Mutations were introduced into the leucine amine dehydrogenase (L-AmDH) derived from G. stearothermophilus leucine dehydrogenase (LeuDH) with the goals of increased activity and expanded substrate acceptance. A triple variant (L-AmDH-TV) including D32A, F101S, and C290V showed an average of 2.5fold higher activity toward aliphatic ketones and an 8.0°C increase in melting temperature. L-AmDH-TV did not show significant changes in relative activity for different substrates. In contrast, L39A, L39G, A112G, and T133G in varied combinations added to L-AmDH-TV changed the shape of the substrate binding pocket. L-AmDH-TV was not active on ketones larger than 2-hexanone. L39A and L39G enabled activity for straightchain ketones as large as 2-decanone and in combination with A112G enabled activity toward longer branched ketones including 5-methyl-2-octanone.[a] R. Scheme 1. Reductive amination of prochiral ketones to form chiral amines with an amine dehydrogenase.
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