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

Typeset version

 

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
  - ()
  - 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  - 
@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},
   = {()},
   = {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}
}
AUTHORSBusca P, Paradisi F, Moynihan E, Maguire AR, Engel PC
YEAR2004
MONTHSeptember
JOURNAL_CODEOrganic and Biomolecular Chemistry
TITLEEnantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis.
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORD
VOLUME2
ISSUE18
START_PAGE2684
END_PAGE2691
ABSTRACTThe 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.
PUBLISHER_LOCATION
ISBN_ISSN
EDITION
URL
DOI_LINK10.1039/B406364C
FUNDING_BODY
GRANT_DETAILS