Penicillinamidohydrolase in Escherichia coli. III. Catabolite repression, diauxie, effect of cAMP and nature of the enzyme induction
Language English Country United States Media print
Document type Journal Article
PubMed
170173
DOI
10.1007/bf02878111
Knihovny.cz E-resources
- 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
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.
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J Bacteriol. 1969 Feb;97(2):550-6 PubMed
Nature. 1969 Mar 15;221(5185):1012-4 PubMed
Appl Microbiol. 1964 May;12:185-7 PubMed
Annu Rev Microbiol. 1969;23:539-78 PubMed
Nature. 1969 Aug 23;223(5208):810-2 PubMed
J Mol Biol. 1968 Dec;38(3):421-6 PubMed
J Biol Chem. 1968 Oct 25;243(20):5420-7 PubMed
Biochem Biophys Res Commun. 1968 Mar 27;30(6):656-64 PubMed
Folia Microbiol (Praha). 1975;20(4):289-97 PubMed
J Biol Chem. 1970 May 10;245(9):2259-67 PubMed
Biochem Biophys Res Commun. 1968 May 23;31(4):603-8 PubMed
Biochem J. 1971 Jul;123(4):579-84 PubMed
Proc Natl Acad Sci U S A. 1970 May;66(1):104-10 PubMed
Biochem J. 1970 Jul;118(3):481-9 PubMed
Folia Microbiol (Praha). 1975;20(3):224-30 PubMed
J Bacteriol. 1970 May;102(2):411-22 PubMed
Antibiotiki. 1973 Oct;18(10):882-6 PubMed
Cold Spring Harb Symp Quant Biol. 1961;26:249-56 PubMed
J Biol Chem. 1969 Nov 10;244(21):5828-35 PubMed
Mikrobiologiia. 1967 Sep-Oct;36(5):912-7 PubMed
J Bacteriol. 1973 Feb;113(2):781-5 PubMed
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