期刊
CHEMCATCHEM
卷 7, 期 5, 页码 757-760出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201403010
关键词
amine transaminase; biocatalysis; protein engineering; substrate scope
资金
- Fonds der Chemischen Industrie
- European Union ithin the European Union Seventh Framework Programme [KBBE-2011-5, 289350]
Although the amine transaminase from Vibrio fluvialis has often been applied as a catalyst for the biocatalytic preparation of various chiral primary amines, it is not suitable for the transamination of a-hydroxy ketones and aryl-alkyl ketones bearing an alkyl substituent larger than a methyl group. We addressed this problem through a systematic mutagenesis study of active site residues to expand its substrate scope towards two bulky ketones. We identified two mutants (F85L/V153A and Y150F/V153A) showing 30-fold increased activity in the conversion of (S)-phenylbutylamine and (R)-phenylglycinol, respectively. Notably, they facilitated asymmetric synthesis of these amines with excellent enantiomeric purities of 98% ee.
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