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KMID : 0624219950030000026
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Focus on Genetic Science
1995 Volume.3 No. 0 p.26 ~ p.38
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The Human Alcohol Dehydrogenase System
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Hur Man-Wook
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Abstract
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Our current understanding on the alcohol dehydrogenases system in-creased enormously over the decade. It is the most extensively and thoroughly studied protein at the molecular biological and biochemical level in many species. The structures of human ADH enzymes, cDNAs, and genes have all been determined. The structures have been correlated with catalytic properties of the enzymes. The functions of alcohol dehydrogenase are diverse. 1) Alcohol dehydrogenase participates in the reversible oxidoreduction of alcohols and aldehydes. Class I liver ADH is the most active enzyme in the elimination of ethanol. Medium to long carbon chain alcohols or aldehydes are much better substrates than ethanol for any alcohol dehydrogenases. 2) Alcohol dehydrogenase (class III) participates in cellular detoxification by removing formaldehyde 3) Alcohol dehydrogenases (class W and class I) are important in the growth and development of vertebrate by participating in the homeostasis of retinoic acid.
There are remarkable differences between ADH isozymes and has explained the molecular basis for the genetic and racial differences in alcohol metabolism. Such genetic variability in ADH genotypes, along with genetic variability of ALDH, may well explain the genetic predispositions that lead to alcoholism and alcohol related diseases.
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