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
-
hypoxia-inducible
- 6-phosphogluconate
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glut-1
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voltage-dependent
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vdacs
- streptozotocin
-
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
-
vastus
-
glycogenolysis
- g6pase
- glycosomes
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antihyperglycemic
-
phosphoglucose
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18f-fluorodeoxyglucose
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fdg-pet
- pharmacology
-
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
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results (Turnover Number
Turnover Number on EC 2.7.1.1 - hexokinase
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TURNOVER NUMBER [1/s] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.7
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
68.4
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
5.9
beta-D-glucose
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co-substrate: ATP, 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
6.1
beta-D-glucose
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co-substrate: ATP, mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
6.37
beta-D-glucose
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co-substrate: ATP, mutant W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
8.47
beta-D-glucose
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co-substrate: ATP, mutant W167F/W257F, pH and temperature not specified in the publication
9.43
beta-D-glucose
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co-substrate: ATP, 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
11.1
beta-D-glucose
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co-substrate: ATP, mutant W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
12.4
beta-D-glucose
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co-substrate: ATP, mutant W99R/W167F, pH and temperature not specified in the publication
12.7
beta-D-glucose
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co-substrate: ATP, mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
26.2
beta-D-glucose
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co-substrate: ATP, mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
37.7
beta-D-glucose
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co-substrate: ATP, wild-type in the presence of 20-30% glycerol, pH and temperature not specified in the publication
38.9
beta-D-glucose
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co-substrate: ATP, 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
60.5
beta-D-glucose
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co-substrate: ATP, 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
69.9
beta-D-glucose
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co-substrate: ATP, mutant W99R/W257F, pH and temperature not specified in the publication
83.7
beta-D-glucose
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co-substrate: ATP, wild-type, pH and temperature not specified in the publication
91.3
beta-D-glucose
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co-substrate: ATP, mutant W99R/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
166
beta-D-glucose
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co-substrate: ATP, wild-type in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.02
D-fructose
pH 7.5, temperature not specified in the publication
2.46
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S336L
17.7
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197E
19.9
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K414E
20.5
D-glucose
pH 7.5, temperature not specified in the publication
22.6
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant T65I
23.1
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214A/V452A
24
D-glucose
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
29.3
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant C252Y
29.8
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G72R
34
D-glucose
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
37.7
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M298K
40
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K140E
43.2
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G68K
44.6
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S263P
44.7
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y215A
47.2
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V62M
48.3
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant P417R
50
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant C213R
50.2
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T
52.2
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant 454-Ala
52.6
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant E442K
54
D-glucose
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
56
D-glucose
mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C
58.1
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I
60.6
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V91L
61
D-glucose
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
61.2
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A379T
61.8
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V455M
62.6
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197L
62.7
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G68V
62.8
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, wild-type
64
D-glucose
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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
65.3
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214C
65.6
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A456V
67.1
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V389L
74
D-glucose
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
75
D-glucose
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wild type enzyme, at 25°C, in the presence of 0.02 mM activator LY-2121260
83.3
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64P
101
D-glucose
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
114
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64Y
117
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214A
122
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V452L
12.1
D-mannose
pH 7.5, temperature not specified in the publication
additional information
additional information
6000/min, wild-type and nonaggregating interface mutant hexokinase I
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additional information
additional information
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6000/min, wild-type and nonaggregating interface mutant hexokinase I
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additional information
additional information
natural hexokinase: 68160/min, recombinant hexokinase expressed in Escherichia coli XL-1 Blue: 18913/min, at pH 7.5
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additional information
additional information
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natural hexokinase: 68160/min, recombinant hexokinase expressed in Escherichia coli XL-1 Blue: 18913/min, at pH 7.5
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additional information
additional information
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as the temperature is raised from 30°C to 47.5°C kcat decreases, falling to about 10 per sec (by 80%) at 50°C
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additional information
additional information
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osmolytes decrease kcat/KM in the order ofedecreasing efficiency NaCl, urea, trimethylamine N-oxide/glycerol, betains. 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
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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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