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The Escherichia coli adenylate cyclase complex: Activation by phosphoenolpyruvate

✍ Scribed by Peterkofsky, Alan ;Gazdar, Celia

Publisher: Wiley (John Wiley & Sons)
Year: 1978
Tongue: English
Weight: 546 KB
Volume: 9
Category: Article
ISSN: 0091-7419
DOI: 10.1002/jss.400090207

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✦ Synopsis

A model for the regulation of the activity of Escherichia coli adenylate cyclase is presented. It is proposed that Enzyme I of the phosphoeno1pyruvate:sugar phosphotransferase system (PTS) interacts in a regulatory sense with the catalytic unit of adenylate cyclase. The phosphoenolpyruvate (PEP)-dependent phosphorylation of Enzyme I is assumed to be associated with a high activity state of adenylate cyclase. The pyruvate or sugar-dependent dephosphorylation of Enzyme I is correlated with a low activity state of adenylate cyclase. Evidence in support of the proposed model involves the observation that Enzyme I mutants have low CAMP levels and that PEP increases cellular CAMP levels and, under certain conditions, activates adenylate cyclase, Kinetic studies indicate that various ligands have opposing effects on adenylate cyclase. While PEP activates the enzyme, either glucose or pyruvate inhibit it. The unique relationships of PEP and Enzyme I t o adenylaie cyclase activity are discussed.

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