Catabolite repression and derepression of arylsulfatase synthesis in Klebsiella aerogenes.
When a mutant (Mao(-)) of Klebsiella aerogenes lacking an enzyme for tyramine degradation (monoamine oxidase) was grown with d-xylose as a carbon source, arylsulfatase was repressed by inorganic sulfate and repression was relieved by tyramine. When the cells were grown on glucose, tyramine failed to derepress the arylsulfatase synthesis. When grown with methionine as the sole sulfur source, the enzyme was synthesized irrespective of the carbon source used. Addition of cyclic adenosine monophosphate overcame the catabolite repression of synthesis of the derepressed enzyme caused by tyramine. Uptake of tyramine was not affected by the carbon source. We isolated a mutant strain in which derepression of arylsulfatase synthesis by tyramine occurred even in the presence of glucose and inorganic sulfate. This strain also produced beta-galactosidase in the presence of an inducer and glucose. These results, and those on other mutant strains in which tyramine cannot derepress enzyme synthesis, strongly suggest that a protein factor regulated by catabolite repression is involved in the derepression of arylsulfatase synthesis by tyramine.
D003470:Culture Media; D000242:Cyclic AMP / Q000494:pharmacology; D005696:Galactosidases / Q000378:metabolism; D005947:Glucose / Q000494:pharmacology; D007700:Kinetics; D007709:Klebsiella / Q000201:enzymology*; D009154:Mutation; D013429:Sulfatases / Q000032:analysis / Q000096:biosynthesis*; D014316:Tritium; D014363:Tryptamines / Q000378:metabolism
D003470:Culture Media; D014363:Tryptamines; D014316:Tritium; D000242:Cyclic AMP; D013429:Sulfatases; D005696:Galactosidases; D005947:Glucose