A zinc-containing enzyme found in bacteria, yeasts, plants, and animals that reversibly oxidizes primary and secondary alcohols to the corresponding aldehydes and ketones. In the case of yeast, ADH functions as the last enzyme in alcoholic fermentation. In Drosophila melanogaster, ADH is a dimeric protein. By suitable crosses between null activity mutants it is possible to generate heteroallelic individuals that exhibit partial restoration of enzyme activity. This is often due to the production of a heterodimer with improved functional activity. The gene is of interest to developmental geneticist because its expression is controlled by two promotors. The proximal promotor lies adjacent to the initiation codon and switches the gene on during the larval stage. The distal promotor lies 700 base pairs upstream and controls the production of ADH in the adult. See allelic complementation, promotor.
Subjects: Genetics and Genomics.