Regulation of aflatoxin biosynthesis: effect of glucose on activities of various glycolytic enzymes.
Catabolism of carbohydrates has been implicated in the regulation of aflatoxin synthesis. To characterize this effect further, the activities of various enzymes associated with glucose catabolism were determined in Aspergillus parasiticus organisms that were initially cultured in peptone-mineral salts medium and then transferred to glucose-mineral salts and peptone-mineral salts media. After an initial increase in activity, the levels of glucose 6-phosphate dehydrogenase, mannitol dehydrogenase, and malate dehydrogenase were lowered in the presence of glucose. Phosphofructokinase activity was greater in the peptone-grown mycelium, but fructose diphosphatase was largely unaffected by carbon source. Likewise, carbon source had relatively little effect on the activities of pyruvate kinase, malic enzyme, isocitrate-NADP dehydrogenase, and isocitrate-NAD dehydrogenase. The results suggest that glucose may, in part, regulate aflatoxin synthesis via a carbon catabolite repression of NADPH-generating and tricarboxylic acid cycle enzymes.
D000348:Aflatoxins / Q000096:biosynthesis*; D001230:Aspergillus / Q000378:metabolism*; D006597:Fructose-Bisphosphatase / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D006019:Glycolysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008354:Mannitol Dehydrogenases / Q000378:metabolism; D010732:Phosphofructokinase-1 / Q000378:metabolism
D000348:Aflatoxins; D008354:Mannitol Dehydrogenases; D005954:Glucosephosphate Dehydrogenase; D010732:Phosphofructokinase-1; D006597:Fructose-Bisphosphatase; D005947:Glucose