Abstract
A phosphoenolpyruvate:dihydroxyacetone phosphotransferase was induced in E. coli grown on dihydroxyacetone as sole C source or in its presence. This is the first example of a triose which can be acted upon by the membrane complex to provide a central intermediate in glycolysis. The presence of this system explains the ability of a mutant, in which the ATP-dependent glycerol kinase is genetically replaced by a glycerol:NAD 2-oxidoreductase, to grow on glycerol.

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