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.

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Biochemical syntheses O 0035Enantioselective Synthesis of Non-Natural Amino Acids Using Phenylalanine Dehydrogenases Modified by Site-Directed Mutagenesis. -Mutants of phenylalanine dehydrogenase are investigated as biocatalysts for the transformation of 2-oxo acids, (I)-(IV), to the corresponding α-amino acids. The enzymes are more tolerant towards the non-natural substrates than the wild type enzyme. -(BUSCA, P.; PARADISI, F.; MOYNIHAN, E.; MAGUIRE*, A. R.; ENGEL, P. C.; Org. Biomol. Chem. 2 (2004) 18, 2684-2691; Dep. Chem. Anal., Univ. Coll., Cork, Ire.; Eng.) -Nuesgen 02-029

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