Inside Back Cover: Development of an  R ‐Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity (ChemCatChem 4/2014) | Zendy

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

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Inside Back Cover: Development of an R ‐Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity (ChemCatChem 4/2014)

Author(s) -

Heath Rachel S.,

Pontini Marta,

Bechi Beatrice,

Turner Nicholas J.

Publication year - 2014

Publication title -

chemcatchem

Language(s) - English

Resource type - Reports

SCImago Journal Rank - 1.497

H-Index - 106

eISSN - 1867-3899

pISSN - 1867-3880

DOI - 10.1002/cctc.201490025

Subject(s) - biocatalysis , monoamine oxidase , enantiomer , chemistry , substrate (aquarium) , oxidase test , stereochemistry , monoamine oxidase a , enzyme , combinatorial chemistry , organic chemistry , reaction mechanism , catalysis , biology , ecology

Mirror mirror on the wall After several years of “reflection” on the use of S ‐selective monoamine oxidase (( S )‐MAO‐N) for the deracemization of amines, an R ‐selective biocatalyst has now been developed. In their Full Paper on p. 996 ff., R. S. Heath et al. describe how 6‐hydroxy‐ D ‐nicotine oxidase (( R )‐6‐HDNO) provides a method for preparing the mirror image S enantiomers and thereby constitutes a perfect enantiocomplementary enzyme to ( S )‐MAO‐N.

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