초록
<P>Kinetic resolution of chiral amines using <SMALL>L</SMALL>-threonine as a cosubstrate was demonstrated by a biocatalytic strategy in which (<I>S</I>)-selective ω-transaminase (ω-TA) was coupled with threonine deaminase (TD), eliminating the need to use an expensive keto acid as an amino acceptor. The coupled enzyme reaction enabled simultaneous production of enantiopure (<I>R</I>)-amine and <SMALL>L</SMALL>-homoalanine which are pharmaceutically important building blocks. To extend the versatility of this strategy to production of both enantiomers of chiral amines, (<I>R</I>)-selective ω-TA coupled with TD was employed to produce (<I>S</I>)-amine.</P><BR><BR><P>Graphic Abstract</P><P>A coupled enzymatic strategy for simultaneous conversion of racemic amine to enantiopure (<I>R</I>) or (<I>S</I>)-amine and <SMALL>L</SMALL>-threonine to <SMALL>L</SMALL> or <SMALL>D</SMALL>-homoalanine is devised, affording a highly enantioselective kinetic resolution of chiral amines. <SMALL>L</SMALL>-Threonine serves as a substitute for an expensive keto acid, leading to stereoselective synthesis of <SMALL>L</SMALL> or <SMALL>D</SMALL>-homoalanine.<BR><IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2gc35615e'><BR></P>