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Literature summary for 2.7.1.40 extracted from

  • Lee, J.C.
    Modulation of allostery of pyruvate kinase by shifting of an ensemble of microstates (2008), Acta Biochim. Biophys. Sin., 40, 663-669.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.40

Activating Compound

Activating Compound Comment Organism Structure
D-fructose-1,6-bisphosphate
-
 Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
S240P the mutant exhibits steady-state kinetic behavior that indicates that it is more responsive to regulation by effectors Oryctolagus cuniculus
T340M the mutant is half as active as the wild type enzyme Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
L-Phe
-
 Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ essential for activity Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + phosphoenolpyruvate Oryctolagus cuniculus
-
 ATP + pyruvate
-
 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P11974
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Oryctolagus cuniculus
-
muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate
-
 Oryctolagus cuniculus ATP + pyruvate
-
 ?

Subunits

Subunits Comment Organism
homotetramer
-
 Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ADP
-
 Oryctolagus cuniculus