Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Misset, O.; Brouwer, M.; Robillard, G.T.
    Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Evidence that the dimer is the active form of enzyme I (1980), Biochemistry, 19, 883-890.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.3.9 Mg2+
-
Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.9 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.9 phosphoenolpyruvate + histidine-containing protein
-
Escherichia coli pyruvate + phosphorylated histidine-containing protein
-
r
2.7.3.9 pyruvate + phosphorylated histidine-containing protein
-
Escherichia coli phosphoenolpyruvate + histidine-containing protein
-
r

Subunits

EC Number Subunits Comment Organism
2.7.3.9 dimer dimerization is induced by phosphoenolpyruvate and Mg2+, dimer is the active form of enzyme Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.3.9 37
-
assay at Escherichia coli