Alcohol dehydrogenase 1B (ADH1B) (ADH1B)

Alcohol dehydrogenase 1B (ADH1B) is a critical enzyme in the Class I alcohol dehydrogenase family, primarily localized in the liver where it catalyzes the rate-limiting step of ethanol metabolism: the oxidation of ethanol to acetaldehyde [1, 2]. The "beta 1" designation refers to the specific subunit encoded by the ADH1B*1 allele, which is part of a polymorphic system including beta 2 and beta 3 variants that significantly influence metabolic efficiency [1, 4]. Beyond its role in processing dietary alcohol, ADH1B is involved in the metabolism of retinol to retinaldehyde and the breakdown of various aliphatic alcohols and lipid peroxidation products [1, 2]. Clinically, ADH1B is a therapeutic target for the drug fomepizole, which acts as a competitive inhibitor to treat toxic alcohol ingestions, such as methanol or ethylene glycol, by halting their conversion into highly toxic acids [3]. Genetic variations in this target are major determinants of susceptibility to alcohol use disorder and associated pathologies, including esophageal and head and neck cancers, due to the differential accumulation of acetaldehyde [4, 5]. Understanding the activity of the beta 1 subunit is essential for assessing metabolic capacity and potential toxicological risks in diverse patient populations [5].

Other names

ADH2Alcohol dehydrogenase beta subunitAlcohol dehydrogenase 1B (class I), beta polypeptideHsADH beta 1Alcohol dehydrogenase 1B beta 1 subunit

Competitive inhibition of the enzyme's active site to prevent the oxidation of alcohols into toxic aldehydes and organic acids.