Deracemization of Phenyl‐Substituted 2‐Methyl‐1,2,3,4‐Tetrahydroquinolines by a Recombinant Monoamine Oxidase from Pseudomonas monteilii ZMU‐T01

Abstract A monoamine oxidase (MAO5) from Pseudomonas monteilii ZMU‐T01 was first heterologously expressed in Escherichia coli BL21(DE3) and then used as a biocatalyst for the deracemization of racemic 2‐methyl‐1,2,3,4‐tetrahdroquinoline derivatives to yield the unreacted R enantiomer with up to >99 % ee . Sequence alignment revealed that MAO5 shared 14.7 % identity toward the well‐studied monoamine oxidase (MAO‐N).