Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis

被引:46
作者
Busca, P
Paradisi, F
Moynihan, E
Maguire, AR [1 ]
Engel, PC
机构
[1] Natl Univ Ireland Univ Coll Cork, Dept Chem, Analyt & Biol Chem Res Facil, Cork, Ireland
[2] Natl Univ Ireland Univ Coll Dublin, Dept Biochem, Conway Inst Biomol & Biomed Res, Dublin 4, Ireland
关键词
D O I
10.1039/b406364c
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
The substrate scope of three mutants of phenylalanine dehydrogenase as biocatalysts for the transformation of a series of 2-oxo acids, structurally related to phenylpyruvic acid, to the analogous alpha-amino acids, non-natural analogues of phenylalanine, has been investigated. The mutant enzymes are more tolerant than the wild type enzyme of the non-natural substrates, especially those with substituents at the 4-position on the phenyl ring. Excellent enantiocontrol resulted in all cases.
引用
收藏
页码:2684 / 2691
页数:8
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