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Literature summary for 4.1.1.49 extracted from

  • Lee, H.J.; Kim, H.J.; Seo, J.; Na, Y.A.; Lee, J.; Lee, J.Y.; Kim, P.
    Estimation of phosphoenolpyruvate carboxylation mediated by phosphoenolpyruvate carboxykinase (PCK) in engineered Escherichia coli having high ATP (2013), Enzyme Microb. Technol., 53, 13-17.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
acetyl-CoA
-
Escherichia coli
L-fructose 1,6-bisphosphate
-
Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli ER2566 cells Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ATP the presence of 9.6 mM ATP decreases 3folds the catalytic efficiency of the enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
phosphoenolpyruvate at pH 7.0 and 37°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + phosphoenolpyruvate + CO2 Escherichia coli
-
ATP + oxaloacetate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P22259
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni+ affinity column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate + CO2
-
Escherichia coli ATP + oxaloacetate
-
?

Synonyms

Synonyms Comment Organism
PCK
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.67
-
phosphoenolpyruvate at pH 7.0 and 37°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
11
-
phosphoenolpyruvate at pH 7.0 and 37°C Escherichia coli