Abstract
Using methyl-l-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.