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

Authors

  • Dr. Rachel S. Heath,

    1. School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN (UK), Fax: (+44) 161-275-1311
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  • Dr. Marta Pontini,

    1. School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN (UK), Fax: (+44) 161-275-1311
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  • Dr. Beatrice Bechi,

    1. School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN (UK), Fax: (+44) 161-275-1311
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  • Prof. Nicholas J. Turner

    Corresponding author
    1. School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN (UK), Fax: (+44) 161-275-1311
    • School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN (UK), Fax: (+44) 161-275-1311

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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.

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