Alcohol dehydrogenase (Drosophila melanogaster) (Adh)

Drosophila alcohol dehydrogenase (Adh) is a vital metabolic enzyme in the fruit fly Drosophila melanogaster, primarily responsible for the oxidation of alcohols to aldehydes and ketones using NAD+ as a cofactor [UniProt: P00334]. It belongs to the short-chain dehydrogenase/reductase (SDR) family and functions as a homodimer essential for the survival of larvae and adults in ethanol-rich environments, such as fermenting fruit [FlyBase: FBgn0000055]. While it is not a therapeutic target for human disease, Adh is one of the most extensively studied proteins in evolutionary biology and population genetics, serving as a primary model for understanding molecular adaptation and enzyme kinetics [PubMed: 6348851]. Research on Adh has provided fundamental insights into how single amino acid substitutions, such as the well-known Fast/Slow polymorphism, affect protein stability and catalytic efficiency under natural selection [PubMed: 16505479]. Although the enzyme can be inhibited by compounds like pyrazole, its significance remains centered on basic biological research and its role as a genetic marker rather than clinical pharmacology [PubMed: 7028476].

Other names

AdhAlcohol dehydrogenase-1ADH-7Drosophila melanogaster alcohol dehydrogenaseADH_DROME

Catalyzes the NAD+-dependent oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones [UniProt: P00334].