Development of an R- Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity
Development of an R- Selective Amine Oxidase with Broad Substrate Specificity and High Enantioselectivity
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DOI：
10.1002/cctc.201301008
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发表时间：
2014-04-01
期刊：
影响因子：
4.5
通讯作者：
Turner, Nicholas J.
中科院分区：
文献类型：
--
作者：
Heath, Rachel S.;Pontini, Marta;Turner, Nicholas J.
胺氧化酶是合成对映异构纯1度、2度和3度手性胺的有效生物催化剂。这类酶（例如来自黑曲霉的MAO-N）以前报道过具有很高的S选择性。本文报道了一种基于6-羟基- d -尼古丁氧化酶（6-HDNO）的对映互补r -选择性胺氧化酶的开发，该酶具有宽底物范围和高对映选择性。该工程6-HDNO酶已被应用于一系列外消旋胺的制备脱去，以产生高ee的S构型产品，例如(S)-尼古丁。
Amine oxidases are useful bio-catalysts for the synthesis of enantiomerically pure 1 degrees, 2 degrees and 3 degrees 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.