Summary
Alcohol dehydrogenases constitute a complex system of enzymes, classes, isozymes, and allelic variants. The zinc containing, well-known liver enzyme is a class I medium-chain alcohol dehydrogenase. Other classes of this family include the class II protein, the glutathione-dependent formaldehyde dehydrogenase (the class III enzyme), the stomach-expressed class IV form, and the recently defined class V protein. Characterized forms suggest that the glutathione-dependent formaldehyde dehydrogenase is the original ancestor, defining a role for the whole protein family in cellular defense mechanisms. The isozyme-multiple class I protein is derived from an early gene duplication, allowing sub-specialization in vertebrates. Class IV is the one most ethanol-active and appears to be derived from the class I line. Allelic variants within class I, in association with aldehyde dehydrogenase variants, correlate with population differences in ethanol metabolism and hence with susceptibility to develop alcohol-related diseases. The structures also correlate with functional properties and define molecular building units for the whole family.
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© 1994 Birkhäuser Verlag Basel/Switzerland
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Jörnvall, H. (1994). The alcohol dehydrogenase system. In: Jansson, B., Jörnvall, H., Rydberg, U., Terenius, L., Vallee, B.L. (eds) Toward a Molecular Basis of Alcohol Use and Abuse. Experientia, vol 71. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7330-7_22
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DOI: https://doi.org/10.1007/978-3-0348-7330-7_22
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