Alcohol dehydrogenase enzyme (ADH)

Alcohol dehydrogenase enzyme (ADH) is a family of zinc-dependent oxidoreductase enzymes that catalyze the reversible oxidation of alcohols to aldehydes or ketones using NAD+ as a cofactor[2][3][4][6]. In humans, multiple ADH isoforms (ADH1-ADH7) are expressed, with liver isoforms playing a major role in the detoxification and metabolism of ethanol and other alcohols. ADH enzymes are crucial for physiologically removing toxic alcohols and for generating metabolic intermediates, such as acetaldehyde from ethanol. They are involved in retinol metabolism, neurotransmitter biosynthesis, and many other metabolic pathways. Genetic variants in ADH genes affect the rate of ethanol metabolism and are implicated in disease susceptibility, intoxication risk, and adverse drug reactions[2][3][4]. Drugs such as fomepizole and disulfiram interact with ADH, modulating its activity in clinical treatment of alcohol intoxication and dependence[2][4]. Dysfunction or altered activity of ADH is associated with risk for alcoholism, alcohol-induced organ damage, cancer, and other diseases[3][4].

Other names

Alcohol dehydrogenaseADHethanol dehydrogenasealcohol:NAD+ oxidoreductase

Substrate competition (e.g., ethanol inhibits methanol oxidation via competitive inhibition); Inhibition of enzyme activity (e.g., fomepizole directly inhibits ADH, decreasing metabolism of toxic alcohols); Impaired enzyme function by genetic polymorphisms; Enzyme inhibition (e.g., disulfiram blocks aldehyde dehydrogenase, but also has minor effects on ADH)