A NADH-dependent engineered amine dehydrogenase from Geobacillus stearothermophilus (LE-AmDH-v1) was applied together with a NADH-oxidase from Streptococcus mutans (NOx) for the kinetic resolution of pharmaceutically relevant racemic α-chiral primary amines. The reaction conditions (e. g., pH, temperature, type of buffer) were optimised to yield S-configured amines with up to >99 % ee.
Keywords: amine dehydrogenases; biocatalysis; kinetic resolution; oxidative deamination; α-chiral amines.
© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.