ECI Digital Archives

Title

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

Authors

Thilak Reddy Enugala, Uppsala University, SwedenFollow
Emil Hamnevik, Uppsala University, Sweden
Dirk Maurer, Uppsala University, Sweden
Heidi Hillier, Uppsala University, Sweden
Doreen Dobritzsch, Uppsala University, Sweden
Mikael Widersten, Uppsala University, Sweden

Conference Dates

September 24-28, 2017

Abstract

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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Recommended Citation

Thilak Reddy Enugala, Emil Hamnevik, Dirk Maurer, Heidi Hillier, Doreen Dobritzsch, and Mikael Widersten, "The angle of a side-chain decides regio- and enantioselectivity in Alcohol Dehydrogenase A" in "Enzyme Engineering XXIV", Pierre Monsan, Toulouse White Biotechnology, France Magali Remaud-Simeon, LISBP-INSA, University of Toulouse, France Eds, ECI Symposium Series, (2017). https://dc.engconfintl.org/enzyme_xxiv/29