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Literature summary for 2.7.1.11 extracted from

  • Brueser, A.; Kirchberger, J.; Schoeneberg, T.
    Altered allosteric regulation of muscle 6-phosphofructokinase causes Tarui disease (2012), Biochem. Biophys. Res. Commun., 427, 133-137.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ADP
-
Homo sapiens
ADP
-
Oryctolagus cuniculus
AMP
-
Homo sapiens
AMP
-
Oryctolagus cuniculus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae strain HD114-8D Homo sapiens

Protein Variants

Protein Variants Comment Organism
D543A the mutation causes an increased efficacy of ATP at the inhibitory allosteric binding site. The mutation drastically increases K0.5 for AMP. The activating effect of ADP found in wild type enzyme is completely lost Homo sapiens
N341A the mutation results in an increased effect of the inhibitor ATP on enzyme activity Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ATP
-
Homo sapiens
ATP
-
Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0232
-
ATP mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0425
-
ATP wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0498
-
ATP wild type enzyme, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0528
-
ATP mutant enzyme N341A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0647
-
ATP mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0674
-
ATP mutant enzyme D543A, in the presence of 1 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0674
-
ATP mutant enzyme D543A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0769
-
ATP mutant enzyme D543A, in the presence of 0.1 mM 5-phospho-alpha-D ribose 1-diphosphate, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.0894
-
ATP mutant enzyme D543A, in the presence of 0.1 mM 2'-iodo-ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.114
-
ATP mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.151
-
ATP mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.169
-
ATP mutant enzyme D543A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.169
-
ATP wild type enzyme, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
PEG 6000 precipitation, Resource Q column chromatography, and BioSep SEC-S4000 gel filtration Homo sapiens
PEG 6000 precipitation, Resource Q column chromatography, and BioSep SEC-S4000 gel filtration Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Homo sapiens
-
skeletal muscle
-
Oryctolagus cuniculus
-

Storage Stability

Storage Stability Organism
-20°C, purified enzyme with 10% glycerol (v/v), 2 weeks, no loss of activity Homo sapiens
-20°C, purified enzyme with 10% glycerol (v/v), 2 weeks, no loss of activity Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-fructose 6-phosphate
-
Homo sapiens ADP + D-fructose 1,6-bisphosphate
-
?
ATP + D-fructose 6-phosphate
-
Oryctolagus cuniculus ADP + D-fructose 1,6-bisphosphate
-
?

Synonyms

Synonyms Comment Organism
ATP-dependent 6-phosphofructokinase
-
Homo sapiens
ATP-dependent 6-phosphofructokinase
-
Oryctolagus cuniculus
ATP: D-fructose-6-phosphate-1-phosphotransferase
-
Homo sapiens
ATP: D-fructose-6-phosphate-1-phosphotransferase
-
Oryctolagus cuniculus
phosphofructokinase-1
-
Homo sapiens
phosphofructokinase-1
-
Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.7
-
ATP mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
0.9
-
ATP mutant enzyme D543A, in the presence of 0.1 mM 2'-iodo-ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
1.1
-
ATP mutant enzyme D543A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
1.4
-
ATP mutant enzyme D543A, in the presence of 0.1 mM 5-phospho-alpha-D ribose 1-diphosphate, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
1.4
-
ATP mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
2
-
ATP wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
2.1
-
ATP mutant enzyme N341A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
2.3
-
ATP mutant enzyme D543A, in the presence of 1 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
2.3
-
ATP mutant enzyme D543A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
5.2
-
ATP mutant enzyme N341A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
5.3
-
ATP wild type enzyme, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens
8.5
-
ATP wild type enzyme, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C Homo sapiens

General Information

General Information Comment Organism
malfunction mutations in the muscle 6-phosphofructokinase gene cause Tarui disease Homo sapiens
malfunction mutations in the muscle 6-phosphofructokinase gene cause Tarui disease Oryctolagus cuniculus