Induction of the acetamidase of Aspergillus nidulans by acetate metabolism.
Growth tests and enzyme determinations strongly suggest that the acetamidase of Aspergillus nidulans is induced by a product of acetate metabolism rather than the substrate, acetamide. The cis-dominant mutation, amdI9, which is closely linked to amdS, the structural gene for the acetamidase, results in greatly increased sensitivity to induction by acetate metabolism. Propionate, L-threonine, and ethanol also result in acetamidase induction. Mutations in the facA, facB, and facC genes, which lead to low levels of acetyl-coenzyme A synthase, are epistatic to the amdI9 mutation for strong growth on acetamide medium and abolish acetamide and propionamide induction of the acetamidase and isocitrate lyase enzymes. Acetate, L-threonine, and ethanol, however, can induce these enzymes in strains containing facA and facC lesions but not in strains containing a facB lesion. The evidence suggests that acetamidase and isocitrate lyase may be induced by a similar mechanism.
D000081:Acetamides; D000106:Acetate-CoA Ligase / Q000096:biosynthesis; D000085:Acetates / Q000378:metabolism*; D000581:Amidohydrolases / Q000096:biosynthesis*; D001233:Aspergillus nidulans / Q000201:enzymology / Q000378:metabolism; D004790:Enzyme Induction; D005796:Genes; D007522:Isocitrate Lyase / Q000096:biosynthesis; D009154:Mutation
D000081:Acetamides; D000085:Acetates; D000581:Amidohydrolases; D007522:Isocitrate Lyase; D000106:Acetate-CoA Ligase