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Glycerol-specific revertants were isolated from a phosphoenolpyruvate phosphotransferase mutant lacking enzyme I activity. Sixteen of the eighteen separately derived revertants were found to synthesize a fully active glycerol kinase no longer subject to feedback inhibition by fructose 1,6-diphosphate. The suppressor mutation mapped at the knownglpK locus. When the fructose, 1,6-diphosphate-insensitive kinase allele was transduced into a strain producing theglp enzymes constitutively, cells of the resultant strain were susceptible to killing by glycerol if this compound was added to a culture growing exponentially in casein hydrolysate. This phenomenon had been previously described for a strain which had a constitutive glycerol kinase refractory to feedback inhibition, but isolated by a different procedure. It is suggested that the suppression of the growth defect on glycerol in the enzyme I− mutant by the fructose 1,6-diphosphate-insensitive kinase is achieved by increasing the in vivo catalytic potential of glycerol kinase. This increased activity would allow more rapid conversion of glycerol tol -α-glycerophosphate, the true inducer of theglp system. The enzyme I defect in the parental strain impaired the inducibility of theglp system so that the normal basal catalytic activity of the kinase was insufficient to insure induction by glycerol.

journal of bacteriology

Glycerol-Specific Revertants of a Phosphoenolpyruvate Phosphotransferase Mutant: Suppression by the Desensitization of Glycerol Kinase to Feedback Inhibition