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Literature summary for 2.7.3.9 extracted from

  • Dimitrova, M.N.; Szczepanowski, R.H.; Ruvinov, S.B.; Peterkofsky, A.; Ginsburg, A.
    Interdomain Interaction and Substrate Coupling Effects on Dimerization and Conformational Stability of Enzyme I of the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System (2002), Biochemistry, 41, 906-913.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H189A cannot undergo autophosphorylation, kinetics of dimerization Escherichia coli
H189E comparable to wild type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Subunits

Subunits Comment Organism
dimer enzyme exists in a monomer-dimer equilibrium, monomer-dimer association regulates activity Escherichia coli