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Characterization of Human Alcohol Dehydrogenases Containing Substitutions at Amino Acids 47 and 51

  • Thomas D. Hurley
  • Torsten Ehrig
  • Howard J. Edenberg
  • William F. Bosron
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 284)

Abstract

The kinetic properties of multiple molecular forms of human liver alcohol dehydrogenase (ADH) have been examined in an effort to gain a better understanding of the structure-function relationships of this enzyme, which catalyzes the rate-limiting step during ethanol metabolism in the liver (Ehrig et al., 1990). In order to accomplish this, a system was developed to express the cloned humanβ 1 β 1 enzyme and mutants at specific amino acid positions which were prepared by site-directed mutagenesis in E. coli (Hurley et al., 1990).

Keywords

Ethanol Oxidation Coenzyme Binding Multiple Molecular Form Horse Liver Alcohol Dehydrogenase Angstrom Resolution 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Thomas D. Hurley
    • 1
  • Torsten Ehrig
    • 1
  • Howard J. Edenberg
    • 1
  • William F. Bosron
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyIndiana University School of MedicineIndianapolisUSA

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