Issue 20, 2016

Asymmetric reductive amination by a wild-type amine dehydrogenase from the thermophilic bacteria Petrotoga mobilis

Abstract

The biocatalytic reductive amination of ketone to chiral amine is one of the most challenging reactions. Using a genome-mining approach, we found proteins catalyzing the reductive amination of ketones without a carboxylic function in the α or β position. The synthesis of (4S)-4-aminopentanoic acid (ee ≥99.5%) was achieved with the thermoactive amine dehydrogenase (AmDH) AmDH4 from Petrotoga mobilis in 88% yield. The high stability and substrate tolerance make AmDH4 a very good starting point for further discovery of reductive amination biocatalysts with an enlarged substrate range. This is the first report of wild-type enzymes with related genes having proper NAD(P)H–AmDH activity.

Graphical abstract: Asymmetric reductive amination by a wild-type amine dehydrogenase from the thermophilic bacteria Petrotoga mobilis

Supplementary files

Article information

Article type
Paper
Submitted
28 Jul 2016
Accepted
29 Jul 2016
First published
01 Aug 2016

Catal. Sci. Technol., 2016,6, 7421-7428

Asymmetric reductive amination by a wild-type amine dehydrogenase from the thermophilic bacteria Petrotoga mobilis

O. Mayol, S. David, E. Darii, A. Debard, A. Mariage, V. Pellouin, J. Petit, M. Salanoubat, V. de Berardinis, A. Zaparucha and C. Vergne-Vaxelaire, Catal. Sci. Technol., 2016, 6, 7421 DOI: 10.1039/C6CY01625A

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