Regulation of glycerol kinase by enzyme IIIGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system.
Wild-type glycerol kinase of Escherichia coli is inhibited by both nonphosphorylated enzyme IIIGlc of the phosphoenolpyruvate:carbohydrate phosphotransferase system and fructose 1,6-diphosphate. Mutant glycerol kinase, resistant to inhibition by fructose 1,6-diphosphate, was much less sensitive to inhibition by enzyme IIIGlc. The difference between the wild-type and mutant enzymes was even greater when inhibition was measured in the presence of both enzyme IIIGlc and fructose 1,6-diphosphate. The binding of enzyme IIIGlc to glycerol kinase required the presence of the substrate glycerol.
D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D005635:Fructosediphosphates / Q000378:metabolism / Q000494:pharmacology; D005990:Glycerol / Q000378:metabolism; D005991:Glycerol Kinase / Q000037:antagonists & inhibitors* / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism / Q000494:pharmacology*; D010770:Phosphotransferases / Q000037:antagonists & inhibitors*
D029968:Escherichia coli Proteins; D005635:Fructosediphosphates; C032242:crr protein, E coli; D010770:Phosphotransferases; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D005991:Glycerol Kinase; C029063:fructose-1,6-diphosphate; D005990:Glycerol