Abstract
2-ketobutyrate and its analogues were found to inhibit strongly and transiently the rate of beta-galactosidase synthesis in Escherichia coli K12. This effect was ascribed to a strong and transient inhibition of the adenylate cyclase activity. By using pts mutants, we showed, in agreement with our previous results (Daniel et al. 1983), that the likely target of 2-ketobutyrate and its analogues is the phosphoenolpyruvate: glycose phosphotransferase transport system (PTS). Furthermore, evidence for such a cascade effect caused by 2-ketobutyrate and its analogues allowed us to corroborate our previous proposal (Daniel et al. 1983) that 2-ketobutyrate, a precursor of isoleucine, acts as an E. coli alarmone monitoring the passage from anaerobic to aerobic growth conditions.
MeSH Terms
Adenylyl Cyclase Inhibitors
Butyrates/toxicity
Cyclic AMP/metabolism
Escherichia coli/drug effects,enzymology,genetics
Galactosidases/genetics
Genotype
Kinetics
Phosphoenolpyruvate Sugar Phosphotransferase System/genetics,metabolism
Species Specificity
Structure-Activity Relationship
beta-Galactosidase/genetics
Chemicals
Adenylyl Cyclase Inhibitors
Butyrates
alpha-ketobutyric acid
Cyclic AMP
Phosphoenolpyruvate Sugar Phosphotransferase System
phosphoenolpyruvate-glucose phosphotransferase
Galactosidases
beta-Galactosidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Daniel J
Joseph E
Danchin A
References (15)
15 references, click to expand
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