Production of (R)-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (LSADH)
| Autor: | Yoshihide Makino, Kousuke Inoue, Nobuya Itoh |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
chemistry.chemical_classification
biology Hydrogen Stereochemistry Organic Chemistry Hydrogen transfer Substrate (chemistry) chemistry.chemical_element General Medicine Medicinal chemistry Catalysis Inorganic Chemistry Enzyme chemistry Yield (chemistry) biology.protein Moiety Physical and Theoretical Chemistry Enantiomeric excess Alcohol dehydrogenase |
| Zdroj: | Tetrahedron: Asymmetry. 16:2539-2549 |
| ISSN: | 0957-4166 |
| DOI: | 10.1016/j.tetasy.2005.06.036 |
| Popis: | 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. LSADH was able to efficiently reproduce NADH when 2-propanol was used as a hydrogen donor in the reaction mixture. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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