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Literature summary for 2.7.1.40 extracted from

  • Fenton, A.W.; Tang, Q.
    An activating interaction between the unphosphorylated N-terminus of human liver pyruvate kinase and the main body of the protein is interrupted by phosphorylation (2009), Biochemistry, 48, 3816-3818.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
D-fructose 1,6-bisphosphate
-
Homo sapiens

Protein Variants

Protein Variants Comment Organism
S12D the introduction of S12D mutation mimics the effects of phosphorylation Homo sapiens
S12E the introduction of S12E mutation mimics the effects of phosphorylation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
L-Ala
-
Homo sapiens
additional information phosphorylation at Ser12 interrupts an activating interaction of N-terminal residues (including those at positions 7-10) with the main body of the protein, as a means of inhibiting substrate affinity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PYK
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ADP
-
Homo sapiens