The involvement of catalase in alcohol metabolism in Drosophila melanogaster larvae.
The involvement of catalase (H2O2:H2O2 oxidoreductase, EC 1.11.1.6) in the metabolism of alcohols was investigated by comparing Drosophila melanogaster larvae in which catalase was inhibited by dietary 3-amino-1,2,4-triazole (3AT) to larvae fed a diet without 3AT. 3AT inhibited up to 80% of the catalase activity with concordant small increases in the in vitro activities of sn-glycerol-3-phosphate dehydrogenase, fumarase, and malic enzyme, but with a 16% reduction in the in vivo incorporation of label from [14C]glucose into lipid. When the catalase activity was inhibited to different degrees in ADH-null larvae, there was a simple linear correlation between the catalase activity and flux from [14C]ethanol into lipid. By feeding alcohols simultaneously with 3AT, ethanol and methanol were shown to react efficiently with catalase in wild-type larvae at moderately low dietary concentrations. Drosophila catalase did not react with other longer chain alcohols. Catalase apparently represents a minor pathway for ethanol degradation in D. melanogaster larvae, but it may be an important route for methanol elimination from D. melanogaster larvae.
van der Zel
A
A
Department of Biology, Knox College, Galesburg, Illinois 61401.
Dadoo
R
R
Geer
B W
BW
Heinstra
P W
PW
D000438:Alcohols / Q000378:metabolism*; D000640:Amitrole / Q000494:pharmacology; D000704:Analysis of Variance; D000818:Animals; D002374:Catalase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000201:enzymology*; D007814:Larva; D050356:Lipid Metabolism; D008297:Male; D000432:Methanol / Q000378:metabolism
D000438:Alcohols; D002374:Catalase; D000432:Methanol; D000640:Amitrole