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Development of an R ‐Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity
Author(s) -
Heath Rachel S.,
Pontini Marta,
Bechi Beatrice,
Turner Nicholas J.
Publication year - 2014
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201301008
Subject(s) - amine oxidase , chemistry , amine gas treating , substrate (aquarium) , yield (engineering) , biocatalysis , catalysis , enantioselective synthesis , combinatorial chemistry , enzyme , organic chemistry , oxidase test , aspergillus niger , stereochemistry , biochemistry , reaction mechanism , materials science , biology , ecology , metallurgy
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 .