Alcohol dehydrogenase 1A (class I), alpha polypeptide (ADH1A)

Alcohol dehydrogenase 1A (ADH1A) is a key enzyme of the alcohol dehydrogenase family, functioning as the alpha subunit of class I alcohol dehydrogenase, and catalyzing the NAD+-dependent oxidation of alcohols to aldehydes[1][2]. It is highly active in the oxidation of ethanol (major pathway for alcohol catabolism in the liver), as well as in the oxidation of retinol to retinaldehyde (an essential step in vitamin A metabolism)[1]. The gene encoding ADH1A is predominantly expressed in fetal and infant liver and is part of a gene cluster on chromosome 4 that also includes genes encoding the beta and gamma subunits[2]. ADH1A shows high sequence similarity to other class I alcohol dehydrogenases but differs in its substrate specificity and developmental expression. Genetic variation within ADH1A and related genes influences susceptibility to alcohol dependence and certain alcohol-induced diseases such as gastric cancer[1]. Therapeutically, ADH1A is an important molecular target for alcohol poisoning interventions (e.g., inhibition by 4-methylpyrazole) and is implicated in the modulation of neurobehavioral and metabolic responses to alcohol.

Other names

Alcohol dehydrogenase 1AADH1AADH1Alcohol dehydrogenase subunit alphaAlcohol dehydrogenase 1 (class I), alpha polypeptideAldehyde reductaseADH, alpha subunit

Catalyzes the NAD+-dependent oxidation of ethanol and other alcohols to aldehydes 4-methylpyrazole acts as a competitive inhibitor of ADH1A by binding to its active site and blocking the oxidation of alcohol substrates[3]