Article
Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108.
Bioscience, biotechnology, and biochemistry - 1 May 2003
Chinnawirotpisan Piyawan, Matsushita Kazunobu, Toyama Hirohide, Adachi Osao, Limtong Savitree, Theeragool Gunjana
Abstract excerpt
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,...
Topics
- Acetobacter
- Alcohol Dehydrogenase
- Alcohol Oxidoreductases
- Amino Acid Sequence
- Electrophoresis, Polyacrylamide Gel
- Isoenzymes
- Kinetics
- Metals
- Molecular Sequence Data
- Molecular Weight
- Mutation
- NAD
- Substrate Specificity