Production of (R)-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (LSADH)
K Inoue, Y Makino, N Itoh
Index: Inoue, Kousuke; Makino, Yoshihide; Itoh, Nobuya Tetrahedron Asymmetry, 2005 , vol. 16, # 15 p. 2539 - 2549
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Citation Number: 92
Abstract
Alcohol dehydrogenase (LSADH) isolated from Leifsonia sp. S749 was used to produce (R)- chiral alcohols. The enzyme with a broad substrate range reduced various prochiral ketones and keto esters to yield optically active secondary alcohols with a high enantiomeric excess. LSADH transferred the pro-S hydrogen of NADH to the carbonyl moiety of phenyl trifluoromethyl ketone 13 through its re face to give (S)-1-phenyl-2, 2, 2-trifluoroethanol 40. ...
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