Premium
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.