The inactivation of saccharopine dehydrogenase (L-lysine-forming) by diethyl pyrocarbonate.

@article{Fujioka1980TheIO,
  title={The inactivation of saccharopine dehydrogenase (L-lysine-forming) by diethyl pyrocarbonate.},
  author={Motoji Fujioka and Yoshimi Takata and Hirofumi Ogawa and Mitsuhiro Okamoto},
  journal={The Journal of biological chemistry},
  year={1980},
  volume={255 3},
  pages={937-42}
}
Saccharopine dehydrogenase (epsilon-N-(L-glutaryl-2)-L-lysine: NAD oxidoreductase (L-lysine-forming) EC 1.5.1.7) from baker's yeast is inactivated by diethyl pyrocarbonate. Spectrophotometric studies show that the inactivation results from the modification of 3 histidyl residues/molecule of enzyme. The sulfhydryl content of the enzyme is unchanged by modification. The reversibility of inactivation by hydroxylamine and the pH dependence of inactivation are also consistent with the inactivation… CONTINUE READING