Abstract
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.
MeSH Terms
Acetamides
Acetate-CoA Ligase/biosynthesis
Acetates/metabolism
Amidohydrolases/biosynthesis
Aspergillus nidulans/enzymology,metabolism
Enzyme Induction
Genes
Isocitrate Lyase/biosynthesis
Mutation
Chemicals
Acetamides
Acetates
Amidohydrolases
Isocitrate Lyase
Acetate-CoA Ligase
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Hynes M J
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