Development of an  R ‐Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity | Zendy

Heath Rachel S. | Zendy; Pontini Marta | Zendy; Bechi Beatrice | Zendy; Turner Nicholas J. | Zendy

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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 .

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