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Literature summary for 2.7.1.105 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

Inhibitors Comment Organism Structure
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.048
-
ATP pH 7.5, 30°C, comparison of Km of skeletal muscle and liver enzyme Rattus norvegicus
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

Metals/Ions Comment Organism Structure
Mg2+
-
Rattus norvegicus

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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
phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
-
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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-
skeletal muscle
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.066
-
-
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 via phosphorylenzyme intermediate r
additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Rattus norvegicus ?
-
?

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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