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dc.contributor.authorSánchez-Moreno, Israel-
dc.contributor.authorIturrate Montoya, Laura-
dc.contributor.authorDoyagüez, Elisa G.-
dc.contributor.authorMartínez, José Antonio-
dc.contributor.authorFernández-Mayoralas, Alfonso-
dc.contributor.authorGarcía-Junceda, Eduardo-
dc.date.accessioned2010-01-19T16:06:49Z-
dc.date.available2010-01-19T16:06:49Z-
dc.date.issued2009-11-10-
dc.identifier.citationAdvanced Synthesis & Catalysis 351(17): 2967 - 2975(2009)en_US
dc.identifier.issn1615-4150-
dc.identifier.urihttp://hdl.handle.net/10261/20183-
dc.descriptionPublished in: Advanced Synthesis & Catalysis, Volume 351, Issue 17, Date: November 2009, Pages: 2967-2975.en_US
dc.description.abstractThe utility for carbon-carbon bond formation of a multienzyme system composed of recombinant dihydroxyacetone kinase (DHAK) from Citrobacter freundii, the fructose bisphosphate aldolase from rabbit muscle (RAMA) and acetate kinase (AK) for adenosine triphosphate (ATP) regeneration has been studied. Several aldehydes with great structural diversity, including three ,-unsaturated aldehydes, have been analysed as acceptor substrates. It was found that ,-unsaturated aldehydes bearing an electron-withdrawing group in the position to the double bond with a trans configuration are good acceptors for RAMA in this multienzyme system. The aldol reaction proceeds with excellent D-threo enantioselectivity and the aldol adduct is obtained in good overall yield. The L-threo and D-erythro enantiomers are also accessible from rhamnulose 1-phosphate aldolase (Rha-1PA) and fuculose 1-phosphate aldolase (Fuc-1PA) catalysed reactions, respectively.en_US
dc.description.sponsorshipFunded by: Spanish Ministerio de Ciencia e Innovación; Grant Number: CTQ2007-67403/BQU Comunidad de Madriden_US
dc.format.extent373284 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherWiley-VCHen_US
dc.rightsopenAccessen_US
dc.subjectAldol reactionen_US
dc.subjectAldolasesen_US
dc.subjectBiotransformationsen_US
dc.subjectCC bond formationen_US
dc.subjectMultienzyme processesen_US
dc.titleActivated α, β-Unsaturated Aldehydes as Substrate of Dihydroxyacetone Phosphate (DHAP)-Dependent Aldolases in the Context of a Multienzyme Systemen_US
dc.typeArtículoen_US
dc.identifier.doi10.1002/adsc.200900603-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1002/adsc.200900603en_US
dc.identifier.e-issn1615-4169-
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