Alcohol dehydrogenase II and fructose-1,6-bisphosphatase appear to be co-regulated in wild-type yeast.
An activity gel assay for fructose-1,6-bisphosphatase (FBP), the enzyme catalyzing the final step in gluconeogenesis in yeast, has been developed which can be used in conjunction with spectrophotometric assays to show that it is tightly co-regulated with the inducible alcohol dehydrogenase, ADHII. Both enzymes are repressed coordinately in aerobically grown yeast by the addition of high levels of glucose or ethanol, and induced on minimal medium by the addition of yeast extract. A mutant deficient in FBP segregates independently of the ADHII structural gene locus. This phenomenon is of interest because of the discovery of Ciriacy [(1979) Mol. Gen. Genet. 176, 427-431] of mutants (ccr, or carbon catabolite repression) which repress both FBP and ADHII simultaneously, along with several other enzymes.
Wills
C
C
Martin
T
T
Melham
T
T
Walker
D
D
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000096:biosynthesis* / Q000235:genetics; D004790:Enzyme Induction / Q000187:drug effects; D000431:Ethanol / Q000494:pharmacology; D006597:Fructose-Bisphosphatase / Q000096:biosynthesis* / Q000235:genetics; D005943:Gluconeogenesis; D005947:Glucose / Q000494:pharmacology; D009154:Mutation; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
D000431:Ethanol; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; D006597:Fructose-Bisphosphatase; D005947:Glucose