Abstract
Alcohol dehydrogenase (ADH) catalyses the reversible interconversion of a variety of alcohols and their corresponding aldehydes and ketones, and is widely distributed in organisms. It has been detected in all animals, in plants, and eukaryotic and prokaryotic microorganisms. In vertebrates the ADH system is complex, with at least seven different enzymatic classes (Jörnvall and Höög, 1995, Kedishvili et al., 1997). The study in sub- mammal species is of interest to understand the relationship between the classes found in mammals and the evolutionary origins of the present structures. Moreover, since the enzyme exhibits a wide substrate specificity, the comparative study of the enzymes from distant species may provide valuable information on the function of the enzyme, and how it may change among groups of vertebrates to adapt to different physiological needs.
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Peralba, J.M., Crosas, B., Martinez, S.E., Julià, P., Farrés, J., Parés, X. (1999). Amphibian Alcohol Dehydrogenase. In: Weiner, H., Maser, E., Crabb, D.W., Lindahl, R. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 7. Advances in Experimental Medicine and Biology, vol 463. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4735-8_42
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DOI: https://doi.org/10.1007/978-1-4615-4735-8_42
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