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A Single Point Mutation Reverses the Enantiopreference of Thermoanaerobacter ethanolicus Secondary Alcohol Dehydrogenase
Author(s) -
Musa Musa M.,
Lott Nathan,
Laivenieks Maris,
Watanabe Leandra,
Vieille Claire,
Phillips Robert S.
Publication year - 2009
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.200900033
Subject(s) - steric effects , stereospecificity , alcohol dehydrogenase , alcohol , chemistry , stereochemistry , directed evolution , substrate (aquarium) , biochemistry , combinatorial chemistry , biology , mutant , catalysis , gene , ecology
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.