Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108.

@article{Chinnawirotpisan2003PurificationAC,
  title={Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108.},
  author={Piyawan Chinnawirotpisan and Kazunobu Matsushita and Hirohide Toyama and Osao Adachi and Savitree Limtong and Gunjana Theeragool Theeragool},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2003},
  volume={67 5},
  pages={958-65}
}
High NAD-dependent alcohol dehydrogenase (ADH) activity was found in the cytoplasm when a membrane-bound, quinoprotein, ADH-deficient mutant strain of Acetobacter pasteurianus SKU1108 was grown on ethanol. Two NAD-dependent ADHs were separated and purified from the supernatant fraction of the cells. One (ADH I) is a trimer, consisting of an identical subunit of 42 kDa, while the other (ADH II) is a homodimer, having a subunit of 31 kDa. One of the two ADHs, ADH II, easily lost the activity… CONTINUE READING