Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.

@article{Tsigos1998PurificationAC,
  title={Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.},
  author={Iason Tsigos and K Velonia and Ioulia Smonou and Vassilis Bouriotis},
  journal={European journal of biochemistry},
  year={1998},
  volume={254 2},
  pages={356-62}
}
An NAD+-dependent alcohol dehydrogenase (ADH) of the Antarctic psychrophile Moraxella sp. TAE123 was purified to homogeneity with an overall yield of 16.7% and further characterized. The native enzyme had an apparent molecular mass of 240 kDa and consisted of four identical 52-kDa subunits. The pI of the enzyme was determined to be 5.5, while its optimum pH is 7.5. The enzyme contained 1 zinc atom/subunit and exhibited a remarkable thermal lability. Moraxella sp. TAE123 ADH exhibited a wide… CONTINUE READING
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