Abstract
Alcohol dehydrogenases (ADH; E.C. 1.1.1.1), in the presence of nicotamide adenine dinucleotide (NAD), catalyse the reversible oxidation of alcohols to aldehydes and ketones. In the mouse there are three known isozymes of ADH designated as ADH-A2, ADH-B2 and ADH-C2 which are encoded by three distinct structural genes Adh-1, Adh-2 and Adh-3, respectively (Holmes et al, 1981; Holmes, 1977; Holmes, 1978; Holmes, 1979). ADH-A2 is the major liver isozyme and is a class I isozyme (Holmes, 1979). ADH-B2 occurs mostly in the liver and kidney and is a class III isozyme (Algar et al, 1983). ADH-C2 exhibits highest activity in the stomach and cornea and has been designated as a separate class of ADH (Algar et al, 1983), consistent with class IV properties (Parés et al, 1994).
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Downes, J.E., Holmes, R.S. (1995). Purification and Properties of Murine Corneal Alcohol Dehydrogenase. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_42
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_42
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