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dc.contributor.authorGüclü, Denizes_ES
dc.contributor.authorSzekrenyi, Annaes_ES
dc.contributor.authorGarrabou, Xavieres_ES
dc.contributor.authorKickstein, Michaeles_ES
dc.contributor.authorJunker, Sebastianes_ES
dc.contributor.authorFessner, Wolf-Dieteres_ES
dc.contributor.authorClapés Saborit, Perees_ES
dc.date.accessioned2016-02-26T09:30:33Z-
dc.date.available2016-02-26T09:30:33Z-
dc.date.issued2016-02-04-
dc.identifier.citationACS Catalysises_ES
dc.identifier.urihttp://hdl.handle.net/10261/129488-
dc.description.abstractApplication of aldolases for the asymmetric synthesis of multifunctional chiral products is hampered by their reputed strict nucleophile (=aldol donor) specificity owing to a mechanistic requirement for creating a carbanion nucleophile in aqueous medium. Here we report that a minimalist engineering can extensively broaden the substrate scope of native d-fructose-6-phosphate aldolase (FSA) from Escherichia coli, for which hydroxyacetone is the most proficient substrate, to accept an unprecedented wide variety of alternative nucleophiles. By single- or double-space-generating mutations using simple conservative Leu to Ala replacement of active site residues, we found enzyme variants to efficiently convert larger ketols and bioisosteric ether components with up to seven skeletal atoms, including linear and branched-chain structures. All reactions occurred with full retention of the natural d-threo diastereospecificity. These FSA variants open new avenues toward the synthesis of novel product families that hitherto were inaccessible by biological catalysis.es_ES
dc.description.sponsorshipThis work was funded by the Bundesministerium für Bildung und Forschung (BMBF grant 0315775B PT-J to W.-D.F.) and the Ministerio de Economı́a y Competitividad (MINECO) (grant CTQ2012-31605 to P.C.), within the transnational Eurotrans-Bio framework, as well as by student exchange funds from the DAAD (grant PPP-50749958 to W.-D.F.), Acciones Integradas (MINECO; grant AIB2010DE-00405 to P.C.), and COST action CM1303 Systems Biocatalysis.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Chemical Societyes_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectaldol reactionses_ES
dc.subjectbiocatalysises_ES
dc.subjectcarbohydrateses_ES
dc.subjectmutagenesises_ES
dc.subjectprotein engineeringes_ES
dc.titleMinimalist Protein Engineering of an Aldolase Provokes Unprecedented Substrate Promiscuityes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1021/acscatal.5b02805-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://pubs.acs.org/doi/full/10.1021/acscatal.5b02805es_ES
dc.embargo.terms2017-02-05es_ES
dc.rights.licensehttp://www.sherpa.ac.uk/romeo/issn/2155-5435/es_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.relation.csices_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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