Thermophilic archaebacteria have generated considerable interest, owing to their ability  to withstand high temperatures, and often, extremes of pressure, pH and salinity.  Enzymes from these organisms are usually quite robust and may offer particular opportunities for biocatalytic, asymmetric synthesis. We will discuss  the expression and characterization of a DH (dehydrogenase) from Sulfolobus solfataricus (SsADH-10) that selectively reduces the (S)-antipode of alpha-aryl propionaldehydes, leading to alcohols of the important Profen class of NSAIDs.  This presentation will highlight a number of important features of the new process. These include (i) the establishment of efficient DYRKR conditions, leading to high isolated yields; (ii) the use of ethanol as terminal reductant to regenerate nicotinamide cofactor; and (iii) the use of temperature as a �recycling switch.�  This latter �thermal recycling� approach may have broad implications for process chemistry, and argues for more widespread collaboration between synthetic chemists and archaebacterial microbiologists

Use of a robust dehydrogenase from an archaebacterial thermophile in asymmetric synthesis: A dynamic reductive kinetic resolution (DYRKR) entry into (S)-profens

239th National Meeting (2010)

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