IRIS publication 5956774
Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis.
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TY - JOUR - Busca P, Paradisi F, Moynihan E, Maguire AR, Engel PC - 2004 - September - Organic and Biomolecular Chemistry - Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis. - Validated - Altmetric: 1 () - 2 - 18 - 2684 - 2691 - 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. - 10.1039/B406364C DA - 2004/09 ER -
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@article{V5956774, = {Busca P, Paradisi F and Moynihan E, Maguire AR and Engel PC }, = {2004}, = {September}, = {Organic and Biomolecular Chemistry}, = {Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis.}, = {Validated}, = {Altmetric: 1 ()}, = {2}, = {18}, pages = {2684--2691}, = {{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.}}, = {10.1039/B406364C}, source = {IRIS} }
Data as stored in IRIS
AUTHORS | Busca P, Paradisi F, Moynihan E, Maguire AR, Engel PC | ||
YEAR | 2004 | ||
MONTH | September | ||
JOURNAL_CODE | Organic and Biomolecular Chemistry | ||
TITLE | Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis. | ||
STATUS | Validated | ||
TIMES_CITED | Altmetric: 1 () | ||
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VOLUME | 2 | ||
ISSUE | 18 | ||
START_PAGE | 2684 | ||
END_PAGE | 2691 | ||
ABSTRACT | 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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DOI_LINK | 10.1039/B406364C | ||
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