriptionFil: Bourand, Alexa. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia-
dc.descriptionFil: Alvarez, Maria de Fatima. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina-
dc.descriptionFil: Immel, Stefan. Technische Universität Darmstad. Institut für Organische Chemie; Alemania-
dc.descriptionFil: Mechakra Maza, Aicha. University Mentouri. Faculty of Natural Science and Life. Department of Biochemistry-Microbiology. Laboratory of Environmental Biology; Argelia-
dc.descriptionFil: Hartke, Axel. Universite de Caen Basse Normandie; Francia-
dc.descriptionFil: Thompson, John. National Institutes of Health. Laboratory of Cell and Developmental Biology. Microbial Biochemistry and Genetics Section; Estados Unidos-
dc.descriptionFil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina-
dc.descriptionFil: Deutscher, Josef. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia-
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dc.languageeng-
dc.publisherWiley-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/mmi.12183/abstract-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/mmi.12183-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.1111/mmi.12183-
dc.relationinfo:eu-repo/semantics/altIdentifier/pmid/PMC3633101-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3633101/-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/4874-
dc.subjectMaltose Metabolism-
dc.subjectEnterococcus faecalis-
dc.subjectMaltose 6-phosphate phosphatase (MapP)-
dc.subjectLactic acid bacterium-
dc.subjectBioquímica y Biología Molecular-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleEnterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose-6-P phosphatase (MapP)-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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