Class I fructose-1,6-bisphosphate aldolases as catalysts for asymmetric aldol reactions |
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| Institution: | 1. University of York, Department of Chemistry, Green Chemistry Centre of Excellence, York, United Kingdom;2. University of Trieste, Department of Chemical and Pharmaceutical Sciences, Trieste, Italy;1. School of Life Sciences, Northwestern Polytechnical University, 710072 Xi''an, China;2. Research & Development Institute of Northwestern Polytechnical University in Shenzhen, 518057 Shenzhen, China;3. School of Marine and Bioengineering, Yancheng Institute of Technology, 224051 Yancheng, China |
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| Abstract: | The activity of two commercially available bacterial class I fructose-1,6-bisphosphate aldolases (FruA) towards a number of aldehydes has been compared with rabbit muscle aldolase (RAMA), which is the most widely used enzyme for aldol reactions with dihydroxyacetone phosphate. The kinetic properties of the three aldolases are very similar, but the bacterial aldolases were much more stable than RAMA. Reaction of butanal and dihydroxyacetone phosphate catalyzed by FruA from Staphylococcus carnosus was performed on a 5 mmol scale in 53% isolated yield. Enantiomeric and diastereomeric purity of the major reaction product 90% (3S,4R)] was determined by chiral gas chromatography. |
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