Production of (R)-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (LSADH)
2005; Elsevier BV; Volume: 16; Issue: 15 Linguagem: Inglês
10.1016/j.tetasy.2005.06.036
ISSN1362-511X
AutoresKousuke Inoue, Yoshihide Makino, Nobuya Itoh,
Tópico(s)Analytical Chemistry and Chromatography
ResumoAlcohol 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. LSADH was able to efficiently reproduce NADH when 2-propanol was used as a hydrogen donor in the reaction mixture.
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