Tailoring D‐Amino Acid Oxidase from the Pig Kidney to R‐Stereoselective Amine Oxidase and its Use in the Deracemization of α‐Methylbenzylamine1. (18th March 2014)

• Record Type: Journal Article
• Authors: Yasukawa, Kazuyuki; Nakano, Shogo; Asano, Yasuhisa
• Is Part Of: Angewandte Chemie. Volume 126:Number 17(2014)
• Page Start: 4517
• Page End: 4520
• Publication Date: 2014-03-18
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.201308812
• Languages: English
• ISSNs: 0044-8249

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>The deracemization of racemic amines to yield enantioenriched amines using S‐stereoselective amine oxidases (AOx) has recently been attracting attention. However, <italic>R</italic>‐stereoselective AOx that are suitable for deracemization have not yet been identified. An <italic>R</italic>‐stereoselective AOx was now evolved from porcine kidney <sc>D</sc>‐amino acid oxidase (pkDAO) and subsequently use for the deracemization of racemic amines. The engineered pkDAO, which was obtained by directed evolution, displayed a markedly changed substrate specificity towards <italic>R</italic> amines. The mutant enzyme exhibited a high preference towards the substrate α‐methylbenzylamine and was used to synthesize the <italic>S</italic> amine through deracemization. The findings of this study indicate that further investigations on the structure–activity relationship of AOx are warranted and also provide a new method for biotransformations in organic synthesis.</p> </abstract>