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- W2022134377 abstract "Abstract Combined manometric studies and enzyme measurements revealed that pyruvate and gluconate repressed the induction of β3-galactosidase in resting cells of Escherichia coli B previously grown on the energy source tested. This inhibition resembled that reported earlier for glucose, xylose, ribose, and glycerol. However, glucose-1-phosphate, glucose-6-phosphate, and α-glycerolphosphate at relatively high concentrations did not exhibit a typical “glucose effect,” although some reduction in the rate of β-galactosidase formation was observed. Tracer experiments with glucose-U-C 14 and inorganic P 32 revealed conversion of glucose to glucose-6-phosphate and glycogen, neither of which was involved in the inhibition of the enzyme synthesis. With endogenous glucose-6-phosphate present after resumption of enzyme production, the subsequent metabolites should also have been present in the respiring cells, and thus these compounds too were excluded as possible repressors. Moreover, the termination of the inhibition coincided with the disappearance of exogenous glucose. Therefore, the repression typical of glucose on resting E. coli B must have involved the conversion of glucose to glucose-6-phosphate. Since glucose permease already exists after growth on glucose, only the actual transport of glucose or the action of glucokinase remain as bases for the repression." @default.
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- W2022134377 date "1964-12-01" @default.
- W2022134377 modified "2023-09-25" @default.
- W2022134377 title "Mechanism of glucose inhibition of β-galactosidase biosynthesis in resting cultures of Escherichia coli" @default.
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- W2022134377 doi "https://doi.org/10.1016/0003-9861(64)90424-2" @default.
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