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Literature summary for 2.7.3.9 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)

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits Comment Organism
dimer
-
Escherichia coli

Synonyms

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