ADH1C is a protein-coding gene that produces a single polypeptide chain containing 399 amino acids, with a molecular mass of approximately 42.4 kDa . The enzyme is characterized by its high activity for ethanol oxidation, converting ethanol to acetaldehyde, which is a key step in ethanol catabolism . This process is essential for the body’s ability to metabolize and eliminate alcohol.
The enzyme exists as several homo- and heterodimers of alpha, beta, and gamma subunits. The gamma subunit, encoded by the ADH1C gene, is one of these subunits and is known for its high activity in ethanol oxidation . The genes encoding the alpha, beta, and gamma subunits are organized in a genomic segment as a gene cluster .
Human recombinant ADH1C is produced using Escherichia coli (E. coli) expression systems. The recombinant enzyme is typically fused to a His-tag at the N-terminus to facilitate purification through chromatographic techniques . This recombinant form is used in various research and industrial applications to study the enzyme’s properties and its role in alcohol metabolism.
ADH1C has been studied extensively for its role in alcohol metabolism and its association with alcohol dependence and other diseases. While an association between ADH1C polymorphism and alcohol dependence has not been firmly established, the enzyme’s activity in ethanol oxidation makes it a significant focus of research in understanding alcohol-related disorders .
Additionally, ADH1C is involved in other metabolic pathways, such as the oxidation of retinol and the metabolism of retinoic acid, which are important for various physiological processes . The enzyme’s role in these pathways highlights its broader significance beyond alcohol metabolism.