Regulation of cyclic AMP synthesis by enzyme IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system in crp strains of Salmonella typhimurium.
We investigated the claim (J. Daniel, J. Bacteriol. 157:940-941, 1984) that nonphosphorylated enzyme IIIGlc of the phosphoenolpyruvate:sugar phosphotransferase system is required for full synthesis of bacterial cyclic AMP (cAMP). In crp strains of Salmonella typhimurium, cAMP synthesis by intact cells was regulated by the phosphorylation state of enzyme IIIGlc. Introduction of either a pstHI deletion mutation or a crr::Tn10 mutation resulted in a low level of cAMP synthesis. In contrast, crp strains containing a leaky pstI mutation exhibited a high level of cAMP synthesis which was inhibited by phosphotransferase system carbohydrates. From these results, we conclude that phosphorylated enzyme IIIGlc rather than nonphosphorylated enzyme IIIGlc is required for full cAMP synthesis.
D000242:Cyclic AMP / Q000096:biosynthesis*; D029968:Escherichia coli Proteins; D009154:Mutation; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000502:physiology*; D010766:Phosphorylation; D012486:Salmonella typhimurium / Q000378:metabolism*
D029968:Escherichia coli Proteins; C032242:crr protein, E coli; D000242:Cyclic AMP; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System