Development of an R‐Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity

Abstract Amine oxidases are useful bio‐catalysts for the synthesis of enantiomerically pure 1°, 2° and 3° chiral amines. Enzymes in this class (e.g., MAO‐N from Aspergillus niger ) reported previously have been shown to be highly S selective. Herein we report the development of an enantiocomplementary R ‐selective amine oxidase based on 6‐hydroxy‐ D ‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity. The engineered 6‐HDNO enzyme has been applied to the preparative deracemisation of a range of racemic amines to yield S ‐configured products, for example, ( S )‐nicotine, in high ee .