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dc.contributor.authorSangari, Félix J.-
dc.contributor.authorPérez-Gil, Jordi-
dc.contributor.authorCarretero-Paulet, Lorenzo-
dc.contributor.authorGarcía-Lobo, Juan M.-
dc.contributor.authorRodriguez-Concepcion, Manuel-
dc.date.accessioned2010-10-26T09:30:32Z-
dc.date.available2010-10-26T09:30:32Z-
dc.date.issued2010-07-26-
dc.identifier.citationProceedings of the National Academy of Sciences 107(32): 14081-14086 (2010)es_ES
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10261/28717-
dc.description6 pages, 4 figures, 1 table.es_ES
dc.description.abstractIsoprenoids are a large family of compounds with essential functions in all domains of life. Most eubacteria synthesize their isoprenoids using the methylerythritol 4-phosphate (MEP) pathway, whereas a minority uses the unrelated mevalonate pathway and only a few have both. Interestingly, Brucella abortus and some other bacteria that only use the MEP pathway lack deoxyxylulose 5-phosphate (DXP) reductoisomerase (DXR), the enzyme catalyzing the NADPH-dependent production of MEP from DXP in the first committed step of the pathway. Fosmidomycin, a specific competitive inhibitor of DXR, inhibited growth of B. abortus cells expressing the Escherichia coli GlpT transporter (required for fosmidomycin uptake), confirming that a DXR-like (DRL) activity exists in these bacteria. The B. abortus DRL protein was found to belong to a family of uncharacterized proteins similar to homoserine dehydrogenase. Subsequent experiments confirmed that DRL and DXR catalyze the same biochemical reaction. DRL homologues shown to complement a DXR-deficient E. coli strain grouped within the same phylogenetic clade. The scattered taxonomic distribution of sequences from the DRL clade and the occurrence of several paralogues in some bacterial strains might be the result of lateral gene transfer and lineage-specific gene duplications and/or losses, similar to that described for typical mevalonate and MEP pathway genes. These results reveal the existence of a novel class of oxidoreductases catalyzing the conversion of DXP into MEP in prokaryotic cells, underscoring the biochemical and genetic plasticity achieved by bacteria to synthesize essential compounds such as isoprenoids.es_ES
dc.description.sponsorshipThe Spanish Ministerio de Ciencia e Innovación provided a PhD fellowship to J.P.-G., a Juan de la Cierva contract to L.C.-P. (cofinanced by the European Social Fund), research Grants BIO2007-63656 to F.J.S. and BIO2008-00432 to M.R.-C., as well as funding through a Consolider program (CSD2007-00036). This work was also supported by grants from the Fundación Marqués de Valdecilla (API 07∕01) to F.J.S., and the Generalitat de Catalunya (SGR and XaRBa) to M.R.-C.es_ES
dc.language.isoenges_ES
dc.publisherNational Academy of Sciences (U.S.)es_ES
dc.rightsopenAccesses_ES
dc.subjectBrucellaes_ES
dc.subjectDXRes_ES
dc.subjectFosmidomycines_ES
dc.subjectMethylerythritoles_ES
dc.subjectPhylogenetices_ES
dc.titleA new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteriaes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1073/pnas.1001962107-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1073/pnas.1001962107es_ES
dc.identifier.e-issn1091-6490-
dc.identifier.pmid20660776-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairetypeartículo-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
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