Regulation of cyclic AMP synthesis by enzyme III super(Glc) of the phosphoenolpyruvate:sugar phosphotransferase system in crp strains of Salmonella typhimurium

The authors investigated the claim (J. Daniel, J. Bacteriol. 157:940-941, 1984) that nonphosphorylated enzyme III super(Glc) of the phosphoenolpyruvate:sugar phosphotransferase system is required for full synthesis of bacterial cyclic AMP (cAMP). In crp strains of Salmonella typhimurium , cAMP synth...

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Bibliographic Details
Published in:Journal of bacteriology 1985-01, Vol.164 (1), p.477-478
Main Authors: Den Blaauwen, JL, Postma, P W
Format: Article
Language:English
Subjects:
Salmonella typhimurium
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Summary:The authors investigated the claim (J. Daniel, J. Bacteriol. 157:940-941, 1984) that nonphosphorylated enzyme III super(Glc) 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 III super(Glc). 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 the results, the authors conclude that phosphorylated enzyme III super(Glc) rather than nonphosphorylated enzyme III super(Glc) is required for full cAMP synthesis.
ISSN:0021-9193