Abstract
The structure and mechanism of alcohol dehydrogenases have been extensively studied (Bränden et al., 1975; Klinman, 1981; Pettersson, 1987). The three-dimensional structures of the horse liver enzyme in several ternary complexes have been solved at high resolution (Eklund et al., 1981, 1982). Amino acid sequences for more than 22 NAD+-dependent alcohol dehydrogenases from 11 animal, plant and fungal species are known. Comparison of these sequences raises many questions about the structure-function relationships in these enzymes. How do the amino acid residues at the active site participate in catalysis? What is the basis of substrate specificity? What was selected for during the evolution of the different enzymes?
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© 1990 Plenum Press, New York
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Plapp, B.V. et al. (1990). Catalysis by Yeast Alcohol Dehydrogenase. In: Weiner, H., Wermuth, B., Crabb, D.W. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 3. Advances in Experimental Medicine and Biology, vol 284. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5901-2_26
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DOI: https://doi.org/10.1007/978-1-4684-5901-2_26
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