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Literature summary for 2.7.1.105 extracted from

  • Aragón, J.J.; Gómez, M.E.; Gancedo, C.
    Identification of two forms of 6-phosphofructo-2-kinase in yeast (1987), FEBS Lett., 226, 121-124.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
AMP not Saccharomyces cerevisiae
citrate not Saccharomyces cerevisiae
diphosphate not phosphate Saccharomyces cerevisiae
phosphoenolpyruvate
-
Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.29 0.38 ATP pH 7.1, 30°C, kinetic data of various enzyme forms Saccharomyces cerevisiae
0.33 0.4 beta-D-fructose 6-phosphate pH 7.1, 30°C, kinetic data of various enzyme forms Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
gel filtration Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phophorylation by cAMP-dependent protein kinase causes activation Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
2 isozymes, partial Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + beta-D-fructose 6-phosphate
-
Saccharomyces cerevisiae ADP + beta-D-fructose 2,6-bisphosphate
-
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