Abstract

The growth of mutantZ4ofBacillus licheniformison glucose and on a number of other carbohydrates is impaired, but growth on fructose, glycerol and on glucuronate is not. There are no significant differences between the mutant and its parent in the levels of glycolytic enzymes and in the ability of the organisms to take up labelled fructose; in contrast, the mutant takes up and phosphorylates labelled glucose, and its analogues methylα-glucoside and 2-deoxyglucose, to a much smaller extent than does the wild-type. Extracts of the mutant are virtually devoid of the inducible phosphoenolpyruvate-dependent glucose phosphotransferase present in the parent, though fructose phosphotransferase activity is present in both organisms. Revertants ofZ4, selected for growth on glucose, fully regain the wild-type phenotype. These results show that the phosphotransferase system plays a necessary role in the utilization of glucose by bacilli.

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