Class I fructose-1,6-bisphosphate aldolases as catalysts for asymmetric aldol reactions
1999; Elsevier BV; Volume: 10; Issue: 4 Linguagem: Inglês
10.1016/s0957-4166(99)00044-0
ISSN1362-511X
AutoresRob Schoevaart, Fred van Rantwijk, Roger A. Sheldon,
Tópico(s)Diet, Metabolism, and Disease
ResumoAbstract 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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