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Literature summary for 2.7.3.9 extracted from

  • Dimitrova, M.N.; Peterkofsky, A.; Ginsburg, A.
    Opposing effects of phosphoenolpyruvate and pyruvate with Mg(2+) on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli (2003), Protein Sci., 12, 2047-2056.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.3.9

Activating Compound

Activating Compound Comment Organism Structure
phosphoenolpyruvate physiological concentrations of phosphoenolpyruvate and Mg2+ increase the amount of dimeric, active dephospho-enzyme I Escherichia coli

Protein Variants

Protein Variants Comment Organism
H189A inactive enzyme form Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
pyruvate physiological concentrations of pyruvate and Mg2+ decrease the amount of dimeric, active dephospho-enzyme I Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ enzyme I of the PEP:sugar phosphotransferase system is regulated by a monomer-dimer equilibrium. A Mg2+-dependent autophosphorylation by phosphoenolpyruvate requires the homodimer. Physiological concentrations of phosphoenolpyruvate and Mg2+ increase, whereas pyruvate and Mg2+ decrease the amount of dimeric, active dephospho-enzyme I Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Subunits

Subunits Comment Organism
More enzyme I of the PEP:sugar phosphotransferase system is regulated by a monomer-dimer equilibrium. A Mg2+-dependent autophosphorylation by phosphoenolpyruvate requires the homodimer. Physiological concentrations of phosphoenolpyruvate and Mg2+ increase, whereas pyruvate and Mg2+ decrease the amount of dimeric, active dephospho-enzyme I Escherichia coli

Synonyms

Synonyms Comment Organism
phosphotransferase enzyme I
-
 Escherichia coli