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Literature summary extracted from

  • Kitamura, K.; Uyeda, K.; Kangawa, K.; Matsuo, H.
    Purification and characterization of rat skeletal muscle fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase (1989), J. Biol. Chem., 264, 9799-9806.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 additional information phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme; phosphorylation by cAMP-dependent protein kinase of liver enzyme, not of skeletal muscle enzyme, since the phosphorylation site target Ser-32 of the liver isozyme is replaced by Ala in the muscle isozyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.105 0.048
-
 ATP pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme Rattus norvegicus
2.7.1.105 0.056
-
 beta-D-fructose 6-phosphate pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.105 Mg2+
-
 Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.105 additional information
-
 amino acid composition Rattus norvegicus
2.7.1.105 54000
-
 2 * 54000, SDS-PAGE, amino acid sequence Rattus norvegicus
2.7.1.105 100000
-
 gel filtration Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.105 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.105 phosphoprotein phosphorylation by cAMP-dependent protein kinase of liver enzyme, not of skeletal muscle enzyme, since the phosphorylation site target Ser-32 of the liver isozyme is replaced by Ala in the muscle isozyme Rattus norvegicus
2.7.1.105 phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Rattus norvegicus

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.105
-
 Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.105 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

EC Number Source Tissue Comment Organism Textmining
2.7.1.105 liver
-
 Rattus norvegicus
-
2.7.1.105 skeletal muscle
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.105 0.066
-
-
 Rattus norvegicus

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.1.105 dimer 2 * 54000, SDS-PAGE, amino acid sequence Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.105 30
-
 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.105 8.5
-
 skeletal muscle Rattus norvegicus