The differential rate of synthesis of penicillinamidohydrolase (penicillin acylase -- EC 3.5.1.11) was studied in Escherichia coli growing in some chemically defined media and in a complex medium. The enzyme is synthesized at a constant rate only during the exponential phase of growth of cells. Its synthesis is induced most effectively (with respect to quantity) by phenylacetic acid. The induction lag of the enzyme synthesis in a medium with acetate corresponds to two generation times. The highest rate of the enzyme synthesis is reached in a medium containing phenylacetic acid as the only source of carbon and energy. The enzyme synthesis is fully repressed by an increased concentration of dissolved oxygen in the medium, even when Escherichia coli is cultivated in the medium with phenylacetic acid as the only carbon and energy source.

• MeSH
• Amidohydrolases biosynthesis   MeSH
• Amides pharmacology   MeSH
• Enzyme Induction MeSH
• Enzyme Repression MeSH
• Escherichia coli enzymology   growth & development   MeSH
• Phenoxyacetates pharmacology   MeSH
• Phenylacetates pharmacology   MeSH
• Kinetics MeSH
• Culture Media MeSH
• Oxygen pharmacology   MeSH
• Penicillin Amidase biosynthesis   MeSH
• Structure-Activity Relationship MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Amidohydrolases MeSH
• Amides MeSH
• Phenoxyacetates MeSH
• Phenylacetates MeSH
• Culture Media MeSH
• Oxygen MeSH
• Penicillin Amidase MeSH

Synthesis of penicillinamidohydrolase (penicillin acylase, EC 3.5.1.11) in Escherichia coli is subjected to the absolute catabolite repression by glucose and partial repression by acetate. Both types of catabolite repression of synthesis of the enzyme in Escherichia coli are substantially influenced by cyclic 3',5'-adenosinemonophosphate (cAMP). Growth diauxie in a mixed medium containing glucose and phenylacetic acid serving as carbon and energy sources is overcome by cAMP. cAMP does not influence the basal rate of the enzyme synthesis (without the inducer). Derepression of synthesis of penicillinamidohydrolase by cAMP in a medium with glucose and inducer (phenylacetic acid) is associated with utilization of the inducer, due probably to derepression of other enzymes responsible for degradation of phenylacetic acid. Lactate can serve as a "catabolically neutral" source of carbon suitable for the maximum production of penicillinamidohydrolase. The gratuitous induction of the enzyme synthesis in a medium with lactate as the carbon and energy source and with phenylacetic acid is not influenced by cAMP; however, cAMP overcomes completely the absolute catabolite repression of the enzyme synthesis by glucose.

• MeSH
• Acetates pharmacology   MeSH
• Amidohydrolases biosynthesis   MeSH
• Cyclic AMP pharmacology   MeSH
• Enzyme Induction MeSH
• Enzyme Repression MeSH
• Escherichia coli enzymology   growth & development   MeSH
• Phenylacetates pharmacology   MeSH
• Glucose antagonists & inhibitors   pharmacology   MeSH
• Kinetics MeSH
• Culture Media MeSH
• Lactates pharmacology   MeSH
• Penicillin Amidase biosynthesis   MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Acetates MeSH
• Amidohydrolases MeSH
• Cyclic AMP MeSH
• Phenylacetates MeSH
• Glucose MeSH
• Culture Media MeSH
• Lactates MeSH
• Penicillin Amidase MeSH