TY  - JOUR
  - Paradisi F, Collins S, Maguire AR, Engel PC
  - 2007
  - February
  - Journal of Biotechnology
  - Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives.
  - Validated
  - Altmetric: 1 ()
  - 128
  - 2
  - 408
  - 411
  - Wild-type phenylalanine dehydrogenase from Bacillus sphaericus, and three mutants N145A, N145V and N145L, are used with a coenzyme recycling system to synthesise L-phenylalanine and three non-natural amino acids (p-F-phenylalanine, p-MeO-phenylalanine and p-CF(3)-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF(3)-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.
  - 10.1016/j.jbiotec.2006.08.008
DA  - 2007/02
ER  - 

@article{V5956761,
   = {Paradisi F,  Collins S and  Maguire AR,  Engel PC },
   = {2007},
   = {February},
   = {Journal of Biotechnology},
   = {Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives.},
   = {Validated},
   = {Altmetric: 1 ()},
   = {128},
   = {2},
  pages = {408--411},
   = {{Wild-type phenylalanine dehydrogenase from Bacillus sphaericus, and three mutants N145A, N145V and N145L, are used with a coenzyme recycling system to synthesise L-phenylalanine and three non-natural amino acids (p-F-phenylalanine, p-MeO-phenylalanine and p-CF(3)-phenylalanine) on a millimole scale. A range of reaction conditions are investigated. The kinetic parameters of WT PheDH and N145A towards p-CF(3)-phenylpyruvate are compared, emphasising the value of protein engineering in creating improved biocatalysts.}},
   = {10.1016/j.jbiotec.2006.08.008},
  source = {IRIS}
}