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Supporting Information for this article can be foundu nder: http://dx.Figure 3. Asymmetric reduction of 2,2,2-trifluoroacetophenone(1h)with ah igh substrate loading by recombinant E. coli whole cells expressingwildtype (WT) EbSDR8 and its double variant G94A/S153L. Experimentsw ere performedi ntriplicate and mean values are presented.

The structure-guided rational design of an NADH-dependent short-chain dehydrogenase/reductase (SDR) reversed the stereoselectivity towards halogenated acetophenones from Prelog to anti-Prelog. The enzyme-substrate interactions involving an aromatic ring and a halogen atom were proven to play critical roles in determining the stereoselectivity of these ketone reductions besides the steric repulsion.