sn-Glycerol-3-phosphate oxidase and alcohol tolerance in Drosophila melanogaster larvae.
The role of sn-glycerol-3-phosphate oxidase (GPO; EC 1.1.99.5) in the variation of ethanol tolerance in Drosophila melanogaster was assessed in isofemale lines derived from individuals collected at the Chateau Tahbilk Winery and Wandin North Orchard of Victoria, Australia. When fed an undefined medium (semolina-treacle) with 6% ethanol (v/v), larvae of lines with high GPO activities survived better than did larvae of lines with low GPO activities. Although GPO was induced to higher activity levels by dietary ethanol in larvae of all the test lines, GPO activity was greater in lines representing the area outside the wine cellar. This implied that the cellar environment selected against individuals with high levels of GPO. These data do not explain the established difference in tolerance between cellar and outside populations. The GPO activities of lines were not dependent upon the activities of the lipogenic enzyme, glycerol-3-phosphate dehydrogenase; the major ethanol-degrading enzyme, alcohol dehydrogenase; or the citric acid cycle enzyme, fumarase. Thus, GPO activity is an important component of the metabolic mechanism of ethanol tolerance in larvae, but the mode of action of GPO has not been defined.
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology / Q000378:metabolism*; D004361:Drug Tolerance; D000431:Ethanol / Q000378:metabolism*; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism*; D007814:Larva
D000431:Ethanol; D005993:Glycerolphosphate Dehydrogenase; D000426:Alcohol Dehydrogenase; C036140:L-alpha-glycerol-phosphate oxidase