Alcohol dehydrogenase 1A (ADH1A) (ADH1A)

Alcohol dehydrogenase 1A (ADH1A) is a member of the class I alcohol dehydrogenase family, specifically representing the alpha subunit that forms the alpha-alpha homodimer isoform [1, 7, 8]. This zinc-dependent enzyme is primarily located in the liver and is responsible for the NAD+-dependent oxidation of ethanol and other primary and secondary alcohols into their corresponding aldehydes [6, 11]. Beyond ethanol metabolism, ADH1A plays a vital role in vitamin A homeostasis by catalyzing the conversion of retinol to retinaldehyde, a rate-limiting step in the synthesis of retinoic acid, which regulates cellular differentiation and development [2, 4]. Clinically, ADH1A is a therapeutic target for fomepizole, a competitive inhibitor used as an antidote for methanol and ethylene glycol poisoning to prevent the formation of toxic metabolites like formaldehyde and glycolic acid [12, 14]. Genetic polymorphisms in the ADH1A gene are associated with susceptibility to alcohol dependence and have been implicated in the progression of various cancers, including breast and gastric cancer [3, 5, 10]. In oncology, ADH1A expression levels serve as a prognostic biomarker, where higher levels are often correlated with improved survival and reduced tumor aggressiveness [4].

Other names

Alcohol dehydrogenase subunit alphaADH1Class I alcohol dehydrogenase alpha subunitAlcohol dehydrogenase 1A (class I), alpha polypeptideAldehyde reductase

Competitive inhibition of alcohol dehydrogenase (for inhibitors like fomepizole); NAD+-dependent oxidation of alcohols to aldehydes (enzymatic activity)