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dc.contributor.authorLu, Zhe
dc.contributor.authorCabiscol Català, Elisa
dc.contributor.authorObradors, Núria
dc.contributor.authorTamarit Sumalla, Jordi
dc.contributor.authorRos Salvador, Joaquim
dc.contributor.authorAguilar, Juan
dc.contributor.authorLin, Edmund C. C.
dc.date.accessioned2016-03-30T08:08:07Z
dc.date.available2016-03-30T08:08:07Z
dc.date.issued1998
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/10459.1/56766
dc.description.abstractL-1,2-Propanediol:NAD1 1-oxidoreductase of Escherichia coli is encoded by the fucO gene, a member of the regulon specifying dissimilation of L-fucose. The enzyme normally functions during fermentative growth to regenerate NAD from NADH by reducing the metabolic intermediate L-lactaldehyde to propanediol which is excreted. During aerobic growth L-lactaldehyde is converted to L-lactate and thence to the central metabolite pyruvate. The wasteful excretion of propanediol is minimized by oxidative inactivation of the oxidoreductase, an Fe21-dependent enzyme which is subject to metalcatalyzed oxidation (MCO). Mutants acquiring the ability to grow aerobically on propanediol as sole carbon and energy source can be readily selected. These mutants express the fucO gene constitutively, as a result of an IS5 insertion in the promoter region. In this study we show that continued selection for aerobic growth on propanediol resulted in mutations in the oxidoreductase conferring increased resistance to MCO. In two independent mutants, the resistance of the protein was respectively conferred by an Ile7 3 Leu and a Leu8 3 Val substitution near the NAD-binding consensus amino acid sequence. A site-directed mutant protein with both substitutions showed an MCO resistance greater than either mutant protein with a single amino acid change.ca_ES
dc.description.sponsorshipThis work was supported by United States Public Health Service Grants GM40993 and GM30693 from the NIGMS and Grant PB94-0829 from the Dirección General de Investigación Científica y Técnica, Madrid, Spain. Help from the Comissionat per Universitats i recerca de la Generalitat de Catalunya and the Ajuntament de Lleida was also received.ca_ES
dc.language.isoengca_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyca_ES
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1074/jbc.273.14.8308ca_ES
dc.relation.ispartofJournal of Biological Chemistry, 1998, Vol. 273, núm. 14, p. 8308-8316ca_ES
dc.rights(c) The American Society for Biochemistry and Molecular Biology, 1998ca_ES
dc.titleEvolution of an Escherichia coli Protein with Increased Resistance to Oxidative Stressca_ES
dc.typearticleca_ES
dc.identifier.idgrec000364
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1074/jbc.273.14.8308


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