The angle of a side-chain decides regio- and enantioselectivity in Alcohol Dehydrogenase A

Conference Dates

September 24-28, 2017


Alcohol dehydrogenase A (ADH-A) from Rhodococcus ruber DSM 44541 is a promising biocatalyst for asymmetric synthesis of organic compounds.1 This enzyme is capable of catalyzing enantio- and regioselectivity of phenyl-substitute a-hydroxy ketones (acyloins), which are precursors for the synthesis of a range of biologically active compounds.1,2 ADH-A catalyzes the oxidation of (S)-1-phenylethanol 3000-fold more efficiently as compared to the 2-hydroxylated derivatives (R)-phenyl-1,2-ethanediol. ADH-A is highly selective towards secondary-alcohols and displays very low activities with corresponding primary-alcohol derivatives.2,3 Apparently, when this selectivity was tested with substrate contained two secondary-alcohols, we analyzed the catalytic efficiency and the regioselectivity towards (1R,2S)-2.2 The conclusions were yielded that ADH-A is a comparably inefficient catalyst for oxidation of vicinal diols, but displays regioselectivity, oxidizing primarily the benzylic carbon of this substrate.2

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