title: Facile enzymatic aldol reactions with dihydroxyacetone in the presence of arsenate.
abstract: Aldol reactions of in situ formed dihydroxyacetone arsenate with different aldehydes were catalyzed by bacterial D-fructose-1,6-bisphosphate aldolase (FruA). Aldolases from bacteria were found to be much more stable and active than FruA from rabbit muscle. Arsenate acts as a phosphate mimic and can, in principle, be used in catalytic amounts. The use of inorganic arsenate and dihydroxyacetone afforded high yields with hydrophobic aldehydes. Cosolvents increased the solubility of hydrophobic aldehydes and afforded higher reaction rates and enzyme stability. Insight is given, for the first time, in the influence of arsenate on the stereoselectivity of the aldol reaction.
authors: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands.
authors: R
authors: R
authors: Schoevaart
authors: F
authors: F
authors: van Rantwijk
authors: R A
authors: RA
authors: Sheldon
mesh_terms: D001149:Arsenates / Q000737:chemistry*; D001426:Bacterial Proteins; D004098:Dihydroxyacetone / Q000737:chemistry*; D008968:Molecular Conformation; D013210:Staphylococcus / Q000201:enzymology; D013379:Substrate Specificity; D014157:Transcription Factors / Q000378:metabolism*
chemical_list: D001149:Arsenates; D001426:Bacterial Proteins; C104848:FruA protein, Myxococcus xanthus; D014157:Transcription Factors; C025657:arsenic acid; D004098:Dihydroxyacetone