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Literature summary extracted from

  • Yun, Y.; Suh, J.
    Calorimetric and spectroscopic investigation of the interaction between the C-terminal domain of enzyme I and its ligands (2012), Protein Sci., 21, 1726-1733.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.9 the C-terminal and N-terminal domains of enzyme I are expressed in Escherichia coli BL21star(DE3) cells Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.3.9 130000
-
 calculated from amino acid sequence Escherichia coli

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.3.9 phosphoprotein the C-terminal domain can phosphorylate the N-terminal domain of enzyme I, but their binding is transient regardless of the presence of phosphoenolpyruvate Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.3.9 DEAE column chromatography and Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.9 phosphoenolpyruvate + protein histidine enzyme I catalyzes two reversible reactions: an Mg2+-dependent autophosphorylation reaction using phosphoenolpyruvate as a substrate, and a phosphotransfer reaction to histidine-containing phosphocarrier protein Escherichia coli pyruvate + protein Npi-phospho-L-histidine
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.3.9 dimer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.3.9 EIC C-terminal domain of enzyme I Escherichia coli
2.7.3.9 EIN N-terminal domain of enzyme I Escherichia coli