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).
ChemCatChem (Electronic) – Wiley
Published: Jan 7, 2018
Keywords: ; ; ; ;
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