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

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. Nicotine rush: An R‐selective amine oxidase based on 6‐hydroxy‐D‐nicotine oxidase (6‐HDNO) with broadened substrate scope and high enantioselectivity has been developed. The engineered 6‐HDNO enzyme is applied to the preparative deracemization of a range of racemic amines to yield S‐configured products, for example, (S)‐nicotine, in high ee.