A Single Point Mutation Reverses the Enantiopreference of <i>Thermoanaerobacter ethanolicus</i> Secondary Alcohol Dehydrogenase

Abstract

The asymmetric reduction of benzylic and heteroaryl ketones to the corresponding (R)-alcohols using I86A Thermoanaerobacter ethanolicus alcohol dehydrogenase (I86A TeSADH) is described. This single amino acid mutation not only makes the active site of I86A TeSADH able to accommodate more sterically demanding substituents than those accommodated by wild-type TeSADH, but it also reverses the substrate stereospecificity of TeSADH. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.