Metabolism and Metabolic Actions of Ethanol

  • Charles S. Lieber


According to prevailing concepts, the rate-limiting factor in the metabolism of ethanol by the alcohol dehydrogenase (ADH) pathway is the capacity of the liver to reoxidize the NADH produced from the reduction of NAD by the hydrogen from the ethanol rather than the activity of ADH itself. It appears now, however, that ADH is not necessarily present in excess, and that under a variety of circumstances, it is the level of the enzyme itself that actually becomes rate-limiting (Crow et al., 1977). The concept that rates of ethanol metabolism may be determined by the level of ADH activity has been the subject of controversy for many years and has attracted more recent attention because ADH was found to be heterogeneous, and several isoenzymes have been described in human liver (Schenker et al., 1971; Hetruszko et al., 1972; Smith et al., 1971, 1972; Li and Magnes, 1975). In addition, an atypical ADH was isolated (von Wartburg et al., 1965) that, in vitro, has a much higher activity at physiologic pH than does the normal variety. Although those individuals with “atypical” ADH have enzyme activities several times higher than normal in vitro, this is not accompanied by an acceleration of the metabolism of ethanol in vivo (Edwards and Price Evans, 1967).


Retina Pyruvate Folic Acid Cyanide Fructose 
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© Plenum Publishing Corporation 1978

Authors and Affiliations

  • Charles S. Lieber
    • 1
    • 2
  1. 1.Section and Laboratory of Liver Disease, Nutrition and AlcoholismVeterans Administration HospitalBronxUSA
  2. 2.Mount Sinai School of Medicine (CUNY)New YorkUSA

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