Development of an<i>R</i>-Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity
作者:Rachel S. Heath、Marta Pontini、Beatrice Bechi、Nicholas J. Turner
DOI:10.1002/cctc.201301008
日期:2014.4
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
胺氧化酶是用于合成对映体纯的1°,2°和3°手性胺的有用生物催化剂。先前报道的此类酶(例如,来自黑曲霉的MAO-N )已显示出高度的S选择性。在此,我们报道了基于6-羟基-D-烟碱氧化酶(6-HDNO)的对映体互补R-选择性胺氧化酶的开发,该酶具有扩大的底物范围和高对映选择性。工程化的6-HDNO酶已应用于一系列外消旋胺的制备脱硝反应,以产生具有S构型的产物,例如高ee的(S)-烟碱。