How the α-substititionof substrate affects the specific activity and stereoselectivity of carbonyl reductase

Conference Dates

September 24-28, 2017


In asymmetric catalysis, the enantioselectivity of the reaction product is generally controlled by steric repulsion between asymmetric catalyst and substrate. This is also happened when enzyme as the asymmetric catalyst. But steric repulsion wasn’t the sole factor effected on the enzyme activity. The electronic effect of amino acids in or near the enzymatic activity center which interact with substrate can play an important role in this phenomenon.

Stereoselective reduction of aromatic ketones with α-halo groups are of particular interest, since the corresponding chiral halohydrins (β-halo alcohols) are key-intermediates in the synthesis of a number of biologically active compounds. For the mono- or multi- halomethyl ketones as the substrates, the increased electrophilicity of the carbonyl carbon compensates for the lower Lewis basicity and greater steric shielding of the carbonyl oxygen[1].

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