2.7.1.1: hexokinase
This is an abbreviated version!
For detailed information about hexokinase, go to the full flat file.
Word Map on EC 2.7.1.1
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2.7.1.1
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glucose-6-phosphate
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phosphofructokinase
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glycogen
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fructose
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citrate
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adp
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erythrocyte
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malate
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phosphorylase
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pancreatic
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hypoxia
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islet
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pentose
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creatine
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mellitus
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2-deoxyglucose
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aldolase
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hyperglycemia
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phosphoglucomutase
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warburg
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hypoxia-inducible
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6-phosphogluconate
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glut-1
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voltage-dependent
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vdacs
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streptozotocin
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positron
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soleus
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18f-fdg
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lateralis
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fructose-1,6-bisphosphatase
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hypoglycemic
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invertase
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2-deoxy-d-glucose
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fructokinase
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gluconeogenic
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insulin-stimulated
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carboxykinase
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hexoses
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vastus
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glycogenolysis
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g6pase
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glycosomes
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antihyperglycemic
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phosphoglucose
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18f-fluorodeoxyglucose
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fdg-pet
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pharmacology
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suvmax
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analysis
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glutaminolysis
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2,6-bisphosphate
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synthesis
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diagnostics
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industry
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medicine
- 2.7.1.1
- glucose-6-phosphate
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phosphofructokinase
- glycogen
- fructose
- citrate
- adp
- erythrocyte
- malate
- phosphorylase
- pancreatic
- hypoxia
- islet
- pentose
- creatine
- mellitus
- 2-deoxyglucose
- aldolase
- hyperglycemia
- phosphoglucomutase
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warburg
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hypoxia-inducible
- 6-phosphogluconate
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glut-1
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voltage-dependent
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vdacs
- streptozotocin
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positron
- soleus
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18f-fdg
- lateralis
- fructose-1,6-bisphosphatase
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hypoglycemic
- invertase
- 2-deoxy-d-glucose
- fructokinase
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gluconeogenic
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insulin-stimulated
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carboxykinase
- hexoses
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vastus
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glycogenolysis
- g6pase
- glycosomes
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antihyperglycemic
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phosphoglucose
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18f-fluorodeoxyglucose
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fdg-pet
- pharmacology
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suvmax
- analysis
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glutaminolysis
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2,6-bisphosphate
- synthesis
- diagnostics
- industry
- medicine
Reaction
Synonyms
6-phosphate glucose kinase, AtHXK1, ATP-D-hexose 6-phosphotransferase, ATP-D-hexose-6-phosphotransferase, ATP-dependent hexokinase, ATP: D-glucose 6-phosphotransferase, ATP: D-hexose 6-phosphotransferase, ATP:D-glucose 6-phosphotransferase, ATP:D-hexose 6-phosphotransferase, BmHk, brain form hexokinase, CzHXK1, FgHXK1, FgHXK2, GCK, GK, GKbeta, GlcK, glk, GlkB, glucokinase, glucokinase 1, glucokinase B, glucose ATP phosphotransferase, HaHXK1, hexokinase, hexokinase (phosphorylating), hexokinase 1, hexokinase 2, hexokinase 3, hexokinase 6, hexokinase A, hexokinase D, hexokinase Dor, hexokinase I, hexokinase II, hexokinase III, hexokinase IV, hexokinase PI, hexokinase PII, hexokinase type I, hexokinase type II, hexokinase type IV, hexokinase type IV glucokinase, hexokinase, tumor isozyme, hexokinase-1, hexokinase-10, hexokinase-2, hexokinase-4, hexokinase-5, hexokinase-6, hexokinase-7, hexokinase-8, hexokinase-9, hexokinase-II, hexokinase-like 1, hGK, hGK isoform 1, HK, HK II, HK-1, HK-I, HK-R, HK1, HK2, HK4, HKDC1, HKI, HKII, HKIII, HKL1, HPGLK1, HXK, HXK A, HXK II, Hxk1, HXK10, Hxk2, Hxk3, HXK4, HXK5, HXK6, HXK7, HXK8, HXK9, hxkC, hxkD, kinase, hexo- (phosphorylating), KlHxk1, LGK, LGK2, liver glucokinase, liver glucokinase isoform 2, MODY2 glucokinase, More, muscle form hexokinase, NfGlck, NtHXK1, OsHXK, OsHXK1, OsHXK10, OsHXK2, OsHXK3, OsHXK4, OsHXK5, OsHXK6, OsHXK7, OsHXK9, pHXK, plastid hexokinase, PpHXK1, PpHXK10, PpHXK11, PpHXK2, PpHXK3, PpHXK4, PpHXK5, PpHXK6, PpHXK7, PpHXK8, PpHXK9, Rag5p, ROK hexokinase, ScHK2, ScHXK2, SoHXK1, StHK, STK_23540, StoHK, TbHK1, TbHK2, TcHK, TthHK, type II hexokinase, VIT_18s0001g14230, xprF, Zm.5206, Zm.95484
ECTree
2.7.1.1 hexokinaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.7.1.1 - hexokinase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.00000023
ATP
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wild-type in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.0000003
ATP
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mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.00000035
ATP
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wild-type in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000049
ATP
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mutant W99R/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000055
ATP
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mutant W99R/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000057
ATP
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wild-type in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000071
ATP
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mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.00000071
ATP
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mutant W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.00000078
ATP
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mutant W99R/W257F, pH and temperature not specified in the publication
0.00000109
ATP
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mutant W167F/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000143
ATP
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mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000143
ATP
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mutant W99R/W167F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000163
ATP
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mutant W167F/W257F, pH and temperature not specified in the publication
0.00000294
ATP
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mutant W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000335
ATP
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mutant W99R/W167F, pH and temperature not specified in the publication
0.04
ATP
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wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 0.5 mM D-glucose
0.14
ATP
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enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
0.16
ATP
mutant enzyme V182L, glutathione S-transferase glucokinase B fusion protein
0.16
ATP
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wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 60 mM D-glucose
0.21
ATP
mutant enzyme Y61S, glutathione S-transferase glucokinase B fusion protein
0.31
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant 454-Ala
0.31
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G68V
0.32
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64P
0.32 - 0.38
ATP
natural and recombinant hexokinase, expressed in Escherichia coli XL-1 Blue, at pH 7.5
0.35
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A456V
0.35
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K140E
0.38
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V455M
0.39
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G68K
0.4
ATP
mutant enzyme E265K, glutathione S-transferase glucokinase B fusion protein
0.4
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197E
0.41
ATP
mutant enzyme K420E, glutathione S-transferase glucokinase B fusion protein
0.43 - 0.47
ATP
recombinant wild-type hexokinase I, D84A, D84E and D84K mutants
0.45
ATP
wild-type glutathione S-transferase glucokinase B fusion protein
0.46
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, wild-type
0.48
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V91L
0.5
ATP
mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C
0.52
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V62M
0.53
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V452L
0.57
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant T65I
0.58
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y215A
0.63
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S263P
0.66 - 1.2
ATP
wild-type and nonaggregating interface mutant hexokinase I, pH 7.8
0.69
ATP
mutant enzyme A379V, glutathione S-transferase glucokinase B fusion protein
0.7
ATP
wild type enzyme, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.72
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G72R
0.75
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant C252Y
0.76
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V389L
0.77
ATP
wild type enzyme, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.82
ATP
mutant enzyme V62M, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.85
ATP
mutant enzyme V62M, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
0.87
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A379T
0.89
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant C213R
0.92
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214A
1.08
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214C
1.1
ATP
mutant enzyme G72R, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
1.1
ATP
mutant enzyme G72R, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol
1.1 - 1.4
ATP
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MgATP2-, recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2
1.31
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197L
1.39
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I
1.42
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214A/V452A
1.5
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant E442K
1.53
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K414E
1.59
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64Y
2.08
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant P417R
2.71
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T
3.05
ATP
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catalytically active recombinant carboxyl-domain of hexokinase III, at 37°C, pH 8.1
3.32
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M298K
12.6
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S336L
6.49
D-fructose
pH 7.5, temperature not specified in the publication
0.035 - 0.038
D-glucose
recombinant wild-type hexokinase I, D84A, D84E and D84K mutants
0.038
D-glucose
-
catalytically active recombinant carboxyl-domain of hexokinase III, at 37°C, pH 8.1
0.04 - 0.06
D-glucose
-
pH and temperature not specified in the publication
0.057 - 0.061
D-glucose
wild-type and nonaggregating interface mutant hexokinase I, pH 7.8
0.059
D-glucose
-
enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
0.06
D-glucose
recombinant hexokinase expressed in Escherichia coli XL-1 Blue, at pH 7.5
0.06 - 0.065
D-glucose
-
recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2
0.062 - 0.065
D-glucose
-
bound and solubilized mitochondrial HK I, at pH 7.5
0.098
D-glucose
pH and temperature not specified in the publication
0.15
D-glucose
-
enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C
0.183
D-glucose
pH 7.5, temperature not specified in the publication
0.63
D-glucose
-
wild type enzyme, at 25°C, in the presence of 0.02 mM activator LY-2121260
0.76
D-glucose
-
wild type enzyme, at 25°C, in the presence of 0.02 mM activator N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine
2 - 3
D-glucose
-
enzyme from active animals, S0.5 value, Hill coefficient 1.16, pH 7.8, 2°C
2.5
D-glucose
deletion mutant lacking residues 68-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25 °C
3.1
D-glucose
deletion mutant lacking residue 71, K0.5 value, Hill coefficient 1.5, pH 7.6, 25 °C
3.2
D-glucose
deletion mutant lacking residues 67-71, K0.5 value, Hill coefficient 1.1, pH 7.6, 25 °C
3.3
D-glucose
mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C
3.6
D-glucose
deletion mutant lacking residues 66-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25 °C
6.23
D-glucose
-
enzyme from active animals, S0.5 value, Hill coefficient 1.7, pH 7.8, 25°C
9
D-glucose
-
enzyme from hibernating animals, S0.5 value, Hill coefficient 1.6, pH 7.8, 25°C
10.6
D-glucose
deletion mutant lacking residues 70-71, K0.5 value, Hill coefficient 1.3, pH 7.6, 25 °C
45
D-glucose
-
enzyme from hibernating animals, S0.5 value, Hill coefficient 1.2, pH 7.8, 2°C
0.109
D-mannose
pH 7.5, temperature not specified in the publication
0.32
N-acetyl-D-glucosamine
pH 7.5, 50°C, ATP as phosphoryl donor
additional information
additional information
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values for isoenzymes
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additional information
additional information
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of HXK1 mutants with modified active site
-
additional information
additional information
kinetics of isozyme hexokinase 2
-
additional information
additional information
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kinetics of isozyme hexokinase 2
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additional information
additional information
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kinetics, mass spectrometry-based assay, overview, the Mg2+ concentration influence the kinetics
-
additional information
additional information
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non-cooperative conditions shows an ordered, ternary-complex mechanism with MgADP- as the last product to be released, hyperbolic kinetics with both 2-deoxyglucose and MgATP2-
-
additional information
additional information
positive cooperation, mechanism, kinetic model
-
additional information
additional information
stopped-flow steady-state kinetics, dissociation constants of the monomer-homodimer equilibria
-
additional information
additional information
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stopped-flow steady-state kinetics, dissociation constants of the monomer-homodimer equilibria
-
additional information
additional information
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wild-type and mutant enzymes, cooperative/sigmoidal glucose-dependent kinetics
-
additional information
additional information
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osmolytes decrease kcat/KM in the order of decreasing efficiency NaCl, urea, trimethylamine N-oxide/glycerol, betaine. For the organic osmolytes this order correlates with the degree of exclusion from protein/water interfaces
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additional information
additional information
kinetic parameters of hexokinase activity in wine yeast strains
-
additional information
additional information
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kinetic parameters of hexokinase activity in wine yeast strains
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additional information
additional information
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the osmolytes decreases kcat/KM in the order: NaCl/urea/trimethylamine-N-oxide dehydrate/glycerol/betaine. For the organic osmolytes this order correlates with the degree of exclusion from protein-water interfaces. Thus, the stronger the exclusion the weaker the perturbing effects on kcat/KM
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