2.7.1.11: 6-phosphofructokinase
This is an abbreviated version!
For detailed information about 6-phosphofructokinase, go to the full flat file.
Word Map on EC 2.7.1.11
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2.7.1.11
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citrate
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glycogen
-
amp
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glucose-6-phosphate
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2,6-bisphosphate
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aldolase
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phosphorylase
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phosphoenolpyruvate
-
erythrocyte
-
pentose
-
glucokinase
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gluconeogenesis
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malate
-
creatine
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hexose
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glyceraldehyde-3-phosphate
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phosphoglycerate
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fructose-2,6-bisphosphate
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enolase
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fructose-1,6-bisphosphatase
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gluconeogenic
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vastus
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carboxykinase
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6-phosphogluconate
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lateralis
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6-phosphofructo-2-kinase
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phosphoglucose
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triose
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phosphoglucomutase
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pfkfb3
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soleus
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1,6-bisphosphatase
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mgatp
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phosphocreatine
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fbpase
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m-type
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fructose-1,6-diphosphate
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myoglobinuria
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bisphosphatase
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glycogenosis
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2.7.1.1
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1,6-diphosphate
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liver-type
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entner-doudoroff
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2,3-diphosphoglycerate
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3-hydroxyacyl-coa
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mcardle
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synthesis
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heterotropic
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biotechnology
-
analysis
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glycogenolytic
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myophosphorylase
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medicine
- 2.7.1.11
- citrate
- glycogen
- amp
- glucose-6-phosphate
- 2,6-bisphosphate
- aldolase
- phosphorylase
- phosphoenolpyruvate
- erythrocyte
- pentose
- glucokinase
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gluconeogenesis
- malate
- creatine
- hexose
- glyceraldehyde-3-phosphate
- phosphoglycerate
- fructose-2,6-bisphosphate
- enolase
- fructose-1,6-bisphosphatase
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gluconeogenic
-
vastus
-
carboxykinase
- 6-phosphogluconate
- lateralis
- 6-phosphofructo-2-kinase
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phosphoglucose
- triose
- phosphoglucomutase
- pfkfb3
- soleus
-
1,6-bisphosphatase
- mgatp
- phosphocreatine
- fbpase
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m-type
- fructose-1,6-diphosphate
- myoglobinuria
-
bisphosphatase
- glycogenosis
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2.7.1.1
- 1,6-diphosphate
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liver-type
-
entner-doudoroff
- 2,3-diphosphoglycerate
- 3-hydroxyacyl-coa
- mcardle
- synthesis
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heterotropic
- biotechnology
- analysis
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glycogenolytic
- myophosphorylase
- medicine
Reaction
Synonyms
1-phosphofructokinase, 2-keto-3-deoxygluconate kinase, 6-phosphofructo 1-kinase, 6-phosphofructo-1-kinase, 6-phosphofructokinase I, 6-phosphofructokinase, platelet type, 6-phosphofructose 1-kinase, 6-phosphofructose-1-kinase, A/GTP-PFK, ADP-dependent phosphofructokinase, APE0012, At2g22480, At4g26270, At4g29220, At4g32840, At5g56630, At5g61580, ATP-dependent 6-phosphofructokinase, ATP-dependent 6-phosphofructokinase isozyme 2, ATP-dependent PFK, ATP-dependent phosphofructokinase, ATP-PFK, ATP: D-fructose-6-phosphate-1-phosphotransferase, ATP:D-fructose-6-phosphate-1-phosphotransferase, D-fructose-6-phosphate 1-phosphotransferase, fructose 6-phosphate kinase, fructose 6-phosphokinase, hosphofructokinase-1, HVO_A0328, KDG kinase, KDGal kinase, KDGK-1, KDGK-2, kinase, phosphofructo- (phosphorylating), LmPFK, muscle-type phosphofructokinase, nucleotide triphosphate-dependent phosphofructokinase, OC_Os04g39420, PFK, PFK-1, Pfk-2, PFK-L, PFK-M, PFK-P, PFK1, PFK2, PFK3, PFK4, PFK5, PFK6, PFK7, PFKA, PFKA1, PFKA2, PFKA3, pfkB, PFKL, PFKM, PFKMS, PFKP, PfpA4, phospho-1,6-fructokinase, phosphofructo-1-kinase, phosphofructokinase, phosphofructokinase 1, phosphofructokinase M, phosphofructokinase-1, phosphofructokinase-2, phosphofructokinase-M, phosphofructokinase-P, phosphohexokinase, TbPFK, TcPFK
ECTree
2.7.1.11 6-phosphofructokinaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.7.1.11 - 6-phosphofructokinase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.008
ATP
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.012
ATP
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.0151
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
0.017
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C
0.02
ATP
pH 7.2, 25°C, red blood cell lysate from diabetic subjects as source of enzyme
0.0232
ATP
-
mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0275
ATP
-
mutant enzyme S377A/K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0326
ATP
-
mutant enzyme K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0338
ATP
-
mutant enzyme H242A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0356
ATP
-
mutant enzyme K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0356
ATP
-
mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.037
ATP
-
mutant enzyme S377A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0382
ATP
-
mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0384
ATP
-
mutant enzyme K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0415
ATP
-
mutant enzyme S377A/K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0425
ATP
-
mutant enzyme R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0425
ATP
-
wild type enzyme, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.043
ATP
-
mutant enzyme S377A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0432
ATP
-
mutant enzyme R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0477
ATP
-
mutant enzyme R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.049
ATP
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
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
0.05
ATP
pH 7.2, 25°C, red blood cell lysate from diabetic subjects as source of enzyme
0.0508
ATP
-
mutant enzyme R246A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.051
ATP
-
purified enzyme, at pH 7.0, in the absence of D-fructose 2,6-bisphosphate
0.0524
ATP
-
mutant enzyme K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
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
0.063
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.0647
ATP
-
mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
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
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
0.07
ATP
-
wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C
0.076
ATP
-
purified enzyme, at pH 7.0, in the presence of 0.005 mM D-fructose 2,6-bisphosphate
0.076
ATP
N-terminal truncation mutant, presence of 5 mM AMP, pH 7.1, 25°C
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
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
0.114
ATP
-
mutant enzyme D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.114
ATP
-
mutant enzyme H242A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.117
ATP
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.141
ATP
-
mutant enzyme S377A/K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
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
0.166
ATP
-
mutant enzyme R246A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.168
ATP
-
mutant enzyme K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.168
ATP
-
mutant enzyme S377A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
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
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
0.22
ATP
-
mutant enzyme N341A/R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.234
ATP
-
mutant enzyme R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.25
ATP
-
mutant enzyme K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C
0.007
D-fructose 6-phosphate
-
mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.007
D-fructose 6-phosphate
-
mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.018
D-fructose 6-phosphate
-
wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.03
D-fructose 6-phosphate
-
pH 8.2, 30°C, at fructose 6-phosphate concentrations that are less than approx. one-third the fixed MgATP concentration
0.037
D-fructose 6-phosphate
-
wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication
0.096
D-fructose 6-phosphate
pH 7.2, 30°C, cosubstrate gamma-thio-ATP
0.29
D-fructose 6-phosphate
-
pH 7.15, 25°C, in the presence of 0.1 mM fructose 2,6-bisphosphate
0.29
D-fructose 6-phosphate
pH 7.2, 25°C, red blood cell lysate as source of enzyme
0.37
D-fructose 6-phosphate
-
pH 7.15, 25°C, in the presence of 1 mM AMP
0.37
D-fructose 6-phosphate
pH 7.2, 25°C, red blood cell lysate as source of enzyme
100
D-fructose 6-phosphate
pH 8.0, 25°C, mutant enzyme I153V
110
D-fructose 6-phosphate
pH 8.0, 25°C, mutant enzyme I150V
126
D-fructose 6-phosphate
pH 8.0, 25°C, wild-type enzyme
129
D-fructose 6-phosphate
pH 8.0, 25°C, mutant enzyme I234V
additional information
ADP
K0.5: 0.0668 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
ADP
K0.5: 0.0668 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
ADP
K0.5: 0.0668 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
ADP
K0.5: 0.3449 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
ADP
K0.5: 0.3449 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
ADP
K0.5: 0.3449 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.7178 mM, pH 7.4, 25°C, isoenzyme PFK-P
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.7178 mM, pH 7.4, 25°C, isoenzyme PFK-P
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.7178 mM, pH 7.4, 25°C, isoenzyme PFK-P
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.804 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.804 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
D-fructose 1,6-bisphosphate
K0.5: 0.804 mM, pH 7.4, 25°C, isoenzyme PFK-M
additional information
D-fructose 1,6-bisphosphate
K0.5: 1.287 mM, pH 7.4, 25°C
additional information
D-fructose 1,6-bisphosphate
K0.5: 1.54, pH 7.4, 25°C
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.1 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.1 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.1 mM, pH 7.4, 25°C, isoenzyme PFK-L
additional information
D-fructose 1,6-bisphosphate
K0.5: 2.495 mM, pH 7.4, 25°C
additional information
additional information
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kinetic study
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic data of various organism
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additional information
additional information
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kinetic properties of dansylated enzyme
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additional information
additional information
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oligomeric form exhibits negative cooperativity with fructose 6-phosphate
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additional information
additional information
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cooperativity with respect to fructose 6-phosphate
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additional information
additional information
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effects of low temperature and anoxia on kinetic constants
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additional information
additional information
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effects of temperature on kinetic properties
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additional information
additional information
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allosteric kinetics at alkaline pH-values
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additional information
additional information
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kinetic properties of phosphorylated enzyme
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additional information
additional information
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kinetic properties of phosphorylated enzyme
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additional information
additional information
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kinetic properties of phosphorylated enzyme
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additional information
additional information
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kinetic properties of phosphorylated enzyme
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additional information
additional information
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kinetic properties of phosphorylated enzyme
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additional information
additional information
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pH-dependence of kinetic properties of cytosolic and plastid isozymes
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additional information
additional information
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pH-dependence of kinetic properties of cytosolic and plastid isozymes
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additional information
additional information
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pH-dependence of kinetic properties of cytosolic and plastid isozymes
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additional information
additional information
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kinetic model of phosphofructokinase-1
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additional information
additional information
allosteric regulation. At saturating fructose 6-phoshate (5 mM), the Hill number for MgATP binding is 0.8
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additional information
additional information
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allosteric regulation. At saturating fructose 6-phoshate (5 mM), the Hill number for MgATP binding is 0.8
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