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Literature summary for 2.7.1.40 extracted from

  • Portela, P.; Moreno, S.; Rossi, S.
    Characterization of yeast pyruvate kinase 1 as a protein kinase A substrate, and specificity of the phosphorylation site sequence in the whole protein (2006), Biochem. J., 396, 117-126.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
S22A mutant protein activity is decreased by as much as 90% when compared with wild-type, is more active in the absence of fructose 1,6-bisphosphate Saccharomyces cerevisiae
T94A activity similar to the wild type enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
SDS-PAGE Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae JT20454
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Sephadex G25 gel filtration, DEAE-cellulose column chromatography, phosphocellulose column chromatography, and ammonium sulfate precipitation Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate
-
Saccharomyces cerevisiae ATP + pyruvate
-
?
ADP + phosphoenolpyruvate
-
Saccharomyces cerevisiae JT20454 ATP + pyruvate
-
?
additional information pyruvate kinase is a substrate of protein kinase A Saccharomyces cerevisiae ?
-
?
additional information pyruvate kinase is a substrate of protein kinase A Saccharomyces cerevisiae JT20454 ?
-
?

Synonyms

Synonyms Comment Organism
Pyk1
-
Saccharomyces cerevisiae
pyruvate kinase 1
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ADP
-
Saccharomyces cerevisiae

pI Value

Organism Comment pI Value Maximum pI Value
Saccharomyces cerevisiae 2D-PAGE
-
7.5