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Literature summary for 2.7.1.105 extracted from

  • Bruni, P.; Vandoolaeghe, P.; Rousseau, G.G.; Hue, L.; Rider, M.H.
    Expression and regulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isozymes in white adipose tissue (1999), Eur. J. Biochem., 259, 756-761.
    View publication on PubMed
Search for more literature for 2.7.1.105

Inhibitors

Inhibitors Comment Organism Structure
additional information phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
adipose tissue Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46 Rattus norvegicus
a

Source Tissue

Source Tissue Comment Organism Textmining
adipose tissue equal amounts of isozyme L and M Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + beta-D-fructose 6-phosphate
-
 Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
-
 r
additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
More two isozymes: 55000 Da and 52000 Da Rattus norvegicus