Alcohol-oxidizing enzymes in 13 Drosophila species.
Starch and polyacrylamide gel electrophoresis were used to ascertain the substrate specificities of alcohol-oxidizing enzymes in 13 Drosophila species. The substrates used were a variety of long- and short-chain aliphatic alcohols, one aromatic alcohol, and benzaldehyde. Only one enzyme (product of a single-gene locus) showed significant NAD+-dependent alcohol dehydrogenase activity with short-chain aliphatic alcohols. The 13 species, belonging to four different Drosophila groups, all showed a similar complement of alcohol-oxidizing enzymes, although differences in electrophoretic mobility and in levels of activity existed from species to species. These findings are relevant to the adaptation of Drosophila to alcohol environments.
D000429:Alcohol Oxidoreductases / Q000235:genetics*; D000818:Animals; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics; D004331:Drosophila melanogaster / Q000201:enzymology; D005260:Female; D007814:Larva; D008297:Male; D010084:Oxidation-Reduction; D013045:Species Specificity; D013379:Substrate Specificity
D000429:Alcohol Oxidoreductases