Publisher: American Chemical Society (ACS)

Issue: 12

License:

Publication date(s): 2019/12/06 (print) 2019/11/18 (online)

Pages: 11813-11818

Volume: 9 Issue: 12

Journal: ACS Catalysis

Link: [{"URL"=>"https://pubs.acs.org/doi/pdf/10.1021/acscatal.9b03889", "content-type"=>"unspecified", "content-version"=>"vor", "intended-application"=>"similarity-checking"}]

URL: http://dx.doi.org/10.1021/acscatal.9b03889

Chiral vicinal amino alcohols are an important motif found in many biologically active molecules. In this study, biocatalytic reductive amination of α-hydroxy ketones with ammonia was investigated using engineered amine dehydrogenases (AmDHs) derived from the leucine amino acid dehydrogenase (AADH) from Lysinibacillus fusiformis. The AmDHs thus identified enabled the synthesis of (S)-configured vicinal amino alcohols from the corresponding α-hydroxy ketones in up to 99% conversions and >99% ee. One of the AmDH variants was used to prepare a key intermediate for the antituberculosis pharmaceutical ethambutol.