Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis.

@article{Seah1995AlterationIR,
  title={Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis.},
  author={Stephen Y. K. Seah and K. Linda Britton and Patrick J Baker and David W. Rice and Yasuhisa Asano and Paul C. Engel},
  journal={FEBS letters},
  year={1995},
  volume={370 1-2},
  pages={93-6}
}
Glycine-124 and leucine-307 of phenylalanine dehydrogenase from Bacillus sphaericus were altered by site-specific mutagenesis to the corresponding residues in leucine dehydrogenase: alanine and valine, respectively. These two residues have previously been implicated from molecular modelling as important in determining the substrate discrimination of the two enzymes. Single and double mutants displayed lower activities towards L-phenylalanine and enhanced activity towards almost all aliphatic… CONTINUE READING

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