Biocatalytic Approaches to the Enantiomers of Wieland-Miescher Ketone and its Derivatives

Biocatalytic approaches have been investigated in order to isolate the enantiomers of Wieland-Miescher ketone (1) and of its alcoholic derivatives (cis-2 and trans-3). Specifically, two enzymes from our in-house metagenomic collection of oxidoreductases, IS2-SDR and Dm7 alpha-HSDH, catalyzed the kinetic resolution of the starting racemic ketone 1 or its complete conversion into two diastereomeric products, respectively. Moreover, the kinetic resolution of the racemic cis-alcohol (2) was very efficiently obtained (E approximately equal to 2.000) by lipase PS catalyzed acetylation in dry acetone. All the products were isolated with ee >= 95 %. Simple chemical elaborations of some of them allowed to isolate the missing enantiomers.