English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/20183
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Activated α, β-Unsaturated Aldehydes as Substrate of Dihydroxyacetone Phosphate (DHAP)-Dependent Aldolases in the Context of a Multienzyme System

AuthorsSánchez-Moreno, Israel ; Iturrate Montoya, Laura; Doyagüez, Elisa G.; Martínez, José Antonio; Fernández-Mayoralas, Alfonso ; García-Junceda, Eduardo
KeywordsAldol reaction
CC bond formation
Multienzyme processes
Issue Date10-Nov-2009
CitationAdvanced Synthesis & Catalysis 351(17): 2967 - 2975(2009)
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.
DescriptionPublished in: Advanced Synthesis & Catalysis, Volume 351, Issue 17, Date: November 2009, Pages: 2967-2975.
Publisher version (URL)http://dx.doi.org/10.1002/adsc.200900603
Appears in Collections:(IQOG) Artículos
Files in This Item:
File Description SizeFormat 
Unsaturated Aldehydes.pdf364,54 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.