The alcohol dehydrogenase system.
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.
Jörnvall
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Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
D000426:Alcohol Dehydrogenase / Q000145:classification / Q000235:genetics* / Q000378:metabolism*; D000428:Alcohol Drinking / Q000235:genetics* / Q000378:metabolism; D000437:Alcoholism / Q000201:enzymology / Q000235:genetics*; D000818:Animals; D005075:Biological Evolution; D006801:Humans; D007527:Isoenzymes / Q000145:classification / Q000235:genetics / Q000378:metabolism; D008322:Mammals; D005810:Multigene Family
D007527:Isoenzymes; D000426:Alcohol Dehydrogenase