Alcohol dehydrogenase from Leuconostoc mesenteroides: molecular properties in comparison with the yeast and horse liver enzyme.

@article{SchneiderBernlhr1981AlcoholDF,
  title={Alcohol dehydrogenase from Leuconostoc mesenteroides: molecular properties in comparison with the yeast and horse liver enzyme.},
  author={Helga Schneider-Bernl{\"o}hr and Heinrich Fiedler and Matthias Gerber and Christoph Friedrich Weber and Michael Zeppezauer},
  journal={The International journal of biochemistry},
  year={1981},
  volume={13 12},
  pages={
          1215-24
        }
}
Abstract 1. 1. Leuconostoc mesenteroides alcohol dehydrogenase is an acidic protein (pI =4.1) with a mol wt of 135,000 consisting of 4 identical subunits. 2. 2. It contains 2 Zn atoms and 5 cysteine residues per subunit. 3. 3. Thermal stability increases with increasing ionic strength. 4. 4. One NADPH molecule is bound per subunit. NADPH is bound about 10 times more strongly than NADH. Fluorescence spectra of bound coenzymes show characteristic blue shifts and intensity enhancements compared to… CONTINUE READING

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