Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus.

@article{Sakuraba2001PurificationCA,
  title={Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus.},
  author={Haruhiko Sakuraba and Yuichiro Takamatsu and Takenori Satomura and Ryushi Kawakami and Toshihisa Ohshima},
  journal={Applied and environmental microbiology},
  year={2001},
  volume={67 4},
  pages={1470-5}
}
The distribution of dye-linked L-amino acid dehydrogenases was investigated in several hyperthermophiles, and the activity of dye-linked L-proline dehydrogenase (dye-L-proDH, L-proline:acceptor oxidoreductase) was found in the crude extract of some Thermococcales strains. The enzyme was purified to homogeneity from a hyperthermophilic archaeon, Thermococcus profundus DSM 9503, which exhibited the highest specific activity in the crude extract. The molecular mass of the enzyme was about 160 kDa… CONTINUE READING

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