Evidence for the adaptive significance of enzyme activity levels: interspecific variation in alpha-GPDH and ADH in Drosophila.
The activity levels of alcohol dehydrogenase and alpha-glycerophosphate dehydrogenase were compared among nine species of Drosophila representing three phylogenetic groups. For any given life stage , interspecific variability in activity level was much greater for ADH than for d-GPDH. Patterns of ontogenetic expression of enzyme activity were also much more variable among species for ADH than for alpha-GPDH. These results are consistent with the interpretation that alpha-GPDH is involved with a relatively uniform adaptive function among species, whereas ADH levels may reflect variable adaptive capabilities. There is a significant correlation between ADH activities and survivorship on alcohol-treated media for these nine species.
D000433:1-Propanol / Q000494:pharmacology; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D004330:Drosophila / Q000187:drug effects / Q000201:enzymology; D004331:Drosophila melanogaster / Q000201:enzymology; D014644:Genetic Variation; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism*; D013045:Species Specificity
D000433:1-Propanol; D000429:Alcohol Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase