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Literature summary for 2.7.1.105 extracted from

  • Van Schaftingen, E.; Hers, H.G.
    Purification and properties of phosphofructokinase 2/fructose 2,6-bisphosphatase from chicken liver and from pigeon muscle (1986), Eur. J. Biochem., 159, 359-365.
    View publication on PubMed
Search for more literature for 2.7.1.105

Inhibitors

Inhibitors Comment Organism Structure
citrate
-
 Columba sp.
citrate
-
 Gallus gallus
additional information phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Columba sp.
additional information phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0072
-
 MgATP2- pH 7.1, 30°C, phosphorylated enzyme Columba sp.
0.0095 0.012 MgATP2- pH 7.1, 30°C, native pigeon enzyme Columba sp.
0.05
-
 beta-D-fructose 6-phosphate pH 7.1, 30°C, MgATP2-, phosphorylated chicken enzyme Gallus gallus
0.29
-
 MgATP2- pH 7.1, 30°C, native chicken enzyme Gallus gallus

Metals/Ions

Metals/Ions Comment Organism Structure
phosphate
-
 Gallus gallus
phosphate
-
 Columba sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
 2 * 53000, SDS-PAGE, with a minor constituent of MW 54000 Columba sp.
54000
-
 2 * 54000, SDS-PAGE Gallus gallus
110000
-
 gel filtration Gallus gallus
110000
-
 gel filtration Columba sp.

Organism

Organism UniProt Comment Textmining
Columba sp.
-
-
-
Gallus gallus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Gallus gallus
phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Columba sp.

Purification (Commentary)

Purification (Comment) Organism
-
 Gallus gallus
-
 Columba sp.

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-
muscle
-
 Columba sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.11
-
-
 Columba sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + beta-D-fructose 6-phosphate
-
 Gallus gallus ADP + beta-D-fructose 2,6-bisphosphate
-
 r
ATP + beta-D-fructose 6-phosphate
-
 Columba sp. ADP + beta-D-fructose 2,6-bisphosphate
-
 r
MgATP2- + beta-D-fructose 6-phosphate
-
 Gallus gallus ?
-
 ?
MgATP2- + beta-D-fructose 6-phosphate
-
 Columba sp. ?
-
 ?
additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Gallus gallus ?
-
 ?
additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Columba sp. ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 54000, SDS-PAGE Gallus gallus
dimer 2 * 53000, SDS-PAGE, with a minor constituent of MW 54000 Columba sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Gallus gallus
30
-
 assay at Columba sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Gallus gallus
10
-
-
 Columba sp.

pH Range

pH Minimum pH Maximum Comment Organism
6 10 about 80% of maximal activity at pH 6.0 and 9.5 Gallus gallus
7.5 10 linear increase up to pH 10 from 10% of maximal activity at pH 7.5 Columba sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.083
-
 citrate pH 7.1, 30°C, native enzyme Columba sp.
0.084
-
 citrate pH 7.1, 30°C, phosphorylated enzyme Columba sp.
0.13
-
 citrate pH 7.1, 30°C, phosphorylated enzyme Gallus gallus
0.49
-
 citrate pH 7.1, 30°C, native enzyme Gallus gallus