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  • Title: Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: mechanism of phosphoryl-group transfer from phosphoenolpyruvate to HPr.
    Author: Misset O, Robillard GT.
    Journal: Biochemistry; 1982 Jun 22; 21(13):3136-42. PubMed ID: 7049237.
    Abstract:
    The mechanism of phosphoryl-group transfer from phosphoenolpyruvate (PEP) to HPr, catalyzed by enzyme I of the Escherichia coli PEP-dependent phosphotransferase system, has been studied in vitro. Steady-state kinetics and isotope exchange measurements revealed that this reaction cannot be described by a classical ping-pong mechanism although phosphoenzyme I acts as an intermediate. The kinetic data indicate that HPr and PHPr occupy binding sites on enzyme I that do not overlap with the binding sites for PEP and pyruvate. As a result, binding interactions between HPr and enzyme I exist regardless of their phosphorylated state. A general mechanism is presented that describes the phosphorylation of HPr. The physiological implications of this mechanism are discussed.
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