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Synfacts 2009(9): 1044-1044
DOI: 10.1055/s-0029-1217785
DOI: 10.1055/s-0029-1217785
Organo- and Biocatalysis
© Georg Thieme Verlag
Stuttgart ˙ New York
Enzymatic Control over Self- and Cross-Aldol Reactions
X. Garrabou, J. A. Castillo, C. Guérard-Hélaine, T. Parella, J. Joglar, M. Lemaire, P. Clapés*
Instituto de Química Avanzada de Cataluña-CSIC, Barcelona, Universitat Autònoma de Barcelona, Bellaterra, Spain and Université Blaise Pascal, Aubière, France
Further Information
Publication History
Publication Date:
21 August 2009 (online)
Significance
The enzyme-catalyzed self- and cross-aldol additions of glycolaldehyde (GA) are reported. The investigated enzyme d-fructose-6-phosphate aldolase (FSA) proved to be very effective and able to differentiate carbonyl compounds in its donor and acceptor capabilities. Glycolaldehyde showed the highest donor properties, as illustrated in kinetic studies by its low Michaelis-Menten constant. The K M of glycolaldehyde was even lower than those for dihydroxyacetone and hydroxyacetone, respectively, both known to be well tolerated as donors by the FSA enzyme. Remarkably, even consecutive aldol additions were possible.