Enzyme III stimulation of cyclic AMP synthesis in an Escherichia coli crp mutant.
Cyclic AMP (cAMP) synthesis in Escherichia coli is altered in cAMP receptor protein mutants and in phosphoenolpyruvate:sugar phosphotransferase transport system mutants. The stimulation of cAMP synthesis observed in cAMP receptor protein-deficient mutants is largely dependent upon enzyme III of the phosphoenolpyruvate:sugar phosphotransferase transport system. The phosphoenolpyruvate:sugar phosphotransferase transport system enzyme I is not required for elevated cAMP synthesis. These results suggest that enzyme III plays an important role in regulating adenylate cyclase activity.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000242:Cyclic AMP / Q000096:biosynthesis*; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins; D009154:Mutation; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D010766:Phosphorylation; D017852:Phosphotransferases (Nitrogenous Group Acceptor); D011953:Receptors, Cyclic AMP / Q000502:physiology
D029968:Escherichia coli Proteins; D011953:Receptors, Cyclic AMP; C032242:crr protein, E coli; D000242:Cyclic AMP; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D017852:Phosphotransferases (Nitrogenous Group Acceptor); C022360:phosphoenolpyruvate-protein phosphotransferase; D000262:Adenylyl Cyclases