Identification, characterization and application of M16AT, a new organic solvent–tolerant (R)–enantio–selective type IV amine transaminase from Mycobacterium sp. ACS1612

Biocatalysis has emerged as a powerful alternative to traditional chemical methods, especially for asymmetric synthesis. As biocatalysts usually exhibit excellent chemical, regio‐ and enantioselectivity, they facilitate and simplify many chemical processes for the production of a broad range of products. Here, a new biocatalyst called, R ‐selective amine transaminases ( R ‐ATAs), was obtained from Mycobacterium sp. ACS1612 (M16AT) using in–silico prediction combined with a genome and protein database. A two–step simple purification process could yield a high concentration of pure enzyme, suggesting that industrial application would be inexpensive. Additionally, the newly identified and characterized R ‐ATAs displayed a broad substrate spectrum and strong tolerance to organic solvents. Moreover, the synthetic applicability of M16AT has been demonstrated by the asymmetric synthesis of ( R )‐fendiline from of ( R )‐1‐phenylethan‐1‐amine.