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dc.contributor.authorGutiérrez, Mariana-
dc.contributor.authorParella, Teodor-
dc.contributor.authorJoglar Tamargo, Jesús-
dc.contributor.authorBujons, Jordi-
dc.contributor.authorClapés Saborit, Pere-
dc.date.accessioned2012-03-20T10:36:04Z-
dc.date.available2012-03-20T10:36:04Z-
dc.date.issued2011-
dc.identifier.citationChemical Communicationses_ES
dc.identifier.issn1359-7345-
dc.identifier.urihttp://hdl.handle.net/10261/47209-
dc.description.abstractStructure-guided re-design of the acceptor binding site of D-fructose-6-phosphate aldolase from E. coli leads to the construction of FSA A129S/A165G double mutant with an activity between 5- to >900-fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives.es_ES
dc.language.isoenges_ES
dc.publisherRoyal Society of Chemistry (UK)es_ES
dc.rightsclosedAccesses_ES
dc.titleStructure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutationes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1039/C1CC11069A-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1039/C1CC11069Aes_ES
dc.identifier.e-issn1364-548X-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.openairetypeartículo-
item.languageiso639-1en-
item.grantfulltextnone-
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