Abstract
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.
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