Characterization of Human Alcohol Dehydrogenases Containing Substitutions at Amino Acids 47 and 51
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).
KeywordsEthanol Oxidation Coenzyme Binding Multiple Molecular Form Horse Liver Alcohol Dehydrogenase Angstrom Resolution
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- Hurley, T. D., Edenberg, H. J., and Bosron, W. F., 1990, Expression and Kinetic Characterization of Variants of Human ß1ß1 Alcohol Dehydrogenase Containing Substitutions at Position 47. J. Biol. Chem., in press., 1990.Google Scholar