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Using methyl-1-thio-beta-D-galactoside as the inducer, the biosynthesis of beta-galactosidase was observed in Escherichia coli B with only endogenous sources of nitrogen and energy available. The addition of glucose, ribose, xylose, or glycerol as exogenous energy sources to nitrogen-deficient media blocked enzyme formation. Preinduction of the resting cells failed to overcome inhibition by the added energy sources. With limited quantities of glucose, ribose, xylose, or glycerol, synthesis of beta-galactosidase resumed abruptly and continued at the rate normal for cells in nitrogen-deficient media. Comparison of enzyme activities with oxygen uptake data revealed a reduction in the rate of oxygen uptake at the time enzyme synthesis resumed in media originally containing small amounts of energy sources. This change corresponded to only a fraction of the oxygen required for complete oxidation of one of the exogenous substrates. It is suggested that inhibition by these particular exogenous substrates involves metabolism to a common repressor or interference with an energy-transfer system.

The Effect of Exogenous Energy Sources on the Synthesis of ß-Galactosidase in Resting-Cell Suspensions of Escherichia coli