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2'-dATP + D-glucose
2'-dADP + D-glucose 6-phosphate
2-fluoro-2-deoxy-D-glucose + ATP
2-fluoro-2-deoxy-D-glucose 6-phosphate + ADP
ATP + 1,5-anhydro-D-glucitol
ADP + 1,5-anhydro-D-glucitol 6-phosphate
-
weak
-
-
?
ATP + 1-thio-D-glucose
ADP + 1-thio-D-glucose 6-phosphate
-
isoenzyme II, weak
-
-
?
ATP + 2-deoxy-2-fluoro-D-glucose
ADP + 2-deoxy-2-fluoro-D-glucose 6-phosphate
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
ATP + 3-deoxy-3-amino-D-glucose
ADP + 3-deoxy-3-amino-D-glucose 6-phosphate
-
isoenzyme II, weak
-
-
?
ATP + 5-thio-D-glucose
ADP + 5-thio-D-glucose 6-phosphate
ATP + beta-D-glucose
ADP + beta-D-glucose 6-phosphate
-
-
-
-
?
ATP + D-allose
ADP + D-allose 6-phosphate
ATP + D-fructose
?
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
ATP + D-galactose
?
Q56VN6
-
-
-
?
ATP + D-galactose
ADP + D-galactose 6-phosphate
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
ATP + D-glucose
ADP + D-glucose 6-phosphate
ATP + D-hexose
ADP + D-hexose 6-phosphate
-
-
-
-
?
ATP + D-maltose
?
Q56VN6
-
-
-
?
ATP + D-mannosamine
ADP + D-mannosamine 6-phosphate
ATP + D-mannose
?
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
ATP + hexose
ADP + hexose 6-phosphate
-
-
-
-
?
ATP + mannoheptulose
?
-
sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
-
-
?
ATP + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 6-phosphate
-
sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
-
-
?
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
D-fructose + ATP
ADP + D-fructose 6-phosphate
D-fructose + ATP
D-fructose 6-phosphate + ADP
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
D-glucose + ATP
ADP + D-glucose 6-phosphate
D-glucose + ATP
D-glucose 6-phosphate + ADP
D-mannose + ATP
ADP + D-mannose 6-phosphate
GTP + D-glucose
GDP + D-glucose 6-phosphate
hexose + ATP
ADP + hexose 6-phosphate
-
-
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
N-acetyl-D-glucosamine + ATP
ADP + N-acetyl-D-glucosamine 6-phosphate
-
erythrocyte enzyme, 32.6% of the activity with glucose
-
-
?
TTP + D-glucose
TDP + D-glucose 6-phosphate
UTP + D-glucose
UDP + D-glucose 6-phosphate
additional information
?
-
2'-dATP + D-glucose
2'-dADP + D-glucose 6-phosphate
-
73-80% of the activity with ATP, isoenzyme Hex A, B, C
-
-
?
2'-dATP + D-glucose
2'-dADP + D-glucose 6-phosphate
-
73% of the activity with ATP
-
-
?
2'-dATP + D-glucose
2'-dADP + D-glucose 6-phosphate
-
Hex A: 73% of the activity with ATP, Hex B: 76% of the activity with ATP, Hex C: 80% of the activity with ATP
-
-
?
2-fluoro-2-deoxy-D-glucose + ATP
2-fluoro-2-deoxy-D-glucose 6-phosphate + ADP
-
-
-
?
2-fluoro-2-deoxy-D-glucose + ATP
2-fluoro-2-deoxy-D-glucose 6-phosphate + ADP
-
-
-
?
ATP + 2-deoxy-2-fluoro-D-glucose
ADP + 2-deoxy-2-fluoro-D-glucose 6-phosphate
-
-
-
?
ATP + 2-deoxy-2-fluoro-D-glucose
ADP + 2-deoxy-2-fluoro-D-glucose 6-phosphate
-
good substrate
-
-
?
ATP + 2-deoxy-2-fluoro-D-glucose
ADP + 2-deoxy-2-fluoro-D-glucose 6-phosphate
-
good substrate
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
30% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
Hex A: 93% of the activity with glucose, Hex B: 51% of the activity with glucose, Hex C: 48% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
93% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
Hex A: 93% of the activity with glucose, Hex B: 51% of the activity with glucose, Hex C: 48% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
Hex Ia: 95% of the activity with glucose, Hex Ib: 99% of the activity with glucose, Hex Ic: 74% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
hexokinase I: as effective as glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
17% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
hexokinase Ia: 65% of the activity with glucose, hexokinase Ib: 70% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
54% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
65.7% of the activity with glucose, erythrocyte enzyme
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
84% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
hexokinase III: 151% of the activity with glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
42% of the activity with D-glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
42% of the activity with D-glucose
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
-
-
?
ATP + 5-thio-D-glucose
ADP + 5-thio-D-glucose 6-phosphate
-
very slow phosphorylation
-
-
?
ATP + 5-thio-D-glucose
ADP + 5-thio-D-glucose 6-phosphate
-
very slow phosphorylation
-
-
?
ATP + D-allose
ADP + D-allose 6-phosphate
-
phosphorylation of D-allose at C6 by hexokinase is essential since it up-regulates expression of transcription factor OsABF1
-
-
?
ATP + D-allose
ADP + D-allose 6-phosphate
58% of the activity with D-glucose
-
-
?
ATP + D-allose
ADP + D-allose 6-phosphate
58% of the activity with D-glucose
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
isozyme HKI, isozyme HKII is highly specific for D-fructose
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
Q56VN6
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
16.6% of the activity with ATP
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
8.6% of the activity with ATP
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
8.6% of the activity with ATP
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
best substrate
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
16% of the activity with D-glucose
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
-
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
8% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
67% of the activity with D-glucose
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
67% of the activity with D-glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
involved in glucose catabolism
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
isozyme HKI
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
Q56VN6
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
ATP is the preferred nucleside triphosphate
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
ATP is the preferred nucleside triphosphate
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
641067, 641068, 660810, 660963, 663393, 672188, 672225, 674421, 674942, 677004, 702116, 702119, 702140, 702236, 702314, 702320, 702572, 702666, 703358, 703959, 721535, 721827, 721837, 722237, 723509 -
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
enzyme plays a key role in whole-body glucose homeostasis
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the pancreatic enzyme is imporatnt as glucose sensor in insulin secretion and blood glucose homeostasis, interaction of ATP and glucose during binding to the enzyme
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
control of GK activity and Km through the ratio of distinct conformers (super-open, open, and closed) through either substrate or other ligand binding and/or dissociation
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
hexokinase II displays high affinity for D-glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
under physiological conditions D-glucose is the preferred substrate
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
first step in glucose metabolism, pathway overview, isozyme types are differently regulated and catalytically active, isozyme type I is involved in catabolism, while type II and III are involved in anabolism, the activity rate of type I isozyme i correlated with the oxidative phosphorylation rate, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
isozyme hexokinase 2 plays a role in starch and secondary metabolism in starch sheath, xylem parenchyma, guard cells, and root tips
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
enzyme mediates glucose repression
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
39% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
641070, 641071, 641072, 660949, 660963, 663393, 701997, 702116, 702556, 703129, 704456, 704831, 705268, 705294, 706889 -
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
first step in the process of glycolysis
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the presence of 0.5 mM glucose induced total hexokinase activity in supernatants from sperm extracts of 1.7 mIU/mg protein, while the same concentration of both fructose, mannose, and sorbitol induced total hexokinase activity from 0.3 mIU/mg protein to 0.60 IU/mg protein. Diluted boar sperm from fresh ejaculates phosphorylates glucose through the hexokinase step much more efficiently than fructose or mannose. This difference facilitates a much more rapid intake of glucose into glycolysis than the other sugars
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
best substrate
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
best substrate
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the enzyme shows a narrow substrate specificity, as it does not display activity towards fructose, mannose or galactose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-mannosamine
ADP + D-mannosamine 6-phosphate
-
fairly good substrate
-
-
?
ATP + D-mannosamine
ADP + D-mannosamine 6-phosphate
-
fairly good substrate
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
Q56VN6
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
97% of the activity with ATP
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
52% of the activity with ATP
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
52% of the activity with ATP
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
poor substrate
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
33% of activity with D-fructose at 50 mM substrate concentration
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
75% of the activity with D-glucose
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
11% of the activity with ATP, isoenzyme Hex C, not: isoenzyme Hex A and Hex B
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
35% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
35% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
18% of the activity with ATP
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
Hex B: 5% of the activity with ATP, Hex C: 11% of the activity with ATP, not Hex A
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
MgCTP, hexokinase I: 5% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
35% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
81% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
46.3% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
Hex A: 50% of the activity with glucose, Hex B: 41% of the activity with glucose, Hex C: 134% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
50% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
Hex A: 50% of the activity with glucose, Hex B: 41% of the activity with glucose, Hex C: 134% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
50% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
hexokinase I: 130% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
Hex Ia: 100% of the activity with glucose, Hex Ib: 120% of the activity with glucose, Hex Ic: 90% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
70% of the activity with glucose, erythrocyte enzyme
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
hexokinase Ia: 69% of the activity with glucose, hexokinase Ib: 42% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
110% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
poor substrate
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
hexokinase C
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
hexokinases PI and PII phosphorylate fructose 2.5 and 1.5times faster than glucose, glucokinase: very low or no activity
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
hexokinases PI and PII phosphorylate fructose 2.5 and 1.5times faster than glucose, glucokinase: very low or no activity
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
higher activity than with glucose or mannose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
higher activity than with glucose or mannose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
higher activity than with glucose or mannose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
hexokinase, but not glucokinase
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
HK3: 16% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
HK1: 4% of the activity with glucose, HK2: 3% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
HK3: 5% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
hexokinase III: 12.6% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
79% of the activity with glucose
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
?
D-fructose + ATP
ADP + D-fructose 6-phosphate
-
-
-
-
?
D-fructose + ATP
D-fructose 6-phosphate + ADP
-
fructose metabolism
-
?
D-fructose + ATP
D-fructose 6-phosphate + ADP
-
-
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
44.9% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
Hex A: 19% of the activity with glucose, Hex C: 44% of the activity with glucose, not Hex B
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
Hex A: 19% of the activity with glucose, Hex C: 44% of the activity with glucose, not Hex B
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
-
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
Hex Ia and Ib: 47% of the activity with glucose, Hex Ic: 21% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
hexokinase I: 40% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
-
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
hexokinase Ia: 35% of the activity with glucose, hexokinase Ib: 70% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
erythrocyte enzyme, 43.4% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
-
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
hexokinase III: 35% of the activity with glucose
-
-
?
D-glucosamine + ATP
ADP + D-glucosamine 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
hexokinase bound at type A and B sites of brain mitochondria selectively uses intramitochondrial ATP as substrate, but hexokinase bound at type B sites, after removal of enzyme of type A sites, shows no such selectivity
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
specific for ATP
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
the binding of glucose does not depend on ATP, and vice versa
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
the binding of glucose does not depend on ATP, and vice versa
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
good substrate
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
good substrate
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
bound glucose is present as the beta-anomer, glucose binding sites
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
absolute requirement for D-glucose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
MgATP2-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
good substrate
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
11% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
59% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
11% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
59% of the activity with fructose
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
hexokinase and glucokinase
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
preferred specificity for glucose
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
specific for ATP
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
preferred specificity for glucose
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
-
-
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
specific for glucose
-
?
D-glucose + ATP
ADP + D-glucose 6-phosphate
-
most active with D-glucose
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
cerebral glycolytic metabolism, mechanisms for regulation of mitochondrial hexokinase activity may depend on the ratio of type A:type B sites
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
isoenzymes are a target for effective control of glucose 6-phosphate formation by energy charge of the cell or by the intracellular level of ATP, ADP and glucose instead of allosteric interconversions of the enzyme
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
at high energy charge HXK1 may be involved in glycolysis and in some biosynthetic processes, e.g. phosphorylating mannose or glucose for the later integration into membrane components, at low energy charge HXK1 could be inhibited by AMP and ADP, and HXK2 would be more active and could keep up glucokinase activity for glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
hexokinase I governs the rate-limiting step of glycolysis in brain
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
hexokinase I is the pacemaker of glycolysis in brain tissue
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
hexokinase I is a regulated enzyme and serves a critical role in controlling the rate of glycolysis in both brain and red blood cells
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
key enzyme in the control of brain glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
binding of brain enzyme to the outer mitochondrial membrane plays a role in regulation of hexokinase activity in vivo, and thereby of the cerebral glycolytic rate
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial catalytic step of the cerebral glucose metabolism, glucose 6-phosphate represents a major regulatory influence on the in vivo activity
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
hexokinase isoenzymes are particularly important in glycolytic flux and, in addition, hexokinase PII, hexokinase PIIM or both are also responsible for the overall regulation of carbohydrate metabolism, role in glucose repression
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
organ- and development-specific changes in the abundance of the various enzyme forms contribute to the regulation of hexose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
the presence of type III hexokinase enables the adult pig erythrocytes to metabolize low but appreciable amounts of glucose
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
carbohydrate metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
first step of the glycolytic pathway, physiological function of membrane-bound hexokinase in the tachyzoite: glucose channeling with a glucose/hexose transporter
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
rate-limiting step in the glycolysis
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
rate-limiting step in the glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
glycolytic enzyme
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
27.2% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
Hex A: 100% of the activity with glucose, Hex B: 98% of the activity with glucose, Hex C: 44% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
Hex A: 100% of the activity with glucose, Hex B: 98% of the activity with glucose, Hex C: 44% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
HXK1: good substrate, HXK2: much lower phosphorylation rate than of HXK1
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
HXK1: good substrate, HXK2: much lower phosphorylation rate than of HXK1
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
Hex Ia: 78% of the activity with glucose, Hex Ib: 83% of the activity with glucose, Hex Ic: 85% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
hexokinase I: 106% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
82% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
109% of the activity with glucose, erythrocyte enzyme
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
104-105% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
good substrate
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
glucokinase
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
glucokinase
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
42% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
23% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
23% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
42% of the activity with fructose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
HK1: 53% of the activity with glucose, HK2: 22% of the activity with glucose, HK3: 45% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
hexokinase III: 85% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
55% of the activity with glucose
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
?
D-mannose + ATP
ADP + D-mannose 6-phosphate
-
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
19% of the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
19% of the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
-
14% of the activity with ATP
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
-
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
52% of the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
18% of the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
can partially replace ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
-
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
-
35% of the activity with ATP
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
13.5-14% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
MgITP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
hexokinase I: 9% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
30% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
12% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
36% of the activity with ATP, erythrocyte enzyme
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
MgITP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
64% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
64% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
hexokinase III: 24% of the activity with glucose
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
MgITP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
40% of the activity with ATP
-
-
?
TTP + D-glucose
TDP + D-glucose 6-phosphate
-
-
21% of the activity with ATP
-
?
TTP + D-glucose
TDP + D-glucose 6-phosphate
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
23% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
23% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
-
13% of the activity with ATP
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
hexokinase I: 5% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
MgUTP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
14% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
MgUTP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
-
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
37% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
17% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
can partially replace ATP
-
-
?
additional information
?
-
-
not: UTP
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
the active site is located in the C-terminal domain
-
-
?
additional information
?
-
-
the active site is located in the C-terminal domain
-
-
?
additional information
?
-
hexokinase, Hxk1, but not the glucokinase, Glk1, is required for normal growth and sugar metabolism, and for pathogenicity on fruits
-
-
?
additional information
?
-
-
hexokinase, Hxk1, but not the glucokinase, Glk1, is required for normal growth and sugar metabolism, and for pathogenicity on fruits
-
-
?
additional information
?
-
-
not: UTP
-
-
?
additional information
?
-
-
not: N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: CTP
-
-
?
additional information
?
-
-
not: UTP
-
-
?
additional information
?
-
-
not: ITP
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
no substrates: D-galactose, sorbose. TTP, UTP, CTP and GTP show 6.5%-17.1% of the activity with ATP
-
-
?
additional information
?
-
-
no substrates: D-galactose, sorbose. TTP, UTP, CTP and GTP show 6.5%-17.1% of the activity with ATP
-
-
?
additional information
?
-
no substrates: D-galactose, sorbose. TTP, UTP, CTP and GTP show 6.5%-17.1% of the activity with ATP
-
-
?
additional information
?
-
no substrate: D-galactose
-
-
?
additional information
?
-
-
no substrate: D-galactose
-
-
?
additional information
?
-
-
not: fructose
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
not: fructose
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
not: UTP
-
-
?
additional information
?
-
-
structure model of hexokinase I
-
-
?
additional information
?
-
structure model of hexokinase I
-
-
?
additional information
?
-
-
structure model of hexokinase I
-
-
?
additional information
?
-
-
not: N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
role of the hexokinase III carboxyl-domain in determining the catalytic properties of enzyme
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
the 50 kDa C-terminal half of HK I contains the catalytic domain, the N-terminal half is catalytically inactive
-
-
?
additional information
?
-
-
C-terminal catalytic and N-terminal regulatory domain, detailed structure of hexokinase I, substrate binding sites, models for regulation
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: CTP
-
-
?
additional information
?
-
-
loss of enzyme activity is involved in type 2 diabetes mellitus
-
-
?
additional information
?
-
-
biophysical characterization of the interaction between GK and GKRP and its modulation by physiological and pharmacological effectors
-
-
?
additional information
?
-
the enzyme is the only glucose and fructose phosphorylating enzyme, which is upregulating glucose transport and also mediating glucose repression
-
-
?
additional information
?
-
-
the enzyme is the only glucose and fructose phosphorylating enzyme, which is upregulating glucose transport and also mediating glucose repression
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
the 100 kDa isozymes, displaying internal sequence repetition, may have evolved by gene duplication of a 50 kDa ancestor
-
-
?
additional information
?
-
-
sperm hexokinase p95/116 may serve as cell surface receptor kinase for the zona pellucida glycoprotein ZP3
-
-
?
additional information
?
-
-
glucokinase regulates reproductive function, glucocorticoid secretion, food intake, and hypothalamic gene expression
-
-
?
additional information
?
-
-
role of a bound glucokinase protein fraction in the regulation of insulin granule movement along tubulin filaments
-
-
?
additional information
?
-
no activity with D-xylose, D-galactose, and methyl-alpha-D-glucoside
-
-
?
additional information
?
-
-
no activity with D-xylose, D-galactose, and methyl-alpha-D-glucoside
-
-
?
additional information
?
-
-
not: UTP
-
-
?
additional information
?
-
-
not: N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
not: N-acetyl-D-glucosamine
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: CTP
-
-
?
additional information
?
-
-
not: CTP
-
-
?
additional information
?
-
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
-
ligand binding sites in the N- and C-terminal halves and interactions between these sites
-
-
?
additional information
?
-
structure model of hexokinase I
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
allosteric regulation of hexokinase I, the functional regulatory glucose 6-phosphate binding site is located in the N-terminal half
-
-
?
additional information
?
-
-
isolated catalytically active 51 kDa C-fragment and 52 kDa N-fragment without catalytic activity, both fragments contain discrete binding sites for hexoses and hexose 6-phosphates, one of each pair of sites must be latent in the intact enzyme, the regulatory site binding glucose 6-phosphate is associated with the N-terminal half
-
-
?
additional information
?
-
-
not: trehalose
-
-
?
additional information
?
-
hexokinase I and hexokinase II are independently regulated, implying that they perform different roles in cardiac glucose regulation
-
-
?
additional information
?
-
hexokinase I and hexokinase II are independently regulated, implying that they perform different roles in cardiac glucose regulation
-
-
?
additional information
?
-
-
the enzyme plays a role in glycogen synthesis and glucose homeostasis
-
-
?
additional information
?
-
-
glucokinase: not: fructose, galactose, sorbose, rhamnose, arabinose, mannitol, sorbitol, ribose
-
-
?
additional information
?
-
-
not: N-acetylmannosamine, 6-deoxy-6-aminoglucose
-
-
?
additional information
?
-
-
allosteric enzyme, catalyzes phosphoryl transfer from MgATP2- to the 6-OH group of a number of furanose- and pyranose-type compounds
-
-
?
additional information
?
-
-
hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
?
additional information
?
-
-
relatively nonspecific enzyme
-
-
?
additional information
?
-
G/F discrepancy in Saccharomyces cerevisiae is not related to the maximal hexokinase activity in vitro with glucose or fructose as substrate or to the ratio between the Km values for glucose and fructose phosphorylation but might rather be related to the actual fructose phosphorylating activity at physiological fructose levels in vivo
-
-
?
additional information
?
-
-
G/F discrepancy in Saccharomyces cerevisiae is not related to the maximal hexokinase activity in vitro with glucose or fructose as substrate or to the ratio between the Km values for glucose and fructose phosphorylation but might rather be related to the actual fructose phosphorylating activity at physiological fructose levels in vivo
-
-
?
additional information
?
-
-
glucokinase: not: fructose, galactose, sorbose, rhamnose, arabinose, mannitol, sorbitol, ribose
-
-
?
additional information
?
-
-
hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
?
additional information
?
-
galactose is phosphorylated at rates of 0.8 and 0.08 U/mg at concentrations of 1 and 10 mM, respectively. Ribose, xylose, N-acetylmannosamine, glucose-1-phosphate, and fructose-6-phosphate (10 mM) are not phosphorylated by the enzyme
-
-
?
additional information
?
-
-
galactose is phosphorylated at rates of 0.8 and 0.08 U/mg at concentrations of 1 and 10 mM, respectively. Ribose, xylose, N-acetylmannosamine, glucose-1-phosphate, and fructose-6-phosphate (10 mM) are not phosphorylated by the enzyme
-
-
?
additional information
?
-
galactose is phosphorylated at rates of 0.8 and 0.08 U/mg at concentrations of 1 and 10 mM, respectively. Ribose, xylose, N-acetylmannosamine, glucose-1-phosphate, and fructose-6-phosphate (10 mM) are not phosphorylated by the enzyme
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
not: UTP
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
-
not: CTP
-
-
?
additional information
?
-
not: ADP
-
-
?
additional information
?
-
-
not: ADP
-
-
?
additional information
?
-
not: ribose, xylose, phosphorylated hexoses, UDP, polyphosphates
-
-
?
additional information
?
-
-
not: ribose, xylose, phosphorylated hexoses, UDP, polyphosphates
-
-
?
additional information
?
-
not: D-galactose
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
not: CTP
-
-
?
additional information
?
-
-
not: CTP
-
-
?
additional information
?
-
no activity with D-galactose and N-acetylglucosamine, enzyme shows broad substrate specificity, specificity probably depends on the interaction energy occurring by the positional proximity of sugars bound in the active site
-
-
?
additional information
?
-
no activity with D-galactose and N-acetylglucosamine, enzyme shows broad substrate specificity, specificity probably depends on the interaction energy occurring by the positional proximity of sugars bound in the active site
-
-
?
additional information
?
-
-
no activity with D-galactose and N-acetylglucosamine, enzyme shows broad substrate specificity, specificity probably depends on the interaction energy occurring by the positional proximity of sugars bound in the active site
-
-
?
additional information
?
-
the enzyme shows little catalytic capacity for galactose and fructose
-
-
?
additional information
?
-
-
the enzyme shows little catalytic capacity for galactose and fructose
-
-
?
additional information
?
-
the enzyme shows little catalytic capacity for galactose and fructose
-
-
?
additional information
?
-
not: ADP
-
-
?
additional information
?
-
-
not: ADP
-
-
?
additional information
?
-
not: UTP
-
-
?
additional information
?
-
-
not: UTP
-
-
?
additional information
?
-
not: diphosphate
-
-
?
additional information
?
-
-
not: diphosphate
-
-
?
additional information
?
-
not: D-galactose
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
additional information
?
-
not: ITP
-
-
?
additional information
?
-
-
not: ITP
-
-
?
additional information
?
-
not: GTP
-
-
?
additional information
?
-
-
not: GTP
-
-
?
additional information
?
-
not: CTP
-
-
?
additional information
?
-
-
not: CTP
-
-
?
additional information
?
-
not: ADP
-
-
?
additional information
?
-
not: UTP
-
-
?
additional information
?
-
not: diphosphate
-
-
?
additional information
?
-
not: D-galactose
-
-
?
additional information
?
-
not: ITP
-
-
?
additional information
?
-
the C-terminal tail of TbHK1 is important for hexokinase activity
-
-
?
additional information
?
-
-
the C-terminal tail of TbHK1 is important for hexokinase activity
-
-
?
additional information
?
-
not: diphosphate
-
-
?
additional information
?
-
-
not: diphosphate
-
-
?
additional information
?
-
not: mannose
-
-
?
additional information
?
-
-
not: mannose
-
-
?
additional information
?
-
not: fructose
-
-
?
additional information
?
-
-
not: fructose
-
-
?
additional information
?
-
not: D-galactose
-
-
?
additional information
?
-
-
not: D-galactose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + D-fructose
ADP + D-fructose 6-phosphate
ATP + D-glucose
ADP + D-glucose 6-phosphate
ATP + D-mannose
ADP + D-mannose 6-phosphate
ATP + hexose
ADP + hexose 6-phosphate
-
-
-
-
?
D-fructose + ATP
D-fructose 6-phosphate + ADP
-
fructose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
additional information
?
-
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
involved in glucose catabolism
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
enzyme plays a key role in whole-body glucose homeostasis
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the pancreatic enzyme is imporatnt as glucose sensor in insulin secretion and blood glucose homeostasis, interaction of ATP and glucose during binding to the enzyme
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
control of GK activity and Km through the ratio of distinct conformers (super-open, open, and closed) through either substrate or other ligand binding and/or dissociation
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
first step in glucose metabolism, pathway overview, isozyme types are differently regulated and catalytically active, isozyme type I is involved in catabolism, while type II and III are involved in anabolism, the activity rate of type I isozyme i correlated with the oxidative phosphorylation rate, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
isozyme hexokinase 2 plays a role in starch and secondary metabolism in starch sheath, xylem parenchyma, guard cells, and root tips
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
enzyme mediates glucose repression
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
first step in the process of glycolysis
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
in Sulfolobus tokodaii this is the sole enzyme responsible for the phosphorylation of glucose in vivo
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the presence of 0.5 mM glucose induced total hexokinase activity in supernatants from sperm extracts of 1.7 mIU/mg protein, while the same concentration of both fructose, mannose, and sorbitol induced total hexokinase activity from 0.3 mIU/mg protein to 0.60 IU/mg protein. Diluted boar sperm from fresh ejaculates phosphorylates glucose through the hexokinase step much more efficiently than fructose or mannose. This difference facilitates a much more rapid intake of glucose into glycolysis than the other sugars
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
-
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
cerebral glycolytic metabolism, mechanisms for regulation of mitochondrial hexokinase activity may depend on the ratio of type A:type B sites
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
isoenzymes are a target for effective control of glucose 6-phosphate formation by energy charge of the cell or by the intracellular level of ATP, ADP and glucose instead of allosteric interconversions of the enzyme
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
at high energy charge HXK1 may be involved in glycolysis and in some biosynthetic processes, e.g. phosphorylating mannose or glucose for the later integration into membrane components, at low energy charge HXK1 could be inhibited by AMP and ADP, and HXK2 would be more active and could keep up glucokinase activity for glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
hexokinase I governs the rate-limiting step of glycolysis in brain
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
hexokinase I is the pacemaker of glycolysis in brain tissue
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
hexokinase I is a regulated enzyme and serves a critical role in controlling the rate of glycolysis in both brain and red blood cells
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial enzyme of glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
key enzyme in the control of brain glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
binding of brain enzyme to the outer mitochondrial membrane plays a role in regulation of hexokinase activity in vivo, and thereby of the cerebral glycolytic rate
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
initial catalytic step of the cerebral glucose metabolism, glucose 6-phosphate represents a major regulatory influence on the in vivo activity
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
hexokinase isoenzymes are particularly important in glycolytic flux and, in addition, hexokinase PII, hexokinase PIIM or both are also responsible for the overall regulation of carbohydrate metabolism, role in glucose repression
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
enzyme of the glucose-phosphate branch of the oxidative pentose phosphate pathway
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glucose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
organ- and development-specific changes in the abundance of the various enzyme forms contribute to the regulation of hexose metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
the presence of type III hexokinase enables the adult pig erythrocytes to metabolize low but appreciable amounts of glucose
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
carbohydrate metabolism
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
first step of the glycolytic pathway, physiological function of membrane-bound hexokinase in the tachyzoite: glucose channeling with a glucose/hexose transporter
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
rate-limiting step in the glycolysis
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
rate-limiting step in the glycolysis
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
-
glycolytic enzyme
-
-
?
D-glucose + ATP
D-glucose 6-phosphate + ADP
glycolytic enzyme
-
-
?
additional information
?
-
hexokinase, Hxk1, but not the glucokinase, Glk1, is required for normal growth and sugar metabolism, and for pathogenicity on fruits
-
-
?
additional information
?
-
-
hexokinase, Hxk1, but not the glucokinase, Glk1, is required for normal growth and sugar metabolism, and for pathogenicity on fruits
-
-
?
additional information
?
-
-
loss of enzyme activity is involved in type 2 diabetes mellitus
-
-
?
additional information
?
-
the enzyme is the only glucose and fructose phosphorylating enzyme, which is upregulating glucose transport and also mediating glucose repression
-
-
?
additional information
?
-
-
the enzyme is the only glucose and fructose phosphorylating enzyme, which is upregulating glucose transport and also mediating glucose repression
-
-
?
additional information
?
-
-
the 100 kDa isozymes, displaying internal sequence repetition, may have evolved by gene duplication of a 50 kDa ancestor
-
-
?
additional information
?
-
-
sperm hexokinase p95/116 may serve as cell surface receptor kinase for the zona pellucida glycoprotein ZP3
-
-
?
additional information
?
-
-
glucokinase regulates reproductive function, glucocorticoid secretion, food intake, and hypothalamic gene expression
-
-
?
additional information
?
-
-
role of a bound glucokinase protein fraction in the regulation of insulin granule movement along tubulin filaments
-
-
?
additional information
?
-
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK2 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK5 expression appears to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
OsHXK6 expression appeared to be significantly upregulated in rice leaves by glucose and fructose
-
-
?
additional information
?
-
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
OsHXK8 may function in the endosperm in the filling phase of rice seed development
-
-
?
additional information
?
-
hexokinase I and hexokinase II are independently regulated, implying that they perform different roles in cardiac glucose regulation
-
-
?
additional information
?
-
hexokinase I and hexokinase II are independently regulated, implying that they perform different roles in cardiac glucose regulation
-
-
?
additional information
?
-
-
the enzyme plays a role in glycogen synthesis and glucose homeostasis
-
-
?
additional information
?
-
-
hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
?
additional information
?
-
G/F discrepancy in Saccharomyces cerevisiae is not related to the maximal hexokinase activity in vitro with glucose or fructose as substrate or to the ratio between the Km values for glucose and fructose phosphorylation but might rather be related to the actual fructose phosphorylating activity at physiological fructose levels in vivo
-
-
?
additional information
?
-
-
G/F discrepancy in Saccharomyces cerevisiae is not related to the maximal hexokinase activity in vitro with glucose or fructose as substrate or to the ratio between the Km values for glucose and fructose phosphorylation but might rather be related to the actual fructose phosphorylating activity at physiological fructose levels in vivo
-
-
?
additional information
?
-
-
hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used
-
-
?
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(1R)-6-bromo-3-ethenyl-1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol
weak activity on hexokinase, 51% growth inhibition on asexual stage Plasmodium falciparum parasite
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
mixed to non-competitive inhibitors against ATP, non-competitive against D-glucose
(22E,24R)-6beta-methoxyergosta-7,9(11),22-triene-3beta,5alpha-diol
steroid from Ganoderma sinense. Potential drug candidate targeting at hexokinase 2 for cancer therapy
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
-
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
-
1,10-phenanthroline
Q56VN6
20 mM, 96% inhibition
1,5-Anhydro-D-glucitol 6-phosphate
1,5-anhydroglucitol-6-phosphate
-
potent inhibition of type I isozyme in absence of oxidative phosphorylation and with extramitochondrial ATP, weak inhibition with ATP supplied by oxidative phosphorylation
1-[(2,4-dichlorophenyl)methyl]-1H-indazole-3-carboxylic acid
2,3-bisphosphoglycerate
-
feedback regulation. The phosphorylation of glucose is the reaction whose rate controls that of the formation of diphosphoglyceric acid. It is therefore clear that this phosphorylation by diphosphoglyceric acid serves as the automatic regulation of the former by the latter
2,5-dihydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
2-(4-chlorophenyl)-1,2-benzothiazol-3(2H)-one
2-(4-chlorophenyl)-5-fluoro-1,2-benzothiazol-3(2H)-one
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
-
2-bromoacetamido-4-nitrophenol
increasing concentrations of glucose protect the SH groups of hexokinase from reaction with 2-bromoacetamido-4-nitrophenol
2-hydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
2-phenyl-1,2-benzothiazol-3(2H)-one
2-[([1,1'-biphenyl]-3-carbonyl)amino]-2,6-dideoxy-6-[(2,3-dichlorobenzene-1-sulfonyl)amino]-D-glucopyranose
inhibits in situ glycolysis in a UM-UC-3 bladder tumor cell line; inhibits in situ glycolysis in a UM-UC-3 bladder tumor cell line. Not selective for isoforms hexokinase 1 or hexokinase 2
22E-6beta-methoxyergosta-7,22-diene-3beta,5alpha-diol
-
3-(methanesulfonyl)-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
3-bromo-2-oxopropionic acid
-
-
3-chloro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
3-methoxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
-
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-(2-hydroxyethoxy)-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-(methanesulfonyl)-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-butyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-chloro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-fluoro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-methoxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
4-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
5,5'-dithiobis-(2-nitrobenzoic acid)
5-fluoro-N-phenyl-2-sulfanylbenzamide
-
5-hydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-2,3-dihydro-1H-indole-2-carbohydrazide
-
5-[[(2R,3S,4R,5R,6S)-5-[(3-bromophenyl)carbonylamino]-3,4,6-tris(oxidanyl)oxan-2-yl]methylsulfamoyl]-2-methyl-furan-3-carboxylic acid
not selective for isoforms hexokinase 1 or hexokinase 2
6-hydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
-
acetate
-
noncompetitive to glucose
acidic phospholipids
-
irreversible inhibition, binds at the nucleotide-binding site of enzyme, ATP and glucose 6-phosphate protect, effectiveness of various ligands in protection against inhibition, effect of pH and temperature
-
adenosine
-
at 10 mM, recombinant HXK1: 36% inhibition, recombinant HXK2: 5% inhibition
alloxan
-
alloxan treatment (100 mg/kg) leads to an 81% reduction in glucokinase immunoreactivity and a greater than 90% reduction in glucokinase enzymatic activity in the liver
arsenate
-
catalytically active 51 kDa C fragment of hexokinase
Br-
-
noncompetitive to glucose
CaCl2
Q56VN6
10 mM, 98% inhibition
cardiolipin
-
effectiveness of various ligands in protection against inhibition, effect of pH and temperature
Cibacron blue
-
competitive to ATP
citrate
-
noncompetitive to glucose and ATP
CoA
-
54.1% decreased activity
Cr(III)-ATP
-
complex of ATP with chromium in the 3+ oxidation state, mixed versus MgATP2-, competitive inhibition versus 2-deoxyglucose
D-fructose 1,6-diphosphate
D-Glucose 1,6-bisphosphate
competitive versus MgATP2-, low concentration of phosphate counteract
D-glucose 1,6-diphosphate
D-xylose
-
irreversible inactivation of the 3 isoenzymes, hexokinase PI inactivation requires ATP, hexokinase PII is inactivated by D-xylose without ATP, glucokinase is protected by ATP, competitive inhibitor of hexokinase PI and glucokinase, non-competitive inhibitor of hexokinase PII
dehydroascorbic acid
dehydroascorbic acid-mediated inhibition completely and irreversibly inactivates the enzyme in a pseudo-first order manner, resulting in the covalent binding of dehydroascorbic acid to the thiol groups of multiple Cys residues within hexokinase, a reaction that depends on the deprotonation of the affected residue with an alkaline pKa. Dehydroascorbic acid does not cause any cleavage of hexokinase, and it does not lead to the formation of any intermolecular crosslinks within this enzyme. The action of dehydroascorbic acid can be prevented, but not reversed, by dithiothreitol, and can be suppressed by the presence of glucose
dihydroxyacetonephosphate
-
hexokinase III
dimethyl 2-[[(2E)-3-(4-ethoxyphenyl)prop-2-enoyl]amino]-5,6-dihydro-4H-cyclopenta[b]thiophene-3,4-dicarboxylate
among most potent inhibitors identified in screen, lacks activity against parasites
dimethyl 2-[[4-(3-methylphenoxy)butanoyl]amino]-5,6-dihydro-4H-cyclopenta[b]thiophene-3,4-dicarboxylate
among most potent inhibitors identified in screen, lacks activity against parasites
F-
-
noncompetitive to glucose
GDP
-
31.3% decreased activity
GK regulatory protein
-
-
-
glucokinase regulatory protein
-
glucokinase-regulatory protein
GK regulatory protein, relative inhibition of glucokinase activity through GKRP alone wild-type: 32.5% and GKRP plus 10 microM sorbitol 6-phosphate: 55
-
glucose 1,6-disphosphate
-
-
human glucokinase regulatory protein
-
inhibition is reversed by activator RO-28-1675
-
Insulin
-
decreases glucokinase activity at 5.5 mM glucose and at 10 mM glucose. No effect at 2.8 mM glucose or at 20 mM glucose
-
KSCN
-
at about 0.25 M, 90% inhibition, reversible
Lactate
-
lactate indirectly inhibits hexokinase activity, which results from its cellular redistribution, attributed to alterations of hexokinase structure. No modulation of hexokinase activity in heart or kidney
lauric acid
IC50: 0.0758 mM, TbHK1
leptin
-
decreases glucokinase activity at all glucose concentrations tested
-
Mn2+
-
enzyme is inhibited by an excess of free divalent metal ion, Mg2+ or Mn2+
myristic acid
IC50: 0.0784 mM, TbHK1
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
-
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]pyridine-3-carbohydrazide
-
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]quinoline-2-carbohydrazide
-
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]thiophene-2-carbohydrazide
-
N,N'-bis(3-hydroxyphenyl)benzophenone-3,3',4,4'-tetracarboxylic diimide
decrease hexokinase activity in a dose-dependent manner
N,N'-[furan-2,5-diylbis(2-chloro-4,1-phenylene)]diguanidine
-
N-(4-[(2E)-2-[(2,3,4-trihydroxyphenyl)methylidene]hydrazinecarbonyl]phenyl)cyclopropanecarboxamide
-
N-acetyl glucosamine
Q56VN6
-
N-methylglucosamine
-
potent inhibitor of hexokinase I
Ni2+
-
competitive versus ATP via replacement of Mg2+, noncompetitive versus D-glucose via a cysteine residue proximal to the D-glucose binding site, enzyme-nickel interactions with positive cooperativity via histidine residues, no saturation is reached, nickel binding induces conformational changes in the secondary structure of the enzyme modifying the monomer/dimer equilibrium and decreasing the activity, overview
oxidized glutathione
-
82.9% decreased activity
p-chloromercuribenzoate
Q56VN6
0.05 mM, 72% inhibition
palmitic acid
IC50: 0.0624 mM, TbHK1
phenylpyruvic acid
the enzyme decreases the activity of enzyme in the presence and absence of glucose-6-phosphate (G6P) and increases the release of the enzyme from mitochondria
phosphatidylinositol
-
effectiveness of various ligands in protection against inhibition, effect of pH and temperature
phosphoenolpyruvate
-
hexokinase III
polyphosphate P3
-
up to 90% inhibition
-
polyphosphate P5
-
up to 90% inhibition
-
pyrrolidinium pyrrolidine-1-carbodithioate
the minimum effective spermicidal concentration of pyrrolidinium pyrrolidine-1-carbodithioate, 0.145 mM, inhibits the sperm-specific activity of hexokinase by 58%
S-nitrosoglutathione
hexokinase is particularly susceptible to protein structure modifications when exposed to even low concentrations of S-nitrosoglutathione. Biologically relevant [S-nitrosoglutathione]/[hexokinase] causes a significant decrease in Vmax with glucose (but not with fructose), along with oxidation of 5 Met and nitration of 4 Tyr. Preincubation of hexokinase with glucose abrogates the effect of S-nitrosoglutathione whereas fructose is ineffective
UDP-glucose
-
62.5% decreased activity
xylose
irreversible inactivation
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
-
mixed to non-competitive inhibitors against ATP, competitive against D-glucose
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
mixed to non-competitive inhibitors against ATP, competitive against D-glucose
1,5-Anhydro-D-glucitol 6-phosphate
-
hexokinase bound at type A and type B sites of brain mitochondria is relatively insensitive, hexokinase bound at type B sites, after removal of enzyme of type A sites, shows increased sensitivity
1,5-Anhydro-D-glucitol 6-phosphate
wild-type and nonaggregating interface mutant hexokinase I, inhibition is relieved by phosphate
1,5-Anhydro-D-glucitol 6-phosphate
-
-
1,5-Anhydro-D-glucitol 6-phosphate
-
HK I and HK I+, the D84A mutant of HK I has 2fold increased Ki, HK I: low millimolar concentrations of phosphate antagonize inhibition by competing for an anion binding site in the N-terminal half of HK I, HK I+: insert abolishes the antagonism of phosphate
1,5-Anhydro-D-glucitol 6-phosphate
-
intact enzyme and catalytically active 51 kDa C fragment of hexokinase
1,5-Anhydro-D-glucitol 6-phosphate
hexokinase I, antagonism by phosphate at low concentrations
1,5-Anhydro-D-glucitol 6-phosphate
-
less effective than glucose 6-phosphate, competitive versus ATP
1-[(2,4-dichlorophenyl)methyl]-1H-indazole-3-carboxylic acid
-
1-[(2,4-dichlorophenyl)methyl]-1H-indazole-3-carboxylic acid
-
-
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
-
hexokinase III
2-(4-chlorophenyl)-1,2-benzothiazol-3(2H)-one
-
2-(4-chlorophenyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-chlorophenyl)-5-fluoro-1,2-benzothiazol-3(2H)-one
-
2-(4-chlorophenyl)-5-fluoro-1,2-benzothiazol-3(2H)-one
-
-
2-deoxy-D-glucose
competitive, compound also inhibits the parasite growth in vitro at concentrations nontoxic to host cells
2-deoxy-D-glucose
2-deoxy-D-glucose is readily phosphorylated by hexokinase II but the product is not further processed by glucose-6-phosphate isomerase and thus accumulates in the cell to inhibit hexokinase II by a negative feedback loop
2-deoxy-D-glucose
-
2-deoxy-D-glucose is readily phosphorylated by hexokinase II but the product is not further processed by glucose-6-phosphate isomerase and thus accumulates in the cell to inhibit hexokinase II by a negative feedback loop
2-deoxy-D-glucose
-
compound is nearly 2fold less toxic Plasmodium falciparum lines overexpressing hexokinase compared with control parasites. Although catalytic activity is higher in in overexpressing cells, they accumulate phospho-2-deoxy-D-glucose at the same rate as control parasites
2-deoxy-D-glucose
-
low substrate inhibition
2-phenyl-1,2-benzothiazol-3(2H)-one
-
2-phenyl-1,2-benzothiazol-3(2H)-one
-
-
2-phosphoglycerate
-
-
2-phosphoglycerate
-
hexokinase III
3-Bromopyruvate
-
3-Bromopyruvate
-
in mice treated with 3-bromopyruvate, mean tumor volumes and tumor volume growth are significantly reduced
3-phosphoglycerate
-
-
3-phosphoglycerate
-
feedback regulation
3-phosphoglycerate
-
hexokinase III
5,5'-dithiobis-(2-nitrobenzoic acid)
-
5,5'-dithiobis-(2-nitrobenzoic acid)
-
inactivation, protection by MgADP-, AMP, 2-deoxyglucose, glucose, and mannose probably via binary complex formation, no protection by glucose 6-phosphate, slight protection by MgATP2-
5-thio-D-glucose
-
-
5-thio-D-glucose
-
marked inhibition
ADP
-
-
ADP
-
competitive versus ATP, both isozymes HKI and HKII
ADP
Q56VN6
0.0001 mM, 50% inhibition. Noncompetitive inhibition with the substrate glucose
ADP
-
mixed inhibitor versus both MgATP2- and glucose
ADP
-
0.1 mM, 60% inhibition
ADP
-
4 mM: 50% inhibition
ADP
-
strong, recombinant HXK1 and 2, HXK1 is more sensitive to inhibition than HXK2
ADP
-
1 mM, 50% inhibition; about 50% inhibition at 1 mM
ADP
-
competitive versus ATP, inhibition mode, 91.3% decreased activity
ADP
-
noncompetitive to glucose, competitive to ATP
ADP
-
0.1 mM, 60% inhibition
ADP
0.5 mM, 43% inhibition
ADP
-
5 mM, about 50% inhibition
ADP
-
isoenzymes HK1 and HK2, competitive to ATP, 0.5 mM: 4-5fold inhibition
ADP
1 mM, 92% inhibition. Competitive inhibition versus ATP, noncompetitive inhibition versus D-glucose
ADP
-
noncompetitive to glucose, competitive to ATP
ADP
natural hexokinase from epimastigotes
ADP
-
1 mM, 45% inhibition, enzyme from kernel. Inhibits non-cytosolic enzyme from root. No inhibition of the cytosolic enzyme from root; inhibition of non-cytosolic enzyme, no inhibition of cytosolic enzyme
AMP
-
competitive versus ATP, both isozymes HKI and HKII
AMP
-
strong, recombinant HXK1 and 2, HXK1 is more sensitive to inhibition than HXK2
AMP
-
binds to free enzyme and to D-glucose-enzyme
AMP
-
51.4% decreased activity
ATP
-
uncomplexed, competitive to MgATP2-, erythrocyte enzyme
ATP
-
uncomplexed, competitive to MgATP2-, erythrocyte enzyme
ATP
-
ATP4-; potent inhibitor of mitochondrial HK I
ATP
-
isoenzymes PII and PIIM are strongly inhibited by high physiological concentrations, 5 mM: 50% inhibition
ATP
-
ATP4-; hexokinase III; uncomplexed, competitive to MgATP2-, erythrocyte enzyme
Cl-
-
reversible, 0.25 M NaCl or KCl: 50% inhibition, at a comparable concentration of LiCl: 30% inhibition
Cl-
-
noncompetitive to glucose
D-fructose 1,6-diphosphate
-
-
D-fructose 1,6-diphosphate
-
hexokinase III
D-fructose 6-phosphate
-
product inhibition, both isozymes HKI and HKII
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
10 mM, 33% inhibition
D-fructose 6-phosphate
-
hexokinase III
D-glucosamine
Q56VN6
-
D-glucosamine
20 mM, 67% inhibition
D-glucose
-
at high concentrations; inhibits hexokinase III
D-glucose
-
hexokinase type III, but not its catalytically active recombinant carboxyl-domain, at concentrations above 0.5 mM
D-glucose
-
substrate inhibition of type III isozyme above 1 mM, antagonized by ATP
D-glucose
-
hexokinase C: above 0.2 mM, inhibition partially relieved by ATP concentrations above 1 mM, inhibition is not pH-dependent
D-glucose
-
higher than 100 mM; inhibits hexokinase III
D-glucose
-
higher than 0.4 mM; inhibits hexokinase III
D-glucose 1,6-diphosphate
-
-
D-glucose 1,6-diphosphate
-
competitive to MgATP2-, inhibition is partially relieved by phosphate
D-glucose 1,6-diphosphate
-
strong inhibition of a recombinant full-length HK I, a truncated form lacking the first 11 amino acids named HK-11aa, and of the 50 kDa C-terminal half containing the catalytic domain, strongly pH-dependent, inhibition is reversed by phosphate, except that of the C-terminal half
D-glucose 1,6-diphosphate
-
at concentrations higher than 0.2 mM, inhibits in a concentration-dependent manner, 1.2 mM: almost complete inhibition
D-glucose 1,6-diphosphate
-
-
D-glucose 1,6-diphosphate
-
15.7% decreased activity
D-glucose 1,6-diphosphate
-
hexokinase III
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
competitive versus MgATP2-
D-glucose 6-phosphate
-
product inhibition, both isozymes HKI and HKII
D-glucose 6-phosphate
Q56VN6
-
D-glucose 6-phosphate
-
strong inhibition, potential physiological effector
D-glucose 6-phosphate
-
hexokinase I inhibition is relieved by inorganic phosphate, but not the inhibition of hexokinase II
D-glucose 6-phosphate
-
inhibitor blocks the action of hexokinase by effecting a conformational change in the structure of enzyme
D-glucose 6-phosphate
-
competitive to MgATP2-; inhibition is partially relieved by phosphate
D-glucose 6-phosphate
-
potent inhibition of hexokinase I is relieved by physiological levels of phosphate, mechanism
D-glucose 6-phosphate
potent product inhibition, allosterically relieved by phosphate, wild-type hexokinase I and nondimerizing mutant
D-glucose 6-phosphate
-
hexokinase type III and its catalytically active recombinant carboxyl-domain
D-glucose 6-phosphate
-
competitive to MgATP2-; strong inhibition of a recombinant full-length HK I, a truncated form lacking the first 11 amino acids named HK-11aa, and of the 50 kDa C-terminal half containing the catalytic domain, at low concentrations, 0-3 mM, inhibition is reversed by phosphate, except that of the C-terminal half
D-glucose 6-phosphate
-
noncompetitive inhibition
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
feedback-inhibition in response to the physiologic concentration of D-glucose 6-phosphate
D-glucose 6-phosphate
-
moderate sensitivity to inhibition. Inhibition is competitive with respect to both ATP and glucose
D-glucose 6-phosphate
-
marked inhibition of particulate hexokinase I activity
D-glucose 6-phosphate
-
inhibition of all isozymes, with type I isozyme inhibition is antagonized by phosphate, while with type II and III isozymes phosphate causes additional inhibition
D-glucose 6-phosphate
-
linear competitive inhibition with MgATP2- as varied substrate
D-glucose 6-phosphate
-
potent inhibitor of mitochondrial HK I
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
inhibition of HK I, antagonism of inhibition by low millimolar concentrations of phosphate results from competition of this ligands for an anion binding site in the N-terminal half of HK I, mechanism
D-glucose 6-phosphate
-
reversible product inhibition
D-glucose 6-phosphate
-
competitive versus ATP; hexokinase C: strong inhibition
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
product inhibition of hexokinase I, antagonism by phosphate at low concentrations results from competition for a common anion binding site located in the N-terminal half
D-glucose 6-phosphate
-
hexokinase activity is strongly inhibited by high, but physiological, concentrations of glucose 6-phosphate
D-glucose 6-phosphate
-
D-glucose 6-phosphate at physiological concentrations is a potent inhibitor of hexokinase isoforms I and II but not of hexokinase type IV
D-glucose 6-phosphate
-
54.3% decreased activity
D-glucose 6-phosphate
-
competitive versus ATP; moderate inhibition
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
isoenzyme HK1, not HK2, noncompetitive to glucose
D-glucose 6-phosphate
hexokinase 1
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
hexokinase III, poor inhibitor, not relieved by phosphate
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
weak inhibition of enzyme from kernel. No effect on the enzyme from root; weak inhibition of enzyme from kernel, no inhibition of cytosolic and non-cytosolic enzyme from root
D-mannoheptulose
-
competitive inhibition
D-mannose
-
-
D-mannose
-
competitive to D-glucose; glucokinase
D-mannose
-
competitive to D-glucose
D-mannose
10 mM, 88% loss of activity
diphosphate
Q56VN6
mixed type of inhibition when ATP is used as substrate
diphosphate
10 mM, 54% inhibition
diphosphate
1 mM, 70% inhibition
diphosphate
natural hexokinase from epimastigotes, mixed-type inhibition
diphosphate
-
non-competitive inhibition towards ATP, mixed-type towards D-glucose; non-competitive inhibitor
ebselen
-
EDTA
Q56VN6
40 mM, 91% inhibition
EDTA
2.5 mM, complete inhibition
glucokinase regulatory protein
-
binds glucokinase in the nucleus and inhibits its activity
-
glucokinase regulatory protein
-
inhibits competitively GCK activity with D-glucose, inhibition of glucokinase activity by glucokinase regulatory protein in vivo is enhanced by fructose 6-phosphate or sorbitol 6-phosphate
-
glucokinase regulatory protein
-
inhibits competitively GCK activity with D-glucose, inhibition of glucokinase activity by glucokinase regulatory protein in vivo is enhanced by fructose 6-phosphate or sorbitol 6-phosphate
-
glucokinase regulatory protein
-
binds glucokinase in the nucleus and inhibits its activity
-
glucokinase regulatory protein
-
inhibits competitively GCK activity with D-glucose, inhibition of glucokinase activity by glucokinase regulatory protein in vivo is enhanced by fructose 6-phosphate or sorbitol 6-phosphate
-
glucokinase regulatory protein
-
human, i.e. GKRP, recombinantly expressed in Escherichia coli, competitive to glucose, strong inhibition in absence of fructose 6-phosphate or sorbitol 6-phosphate, the protein also binds fructose 1-phosphate and chloride are reversing the inhibition
-
glucokinase regulatory protein
-
wild type enzyme and mutant enzymes V62A, V62T, and V62E are significantly inhibited (80% enzyme activity remaining), no inhibition of V62L, V62M, V62Q, V62F, V62K
-
glucokinase regulatory protein
-
competitive inhibitor of glucokinase, in the fasted state, glucokinase is in part sequestered in the nucleus in an inactive state, complexed to a specific regulatory protein, glucokinase regulatory protein
-
glucokinase regulatory protein
-
-
-
glucokinase regulatory protein
-
competitive inhibitor
-
glucokinase regulatory protein
-
competitive inhibitor of GCK activity, fructose 6-phoshate and fructose 1-phosphate enhance or reduce glucokinase regulatory protein-mediated inhibition, respectively. P446L-glucokinase regulatory protein has reduced regulation by physiological concentrations of fructose 6-phoshate, resulting indirectly in increased glucokinase activity
-
glucokinase regulatory protein
-
competitive inhibitor of glucokinase. Binding of glucokinase regulatory protein (GKRP) to glucokinase (GCK) involves two steps, formation of an initial encounter complex followed by conformational equilibration between two GKRP-GCK states. Fructose 6-phosphate, an enhancer of GKRP action, promotes formation of the initial encounter complex via a 2.6fold increase in k(on) and stabilizes the complex through a 60fold decrease in k(of)
-
glucokinase regulatory protein
-
competitive inhibitor of glucokinase, in the fasted state, glucokinase is in part sequestered in the nucleus in an inactive state, complexed to a specific regulatory protein, glucokinase regulatory protein
-
glucokinase regulatory protein
-
inhibits competitively GCK activity with D-glucose, inhibition of glucokinase activity by glucokinase regulatory protein in vivo is enhanced by fructose 6-phosphate or sorbitol 6-phosphate
-
glucokinase regulatory protein
-
i.e. GKRP, recombinantly expressed in Escherichia coli, inhibition in absence of fructose 6-phosphate or sorbitol 6-phosphate, competitive to D-glucose, fructose 1-phosphate and chloride are reversing the inhibition
-
glucokinase regulatory protein
-
competitive inhibitor of glucokinase, in the fasted state, glucokinase is in part sequestered in the nucleus in an inactive state, complexed to a specific regulatory protein, glucokinase regulatory protein
-
glucokinase regulatory protein
-
binding of fructose 6-phosphate to glucokinase regulatory protein favors the glucokinase regulatory protein-glucokinas interaction with a negative effect on enzyme activity, while binding of fructose-1-phosphate weakens the glucokinase regulatory protein-glucokinase interaction and releases active glucokinase, the reversible association of glucokinase with glucokinase regulatory protein does more than simply regulate the catalytic activity of glucokinase, it also appears to underlie the intracellular trafficking of glucokinase between cytoplasm and nucleus
-
glucokinase regulatory protein
-
inhibits competitively GCK activity with D-glucose, inhibition of glucokinase activity by glucokinase regulatory protein in vivo is enhanced by fructose 6-phosphate or sorbitol 6-phosphate
-
glucokinase regulatory protein
-
-
-
glucokinase regulatory protein
-
binds glucokinase in the nucleus and inhibits its activity
-
glucokinase regulatory protein
-
-
-
GSSG
-
product inhibition
GSSG
-
strong inhibitor at all concentrations
I-
-
at about 0.25 M KI, 70% inhibition, reversible
I-
-
noncompetitive to glucose
KCl
Q56VN6
10 mM, 92% inhibition
lonidamine
-
lonidamine
-
lonidamine is toxic to cultured bloodstream form parasites and procyclic form parasites. Overexpression of TbHK1 protects procyclic forms from lonidamine
mannoheptulose
Q56VN6
-
mannoheptulose
-
inhibition of non-cytosolic enzyme and cytosolic enzyme
Mg2+
-
enzyme is inhibited by an excess of free divalent metal ion, Mg2+ or Mn2+
Mg2+
Q56VN6
100 mM, 72% inhibition
Mg2+
-
competitive to MgATP2-; uncomplexed
Mg2+
-
competitive to MgATP2-; uncomplexed
MgADP-
-
erythrocyte enzyme, mixed inhibitor versus MgATP2- and D-glucose
MgADP-
-
product inhibition, mixed type inhibition versus MgATP2-, competitive inhibition versus 2-deoxyglucose
N-acetyl-D-glucosamine
-
potent inhibitor of hexokinase I
N-acetyl-D-glucosamine
-
competitive to glucose; erythrocyte enzyme; noncompetitive to MgATP2-
N-acetyl-D-glucosamine
-
-
N-acetyl-D-glucosamine
-
competitive to glucose
N-acetylglucosamine
-
-
N-acetylglucosamine
-
mixed versus MgATP2-, competitive inhibition versus 2-deoxyglucose
NaCl
Q56VN6
10 mM, 96% inhibition
NO3-
-
at about 0.25 M NaNO3, 40% inhibition, reversible
NO3-
-
noncompetitive to glucose
palmitoyl-CoA
-
-
palmitoyl-CoA
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast; inhibitor binds to a site distinct from the catalytic site, noncompetitive to MgATP2-, competitive to glucose, synergistic with N-acetylglucosamine
palmitoyl-CoA
-
glucokinase is inhibited by endogenous long-chain fatty acyl-CoA in islets from omega3-depleted rats
palmitoyl-CoA
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
palmitoyl-CoA
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
phosphate
-
-
phosphate
-
at high concentrations, 10-50 mM, inhibition of recombinant full-length HK I, a truncated form lacking the first 11 amino acids named HK-11aa, and of the 50 kDa C-terminal half containing the catalytic domain, competitive versus MgATP2-
phosphate
-
inhibits type II and III isozymes, synergistic with D-glucose 6-phosphate product inhibition
phosphate
-
at higher concentrations, binds to a lower affinity site in the C-terminal half, HK I and HK I+
phosphate
-
noncompetitive to glucose
phosphate
-
competitive versus ATP; intact enzyme: at high concentrations, catalytically active 51 kDa C fragment of hexokinase: also at low concentrations; noncompetitive to glucose
phosphate
competitive versus ATP; hexokinase I, at high concentrations
phosphate
-
hexokinase III
quercetin
-
quercetin
-
quercetin inhibition, but not binding, is relieved by glycerol 3-phosphate at pH 6.5
reduced glutathione
-
1 mM: reduced state of the enzyme with full catalytic activity, marked inhibition at high concentrations
reduced glutathione
-
54.5% decreased activity
Regulatory protein
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast; inhibitor binds to a site distinct from the catalytic site, noncompetitive to MgATP2-, competitive to glucose, synergistic with N-acetylglucosamine, phosphate and sulfate decrease inhibition, monovalent anions antagonize inhibition with the following decreasing order of potency: I-, Br-, NO3-, Cl-, F-, acetate
-
Regulatory protein
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
-
Regulatory protein
-
inhibition of enzymes from rat liver, pig liver, Buffo marinus, no inhibition: rat brain, bovine heart, yeast
-
SO42-
-
noncompetitive to glucose
SO42-
-
catalytically active 51 kDa C fragment of hexokinase
trehalose 6-phosphate
-
trehalose 6-phosphate
competitive to D-glucose
trehalose 6-phosphate
-
90.9% decreased activity
Triethyltin bromide
-
0.5 mM, 1 h, 37°C, nearly complete inhibition; selective inhibitor, sugar substrates D-glucose and D-mannose protect
Triethyltin bromide
-
selective inhibitor, sugar substrates D-glucose and D-mannose protect
UDP
-
weak
UDP
-
51.9% decreased activity
UMP
-
very weak
Urea
-
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
enzymes from rat brain and bovine heart are not inhibited by palmitoyl-CoA or regulatory protein
-
additional information
-
not inhibited by D-glucose-6-phosphate
-
additional information
-
no inhibition by D-glucose 6-phosphate and D-trehalose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose-6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
inactivation by autophosphorylation at Ser157 utilizing MgATP2-, first order kinetics reaveal an extrapolated residual activity of about 60%
-
additional information
-
inactivation by autophosphorylation at Ser157 utilizing MgATP2-, first order kinetics reaveal an extrapolated residual activity of about 60%
-
additional information
-
not inhibited by 2-deoxy-D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
D-glucose 6-phosphate has no effect on the enzyme from seed
-
additional information
-
enzymes from rat brain and bovine heart are not inhibited by palmitoyl-CoA or regulatory protein
-
additional information
-
not inhibited by 1 mM phosphatidylethanolamine or phosphatidylcholine
-
additional information
-
inhibition mechanism, overview
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
-
no product inhibition by D-glucose 6-phosphate
-
additional information
-
not inhibited by D-glucose-6-phosphate
-
additional information
-
multiplex inhibitor screening, mass spectrometry-based assay
-
additional information
not inhibited by trehalose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
not inhibited by trehalose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
-
not inhibited by trehalose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
-
D-glucose 6-phosphate has no effect
-
additional information
-
D-glucose 6-phosphate has no effect; no inhibition of hexokinase 2: D-glucose 6-phosphate
-
additional information
D-glucose 6-phosphate has no effect; no inhibition of hexokinase 2: D-glucose 6-phosphate
-
additional information
D-glucose 6-phosphate has no effect; no inhibition of hexokinase 2: D-glucose 6-phosphate
-
additional information
-
-
-
additional information
-
not inhibited by glyceraldehyde 3-phosphate, pyruvate, lactate
-
additional information
not inhibited by D-fructose 6-phosphate, ADP; not inhibited by D-glucose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
-
not inhibited by D-fructose 6-phosphate, ADP; not inhibited by D-glucose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
-
not inhibited by D-glucose 6-phosphate
-
additional information
not inhibited by D-fructose; not inhibited by D-glucose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
-
not inhibited by D-fructose; not inhibited by D-glucose 6-phosphate; not inhibited by trehalose 6-phosphate
-
additional information
-
enzyme is not affected by D-glucose 6-phosphate; TcHK is not affected by D-glucose 6-phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E)-3-cyclopentyl-2-[4-(cyclopropylsulfonyl)phenyl]-N-[4-(1,2-dihydroxyethyl)-1,3-thiazol-2-yl]prop-2-enamide
-
-
(2R)-2-[4-(cyclopropylsulfonyl)phenyl]-N-(5-fluorothiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
96% maximum activation above control at 6.5 mM glucose
(2R)-3-cyclopentyl-2-[4-(methylsulfonyl)phenyl]-N-(1,3-thiazol-2-yl)propanamide
-
activator associates with glucokinase in a glucose-independent fashion. Kinetic assays reveal a lag in enzyme progress curves that is systematically reduced when the enzyme is preincubated with the activator. Activator binding is enthalpically driven. The kcat value of glucokinase is almost fully limited by product release, both in the presence and absence of activator
(2R)-3-cyclopentyl-2-[4-(methylsulfonyl)phenyl]-N-(1,3-thiazol-2-yl)propanamide}
-
RO0281675, 1.5fold change in Vmax or kcat at 0.003 mM
(6-ethoxyquinazolin-4-yl)(1-methyl-1H-pyrazol-3-yl)amine
-
increases glucokinase activity at glucose concentrations up to approximately 20 mM
(6-ethoxyquinazolin-4-yl)pyridin-2-ylamine
-
increases glucokinase activity at glucose concentrations below approximately 7 mM
(6-isopropoxyquinazolin-4-yl)(1-methyl-1H-pyrazol-3-yl)amine
-
increases glucokinase activity at glucose concentrations up to approximately 20 mM
(R)-2-(4-(methylsulfonyl)phenyl)-3-((R)-3-oxocyclopentyl)-N-(pyrazin-2-yl)propanamide
-
piragliatin
(S)-2-(4-(cyclopropylsulfonyl)phenyl)-N-(5-fluorothiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
PSN-GK1, 1.1fold change in Vmax or kcat at 0.0001 mM
(S)-2-[3-chloro-4-(ethylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
26% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-(4,4-difluorocyclohexyl)-N-(5-methylpyridin-2-yl)propanamide
-
15% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclobutyl-N-(5-methylpyridin-2-yl)propanamide
-
72% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclohexyl-N-(5-methylpyridin-2-yl)propanamide
-
46% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
57% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-4-methyl-N-(5-methylpyridin-2-yl)pentanamide
-
37% maximum activation above control at 6.5 mM glucose
(S)-2-[3-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)-3-phenylpropanamide
-
30% maximum activation above control at 6.5 mM glucose
(S)-2-[4-(cyclobutylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
67% maximum activation above control at 6.5 mM glucose
(S)-2-[4-(cyclobutylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-pyrazin-2-ylpropanamide
-
66% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(cyclobutylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(1-methyl-1H-pyrazol-3-yl)propanamide
-
67% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(cyclopropylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(1-methyl-1H-pyrazol-3-yl)propanamide
-
84% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
122% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-chloropyridin-2-yl)-3-cyclopentylpropanamide
-
82% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(1-methyl-1H-pyrazol-3-yl)propanamide
-
57% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyrazin-2-yl)propanamide
-
104% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-(5-methylpyridin-2-yl)propanamide
-
69% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-1,3-thiazol-2-ylpropanamide
-
42% maximum activation above control at 6.5 mM glucose
(S)-2-[5-chloro-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-3-cyclopentyl-N-1H-pyrazol-3-ylpropanamide
-
50% maximum activation above control at 6.5 mM glucose
(S)-3-(4-((3-fluoropyrrolidin-1-yl)sulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)-N-(thiazol-2-yl)benzamide
-
activation: 1.9fold
(S)-3-(4-((3-fluoropyrrolidin-1-yl)sulfonyl)phenoxy)-N-(5-fluorothiazol-2-yl)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 2.2fold
(S)-3-cyclopentyl-2-[4-(cyclopropylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
76% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-(cyclopropylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-pyrazin-2-ylpropanamide
-
94% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-(ethylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
73% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
65% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-pyridin-2-ylpropanamide
-
43% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-[5-(trifluoromethyl)pyridin-2-yl]propanamide
-
35% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[5-methyl-4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
103% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-2-[5-methyl-4-[(1-methylethyl)sulfonyl]-2-oxopyridin-1(2H)-yl]-N-(5-methylpyridin-2-yl)propanamide
-
48% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-N-(5-methylpyrazin-2-yl)-2-[4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]propanamide
-
101% maximum activation above control at 6.5 mM glucose
(S)-3-cyclopentyl-N-(5-methylpyridin-2-yl)-2-[4-(methylsulfonyl)-2-oxopyridin-1(2H)-yl]propanamide
-
58% maximum activation above control at 6.5 mM glucose
(S)-6-(3-cyclopentyl-2-[4-(trifluoromethyl)-1H-imidazol-1-yl]propanamido)nicotinic acid
-
in the presence of liver-specific GKA, progress curves at 1 mM glucose are similar to those at 5 mM, reflecting activation of GK. With steady-state kinetic methods it is shown that there are at least two kinetically distinct forms of glucokinase that interconvert through a slow conformational change and that this interconversion is affected by glucose concentration and a liver-specific GKA
(Z)-2-(4-(cyclopropylsulfonyl)phenyl)-N-(5-(2-methylpropylidene)-4-oxo-4,5-dihydro thiazol-2-yl)-3-(tetrahydro-2Hpyran-4-yl)propanamide
-
activation: 1.17fold
(Z)-N-(5-benzylidene-4-oxo-4,5-dihydrothiazol-2-yl)-2-(4-(cyclopropylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.24fold
1-(1-(4-chlorophenyl)cyclohexyl)-3-(thiazol-2-yl)urea
-
-
1-[6'-(2-hydroxy-2-methylpropoxy)-4-[(5-methylpyridin-3-yl)oxy]-3,3'-bipyridin-6-yl]-3-methylurea
i.e. AM-2394. Compound activates glucokinase with an EC50 of 60 nM, increases the affinity of glucokinase for glucose by approximately 10fold, exhibits moderate clearance and good oral bioavailability in multiple animal models, and lowers glucose excursion following an oral glucose tolerance test in an ob/ob mouse model of diabetes
2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido)-N,N-dimethyl-6,7-dihydro[1,3]thiazolo[5,4-c]pyridine-5(4H)-carboxamide
-
maximal activation: 2.35fold
2-(4-(cyclopropylsulfonyl)phenyl)-3-(tetrahydro-2Hpyran-4-yl)-N-(4,5,6,7-tetrahydrobenzo[d]thiazol-2-yl)propanamide
-
activation: 2.27fold
2-(4-(cyclopropylsulfonyl)phenyl)-N-(4-(prop-1-en-2-yl)thiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 2.4fold
2-(4-(cyclopropylsulfonyl)phenyl)-N-(4-isopropylthiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 2.97fold
2-(4-(cyclopropylsulfonyl)phenyl)-N-(4-oxo-4,5-dihydrothiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.65fold
2-(4-(cyclopropylsulfonyl)phenyl)-N-(5,6-dihydro-4Hcyclopenta[d]thiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 3.4fold
2-(4-(cyclopropylsulfonyl)phenyl)-N-(5-iodo-4-isopropylthiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.34fold
2-(4-(cyclopropylsulfonyl)phenyl)-N-(5-methyl-4,5,6,7-tetrahydrothiazolo[5,4-c] pyridin-2-yl)-3-(tetrahydro-2Hpyran-4-yl)propanamide
-
activation: 2.26fold
2-(4-(methylsulfonyl)phenyl)-N-(4-phenylthiazol-2-yl)-3-(tetrahydro-2H-pyran-4-yl)-propanamide
-
activation: 1.3fold
2-(methylamino)-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-4-chloro-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-4-fluoro-5-((1-methyl-1H-imidazol-2-yl)thio)-N-(thiazol-2-yl)benzamide
2-amino-4-fluoro-5-(1,3,4-thiadiazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
1.14fold activation at 0.01 mM
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
1.47fold activation at 0.01 mM
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-thiazol-2-yl-benzamide
2-amino-4-fluoro-5-(4-methyl-thiazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
0.89fold activation at 0.01 mM
2-amino-4-fluoro-5-(thiazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
-
1.15fold activation at 0.01 mM
2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]-N-(4-methylthiazol-2-yl)benzamide
-
108% maximum activation above control at 6.5 mM glucose
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1,3,4-thiadiazol-2-ylsulfanyl)-benzamide
-
1.36fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1-methyl-1Himidazol-2-ylsulfanyl)-benzamide
-
2.04fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(pyridin-2-ylsulfanyl)-benzamide
-
1.1fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(thiazol-2-ylsulfanyl)-benzamide
-
1.25fold activation at 0.01 mM
2-amino-4-fluoro-N-(3-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
1.15fold activation at 0.01 mM
2-amino-4-fluoro-N-(4-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
2.01fold activation at 0.01 mM
2-amino-5-((4-methyl-4H-1,2,4-triazol-3-yl)thio)-N-(5-methylthiazol-2-yl)benzamide
-
1.3fold change in Vmax or kcat at 0.01 mM
2-amino-5-(1H-imidazol-2-ylsulfanyl)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(2-fluorophenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(2-methoxyphenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(3-fluorophenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(4-fluorophenoxy)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-(benzoxazol-2-ylsulfanyl)-4-fluoro-N-(3-fluoro-phenyl)-benzamide
-
0.83fold activation at 0.01 mM
2-amino-5-(ethylsulfanyl)-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-chloro-N-(1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-chloro-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-ethoxy-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-(1,2,4-thiadiazol-5-yl)benzamide
-
-
2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-(1,3-thiazol-2-yl)benzamide
-
-
2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-[4-(trifluoromethyl)-1,3-thiazol-2-yl]benzamide
-
-
2-amino-5-[2-[methyl(methylidene)oxido-l6-sulfanyl]phenoxy]-N-(4-methyl-1,3-thiazol-2-yl)benzamide
-
-
2-amino-N-(1,3-thiazol-2-yl)benzamide
-
-
2-amino-N-(3,4-dimethoxy-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
1.32fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1,3,4-thiadiazol-2-ylsulfanyl)-benzamide
-
1.22fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
2.09fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(4-methylthiazol-2-ylsulfanyl)-benzamide
-
1.1fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(pyridin-2-ylsulfanyl)-benzamide
-
1.12fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(thiazol-2-ylsulfanyl)-benzamide
-
1.21fold activation at 0.01 mM
2-amino-N-(3-amino-phenyl)-5-(4,6-dimethyl-pyrimidin-2-ylsulfanyl)-4-fluoro-benzamide
-
1.09fold activation at 0.01 mM
2-amino-N-(3-aminomethyl-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
-
1.01fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1,3,4-thiadiazol-2-ylsulfanyl)-benzamide
-
1.2fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1-methyl-1Himidazol-2-ylsulfanyl)-benzamide
-
1.95fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(4-methylthiazol-2-ylsulfanyl)-benzamide
-
0.99fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(thiazol-2-ylsulfanyl)-benzamide
-
1.2fold activation at 0.01 mM
2-amino-N-(3-cyano-phenyl)-5-(4,6-dimethyl-pyrimidin-2-ylsulfanyl)-4-fluoro-benzamide
-
1.01fold activation at 0.01 mM
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(phenylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(pyridin-2-ylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(pyridin-3-ylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-(pyridin-4-ylsulfanyl)benzamide
-
-
2-amino-N-(3-methyl-1,2,4-thiadiazol-5-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-(4H-1,2,4-triazol-3-ylsulfanyl)benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-(phenylsulfanyl)benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-(pyridin-2-ylsulfanyl)benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
2-amino-N-(4-methylthiazol-2-yl)-5-phenoxybenzamide
-
-
2-amino-N-(5-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-N-[4-(hydroxymethyl)-1,3-thiazol-2-yl]-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-cyclopentyl-1-(4-(methylsulfonyl)phenyl)-N-(thiazol-2-yl)ethanesulfonamide
-
-
2-[(3-cyclopentyl-2-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]propanoyl)amino]-5-methoxy-1H-[1,3]thiazolo[5,4-b]pyridin-3-ium
-
-
2-[4-(2,4-difluoro-phenyl)-piperazin-1-yl]-N-(3,4-dimethoxy-phenyl)-acetamide
-
1.01fold activation at 0.01 mM
2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-N-(3-trifluoromethyl-phenyl)-acetamide
-
1.06fold activation at 0.01 mM
2-[4-(methylsulfonyl)phenyl]-3-(tetrahydro-2H-pyran-4-yl)-N-(1,3-thiazol-2-yl)propanamide
-
activation: 2.45fold
28-homobrassinolide
28-homobrassinolide is able to protect or restore the native structure of hexokinase when exposed to diabetic levels of glucose. The denatured hexokinase is renatured upon binding with homobrassinolide. Homobrassinolide is able to bind to the drug-binding pocket of glucokinase. The glide energy is -7.1 kcal/mol
3-((3-methylbut-2-en-1-yl)oxy)-5-(4-(morpholinosulfonyl)phenoxy)-N-(thiazol-2-yl)benzamide
-
activation: 2.1fold
3-(4-(((2S,6R)-2,6-dimethylmorpholino)sulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)-N-(thiazol-2-yl)benzamide
-
activation: 1.5fold
3-(4-(((2S,6R)-2,6-dimethylmorpholino)sulfonyl)phenoxy)-N-(5-fluorothiazol-2-yl)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 1.7fold
3-(4-((4-methoxypiperidin-1-yl)sulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)-N-(thiazol-2-yl)benzamide
-
activation: 1.7fold
3-(4-(8-oxa-3-azabicyclo[3.2.1]octan-3-ylsulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)-N-(thiazol-2-yl)benzamide
-
activation: 1.7fold
3-(4-(8-oxa-3-azabicyclo[3.2.1]octan-3-ylsulfonyl)phenoxy)-N-(5-fluorothiazol-2-yl)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 1.9fold
3-(4-(cyclopropylsulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)-N-(4-oxo-4,5-dihydrothiazol-2-yl)benzamide
-
activation: 1.5fold
3-(4-(cyclopropylsulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)-N-(5-methylpyrazin-2-yl)benzamide
-
activation: 1.6fold
3-(4-(cyclopropylsulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)-N-(thiazol-2-yl)benzamide
-
activation: 2.4fold
3-(4-(cyclopropylsulfonyl)phenoxy)-N-(1,5-dimethyl-1H-pyr-azol-3-yl)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 1.5fold
3-(4-(cyclopropylsulfonyl)phenoxy)-N-(4-(4-fluorophenyl)thiazol-2-yl)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 0.9fold
3-(4-(cyclopropylsulfonyl)phenoxy)-N-(5-fluorothiazol-2-yl)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 1.8fold
3-(5-chloro-1,3-thiazol-2-yl)-1-[4-(methylsulfonyl)phenyl]-1-(thiophen-2-ylmethyl)urea
-
-
3-(5-chlorothiazol-2-yl)-1-(4-(methylsulfonyl)phenyl)-1-(thiophen-3-ylmethyl)urea
-
-
3-amino-N-[2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-phenyl]-benzamide
-
1.16fold activation at 0.01 mM
3-phosphoglycerate
-
activates
3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]-N-(4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)benzamide
-
maximal activation: 2.2fold
3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]-N-[5-(2-oxo-1,2-dihydropyridin-4-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 2.13fold
3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]-N-[5-(pyridin-2-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 1.92fold
3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]-N-[5-(pyrimidin-2-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 2.35fold
3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]-N-[5-(pyrimidin-4-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 2.53fold
3-[4-(azetidine-1-carbonyl)phenoxy]-N-[5-(2-hydroxyethyl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamide
-
maximal activation: 1.97fold
3-[4-(azetidine-1-carbonyl)phenoxy]-N-[5-(2-methoxyethyl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamide
-
maximal activation: 1.76fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-(4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl)benzamide
-
maximal activation: 3.42fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-(5-methyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)benzamide
-
maximal activation: 3.41fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-(5-phenyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)benzamide
-
maximal activation: 2.05fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-(7-oxo-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl)benzamide
-
maximal activation: 2.61fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-[5-(propan-2-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 2fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-[5-(pyridin-2-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 2.39fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-[5-(pyridin-3-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 2.7fold
3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]-N-[5-(pyridin-4-yl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]benzamide
-
maximal activation: 2.97fold
4-[4-(dimethylcarbamoyl)-3-fluorophenoxy]-2-ethyl-2-methyl-N-(5-methylpyridin-2-yl)-2,3-dihydro-1-benzofuran-6-carboxamide
-
-
5-(2-methylpropyl)-N-(1,3-thiazol-2-yl)-1H-indazol-3-amine
-
-
5-({3-(propan-2-yloxy)-5-[2-(thiophen-3-yl)ethoxy]benzoyl}amino)-1,3,4-thiadiazole-2-carboxylic acid
-
-
6-(3-(((S)-1-methoxypropan-2-yl)oxy)-5-(((S)-1-phenylpropan-2-yl)oxy)benzamido)nicotinic acid
6-({3-(propan-2-yloxy)-5-[2-(thiophen-3-yl)ethoxy]benzoyl}amino)pyridine-3-carboxylic acid
-
GKA22
6-ethoxy-N-(1-methyl-1H-pyrrol-3-yl)-quinazolin-4-amine
-
0.95fold change in Vmax or kcat at 0.05 mM
6-ethoxy-N-(pyridin-2-yl)-quinazolin-4-amine
-
0.62fold change in Vmax or kcat at 0.05 mM
6-isopropoxy-N-(1-methyl-1H-pyrrol-3-yl)quinazolin-4-amine
-
0.8fold change in Vmax or kcat at 0.05 mM
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
6-[[3-hydroxy-5-(propan-2-yloxy)benzoyl]amino]pyridine-3-carboxylic acid
-
activator associates with glucokinase in a glucose-independent fashion. Kinetic assays reveal a lag in enzyme progress curves that is systematically reduced when the enzyme is preincubated with the activator. Activator binding is enthalpically driven. The kcat value of glucokinase is almost fully limited by product release, both in the presence and absence of activator
6-{[3-(2-methylpropoxy)-5-(propan-2-yloxy)benzoyl]amino}pyridine-3-carboxylic acid
-
-
citrate
-
allosteric activator
ethyl 2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[5,4-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.22fold
ethyl 2-[([2-amino-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]phenyl]carbonyl)amino]-1,3-thiazole-4-carboxylate
-
-
galactose
-
activates isoenzyme Hex II
glucokinase-associated phosphatase
-
-
-
glucokinase-associated protein
-
glucose 6-phosphate
-
recombinant HXK1: at 10 mM 13% activation, at 20 mM 31% activation, recombinant HXK2: at 10 mM 23% activation, at 20 mM 48% activation
glucose-6-phosphate
Q56VN6
10 mM, recombinant enzyme is 3fold activated
glycerol 3-phosphate
-
influences enzyme activity at pH 6.5 by preventing substrate and product inhibition by ATP and ADP, respectively
Insulin
-
stimulating effect is abolished when lactate is added
-
isocitrate
-
activates isoenzyme Hex II
lyxose
-
activates isoenzyme Hex II
mannose 6-phosphate
-
activates isoenzyme Hex II
methyl 2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[5,4-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.38fold
N,N'-bis-(2-methoxy-phenyl)-isophthalamide
-
1.02fold activation at 0.01 mM
N,N'-bis-(3-methoxy-phenyl)-isophthalamide
-
0.81fold activation at 0.01 mM
N,N'-bis-(4-methoxy-phenyl)-isophthalamide
-
0.89fold activation at 0.01 mM
N,N-dicyclohexyl-N'-methyldicarbonimidic diamide
-
-
N-(3-amino-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
1.08fold activation at 0.01 mM
N-(3-cyano-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
0.96fold activation at 0.01 mM
N-(3-fluoro-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
1.01fold activation at 0.01 mM
N-(4,5-dimethylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.72fold
N-(4-(4-fluorophenyl)thiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.25fold
N-(4-(4-methoxyphenyl)thiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.22fold
N-(4-(tert-butyl)thiazol-2-yl)-3-(4-(cyclopropylsulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 0.7fold
N-(4-cyclopropylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.87fold
N-(4-ethylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)-propanamide
-
activation: 2.17fold
N-(4-isobutylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)-propanamide
-
activation: 2.05fold
N-(4-isopropylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)-propanamide
-
activation: 2.49fold
N-(4-methyl-1,3-thiazol-2-yl)-3-(pyridin-3-ylmethoxy)pyridin-2-amine
-
-
N-(4-methyl-1,3-thiazol-2-yl)-3-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-2-nitrobenzamide
-
-
N-(4-tert-butylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)-propanamide
-
activation: 1.29fold
N-(5,6-dihydro-4H-cyclopenta[d][1,3]thiazol-2-yl)-3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamide
-
maximal activation: 4.8fold
N-(5-acetyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)-3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamide
-
maximal activation: 2.5fold
N-(5-benzyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)-3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamide
-
maximal activation: 2.1fold
N-(5-bromo-4-isopropylthiazol-2-yl)-2-(4-(cyclopropylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.67fold
N-(5-ethyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)-3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamide
-
maximal activation: 2.08fold
N-(5-fluorothiazol-2-yl)-3-((3-methylbut-2-en-1-yl)oxy)-5-(4-(morpholinosulfonyl)phenoxy)benzamide
-
activation: 1.8fold
N-(5-fluorothiazol-2-yl)-3-(4-((4-methoxypiperidin-1-yl)sulfonyl)phenoxy)-5-((3-methylbut-2-en-1-yl)oxy)benzamide
-
activation: 1.7fold
N-(5-isopropyl-4-methylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.13fold
N-(6,7-dihydro-4H-pyrano[4,3-d][1,3]thiazol-2-yl)-3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamide
-
maximal activation: 2.17fold
N-(6-fluorobenzo[d]thiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.3fold
N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine
-
addition of 0.02 mM N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine results in the loss of positive cooperativity with glucose and in activation of glucokinase catalysis increasing both kcat and the apparent glucose affinity
PF-04937319
-
maximal activation: 2.11fold
phosphoenolpyruvate
-
activates isoenzyme Hex I
propionyl-CoA carboxylase beta-subunit
-
-
-
ribose
-
activates isoenzyme Hex II
RO-1440
-
148% maximum activation above control at 6.5 mM glucose
RO-28-0450
-
racemic, activates the enzyme
RO-4389620
-
also known as R1440, GK2, or piragliatin
RO0274375
-
wild-type enzyme V62A, V62T, and V62L respond to the activator. V62Q, V62E, V62F, and V62K are resistant to the activators
RO0281675
-
wild-type enzyme V62A, V62T, and V62L respond to the activator. V62Q, V62E, V62F, and V62K are resistant to the activators
RO0283946
-
wild-type enzyme V62A, V62T, and V62L respond to the activator. V62Q, V62E, V62F, and V62K are resistant to the activators
-
tert-butyl (S)-2-(3-(4-(azetidine-1-carbonyl)phenoxy)-5-((1-methoxypropan-2-yl)oxy)benzamido)-6,7-dihydrothiazolo[5,4-c]pyridine-5(4H)-carboxylate
-
glucokinase activators are being developed for the treatment of type 2 diabetes mellitus. Glucokinase activators have risks of hypoglycemia caused by over-activation of glucokinase in islet cells and dyslipidemia caused by over-activation of intrahepatic glucokinase. In the effort to mitigate risks of hypoglycemia and dyslipidemia while maintaining the promising efficacy of glucokinase activator. tert-Butyl (S)-2-(3-(4-(azetidine-1-carbonyl)phenoxy)-5-((1-methoxypropan-2-yl)oxy)benzamido)-6,7-dihydrothiazolo[5,4-c]pyridine-5(4H)-carboxylate shows a good balance between in vitro potency and enzyme kinetic parameters, and protects beta-cells from streptozotocin-induced apoptosis. Chronic treatment of this compound demonstrates its potent activity in regulation of glucose homeostasis and low risk of dyslipidemia with diabetic db/db mice in oral glucose tolerance test. Acute treatment of this compound does not induce hypoglycemia in C57BL/6J mice even at 200 mg/kg via oral administration
tert-butyl 2-(3-[4-(azetidine-1-carbonyl)-3-fluorophenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.83 fold
tert-butyl 2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2R)-1-methoxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.96fold
tert-butyl 2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-hydroxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.62fold
tert-butyl 2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.65fold
tert-butyl 2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[5,4-b]pyridine-4(5H)-carboxylate
-
maximal activation: 1.8fold
tert-butyl 2-(3-[4-(azetidine-1-carbonyl)phenoxy]-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido)-6,7-dihydro[1,3]thiazolo[5,4-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.84fold
tert-butyl 2-(3-[[6-(azetidine-1-carbonyl)pyridin-3-yl]oxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido)-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.1fold
tert-butyl 2-(3-[[6-(methanesulfonyl)pyridin-3-yl]oxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido)-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 4.07fold
tert-butyl 2-[3-(3,5-difluorophenoxy)-5-[[(2S)-1-methoxypropan-2-yl]oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.72fold
tert-butyl 2-[3-(benzyloxy)-5-[4-(methanesulfonyl)phenoxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.3fold
tert-butyl 2-[3-(cyclohexyloxy)-5-[4-(methanesulfonyl)phenoxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 1.71fold
tert-butyl 2-[3-(cyclopentylmethoxy)-5-[4-(methanesulfonyl)phenoxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.11fold
tert-butyl 2-[3-(cyclopentyloxy)-5-[4-(methanesulfonyl)phenoxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 3.17fold
tert-butyl 2-[3-[2-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 1.89fold
tert-butyl 2-[3-[3-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.74fold
tert-butyl 2-[3-[4-(azetidine-1-carbonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.89fold
tert-butyl 2-[3-[4-(azetidine-1-sulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 3.26fold
tert-butyl 2-[3-[4-(cyclopropanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 3.12fold
tert-butyl 2-[3-[4-(dimethylcarbamoyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 1.91fold
tert-butyl 2-[3-[4-(ethanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.37fold
tert-butyl 2-[3-[4-(methanesulfonyl)phenoxy]-5-(2-methoxyethoxy)benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.3fold
tert-butyl 2-[3-[4-(methanesulfonyl)phenoxy]-5-[(1-methoxypropan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[5,4-c]pyridine-5(4H)-carboxylate
-
maximal activation: 2.94fold
tert-butyl 2-[3-[4-(methanesulfonyl)phenoxy]-5-[(propan-2-yl)oxy]benzamido]-6,7-dihydro[1,3]thiazolo[4,5-c]pyridine-5(4H)-carboxylate
-
maximal activation: 3.55fold
xylose
-
activates isoenzyme Hex II
2-amino-4-fluoro-5-((1-methyl-1H-imidazol-2-yl)thio)-N-(thiazol-2-yl)benzamide
-
-
2-amino-4-fluoro-5-((1-methyl-1H-imidazol-2-yl)thio)-N-(thiazol-2-yl)benzamide
-
1.6fold change in Vmax or kcat at 0.03 mM
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-thiazol-2-yl-benzamide
-
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-thiazol-2-yl-benzamide
potent synthetic allosteric activator, acts on the wild-type and the N-terminal deletion mutants DELTA N1-11 and DELTA N1-15, mechanism of activation
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
activator associates with glucokinase in a glucose-independent fashion. Kinetic assays reveal a lag in enzyme progress curves that is systematically reduced when the enzyme is preincubated with the activator. Activator binding is enthalpically driven. The kcat value of glucokinase is almost fully limited by product release, both in the presence and absence of activator
2-amino-N-(4-methyl-1,3-thiazol-2-yl)-5-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]benzamide
-
-
6-(3-(((S)-1-methoxypropan-2-yl)oxy)-5-(((S)-1-phenylpropan-2-yl)oxy)benzamido)nicotinic acid
-
23% maximum activation above control at 6.5 mM glucose
6-(3-(((S)-1-methoxypropan-2-yl)oxy)-5-(((S)-1-phenylpropan-2-yl)oxy)benzamido)nicotinic acid
-
GKA50, 0.94fold change in Vmax or kcat at 0.03 mM
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
-
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
-
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
-
-
GKA50
-
-
glucokinase-associated protein
-
stimulates glucokinase activity by 30-40% when present at a 3-5fold molar excess and 2.5fold at a 50fold molar excess
-
glucokinase-associated protein
-
stimulates glucokinase activity by 30-40% when present at a 3-5fold molar excess and 2.5fold at a 50fold molar excess
-
glucokinase-associated protein
-
stimulates glucokinase activity by 30-40% when present at a 3-5fold molar excess and 2.5fold at a 50fold molar excess
-
LY-2121260
-
-
LY-2121260
-
addition of 0.02 mM LY-2121260 results in the loss of positive cooperativity with glucose and in activation of glucokinase catalysis increasing both kcat and the apparent glucose affinity
pentaubiquitin
-
the recombinant glucokinase is allosterically activated up to 1.4fold by purified free pentaubiquitin chains at about 100 nM, and possibly also by unidentified polyubiquitinated proteins
-
polyubiquitin
-
causes modest activation
-
polyubiquitin
-
causes modest activation
-
polyubiquitin
-
causes modest activation
-
RO-0281675
-
-
RO-0281675
-
81% maximum activation above control at 6.5 mM glucose
RO-28-1675
-
R-enantiomer, highly activates the enzyme by elevating Vmax 1.5fold and decreasing Km about 4fold, reverses enzyme inhibition by human glucokinase regulatory protein, the S-enantiomer is inactive
RO-28-1675
-
reduced blood glucose level in vivo after feeding to type 2 diabetic mice
RO-28-1675
-
lowers the threshold concentration of D-glucose required for insulin release from 7 mM to 3 mM in pancreatic islets in vivo, reduced blood glucose level in vivo after feeding to type 2 diabetic Goto-Kakizaki rats and supresses endogenous glucose production in ZDF-Gmi rats
additional information
-
RO-28-1674 is inactive
-
additional information
-
RO-28-1674 is inactive
-
additional information
-
increased activity of the cytosolic and non-cytosolic isozymes induced by tobacco mosaic virus TMV
-
additional information
-
the allosteric activator compound A, increases the level of cytoplasmic glucokinase in both isolated rat primary hepatocytes and the liver tissues from rats. Compound A interacts with glucose-bound free GK, thereby impairing the association of glucokinase and glucokinase regulatory protein
-
additional information
-
not affected by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-
additional information
hxk1+ expression increases strongly during growth in fructose or glycerol
-
additional information
hxk1+ expression increases strongly during growth in fructose or glycerol
-
additional information
-
hxk1+ expression increases strongly during growth in fructose or glycerol
-
additional information
hxk2+ expression is highest during growth in glycerol
-
additional information
hxk2+ expression is highest during growth in glycerol
-
additional information
-
hxk2+ expression is highest during growth in glycerol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
20
1,5-anhydro-D-glucitol
-
at 37°C, pH 7.4
5
1-thio-D-glucose
-
at 37°C, pH 7.4
0.2
2-deoxy-2-fluoro-D-glucose
0.033 - 19.2
2-deoxy-D-glucose
18
2-deoxyglucose
-
30°C, pH 7.5, wild-type
0.055 - 0.174
2-fluoro-2-deoxy-D-glucose
30
3-deoxy-3-amino-D-glucose
-
at 37°C, pH 7.4
105
D-galactose
pH 7.0, 50°C
5
D-mannosamine
-
at 37°C, pH 7.4
0.32 - 41.6
N-acetyl-D-glucosamine
additional information
additional information
-
0.2
2-deoxy-2-fluoro-D-glucose
-
at 37°C, pH 7.4
0.2
2-deoxy-2-fluoro-D-glucose
-
at 37°C, pH 7.4
0.033
2-deoxy-D-glucose
-
hexokinase III, at 30°C, pH 8.1
0.1
2-deoxy-D-glucose
-
rat brain enzyme, hexokinase I
0.125
2-deoxy-D-glucose
-
-
0.125
2-deoxy-D-glucose
-
bovine heart enzyme, hexokinase II
0.134
2-deoxy-D-glucose
-
at 30°C, pH 8.1
0.152
2-deoxy-D-glucose
-
HKI, at 25°C, pH 7.4
0.18
2-deoxy-D-glucose
-
HKI, at 25°C, pH 7.4
0.187
2-deoxy-D-glucose
at 50°C, pH 7.5
0.33
2-deoxy-D-glucose
-
90°C, pH 6.2
0.44
2-deoxy-D-glucose
pH 7.5, 50°C, ATP as phosphoryl donor
0.5
2-deoxy-D-glucose
-
hexokinase I, at 37°C, pH 8.1
0.56
2-deoxy-D-glucose
-
hexokinase Ib, at 37°C, pH 7.2
0.613
2-deoxy-D-glucose
-
HKII, at 25°C, pH 7.4
0.77
2-deoxy-D-glucose
-
hexokinase Ia, at 37°C, pH 7.2
0.9
2-deoxy-D-glucose
-
hexokinase Ia
1.16
2-deoxy-D-glucose
-
hexokinase Ic, at 37°C, pH 7.2
1.33
2-deoxy-D-glucose
-
erythrocyte enzyme
1.9
2-deoxy-D-glucose
-
30°C, pH 7.5, S151A
2
2-deoxy-D-glucose
-
at 37°C, pH 8.1
2
2-deoxy-D-glucose
-
hexokinase Ib
3.6
2-deoxy-D-glucose
-
-
5.66
2-deoxy-D-glucose
wild-type, pH 9.0, 36°C
9
2-deoxy-D-glucose
-
rat liver enzyme, hexokinase IV
19.2
2-deoxy-D-glucose
-
pH 8.0, 30°C
0.055 - 0.062
2-fluoro-2-deoxy-D-glucose
-
HK I, at 25°C, pH 7.4
0.068 - 0.077
2-fluoro-2-deoxy-D-glucose
-
HK I, at 25°C, pH 7.4
0.166 - 0.174
2-fluoro-2-deoxy-D-glucose
-
HK II, at 25°C, pH 7.4
0.00000023
ATP
-
wild-type in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.0000003
ATP
-
mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.00000035
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
0.00000046
ATP
-
wild-type, pH and temperature not specified in the publication
0.00000049
ATP
-
mutant W99R/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000055
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
0.00000057
ATP
-
wild-type in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000071
ATP
-
mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.00000071
ATP
-
mutant W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication
0.00000078
ATP
-
mutant W99R/W257F, pH and temperature not specified in the publication
0.00000109
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
0.00000143
ATP
-
mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000143
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
0.00000163
ATP
-
mutant W167F/W257F, pH and temperature not specified in the publication
0.00000294
ATP
-
mutant W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication
0.00000335
ATP
-
mutant W99R/W167F, pH and temperature not specified in the publication
0.04
ATP
-
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
0.07
ATP
-
mutant enzyme V62E
0.075
ATP
-
MgATP2-, bound mitochondrial HK I, at pH 7.5
0.11
ATP
-
mutant enzyme V62Q
0.12
ATP
pH 7.5, 50°C, D-glucose as phosphoryl acceptor
0.125
ATP
-
MgATP2-, at 30°C, pH 8.1
0.14
ATP
-
cosubstrate: glucose, wild-type enzyme
0.14
ATP
-
enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
0.16
ATP
-
mutant enzyme V62K
0.16
ATP
mutant enzyme V182L, glutathione S-transferase glucokinase B fusion protein
0.16
ATP
-
wild-type, 37°C, pH not specified in the puclication
0.16
ATP
-
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
0.16
ATP
-
enzyme from hepatopancreas, pH 7.5, 22°C
0.181
ATP
-
MgATP2-, solubilized mitochondrial HK I, at pH 7.5
0.183
ATP
-
recombinant HXK1, at 30°C, pH 8
0.2
ATP
-
mutant enzyme V62A
0.2
ATP
deletion mutant lacking residues 66-71, pH 7.6, 25 °C
0.2
ATP
deletion mutant lacking residues 68-71, pH 7.6, 25 °C
0.21
ATP
mutant enzyme Y61S, glutathione S-transferase glucokinase B fusion protein
0.22
ATP
-
mutant enzyme V62T
0.22
ATP
-
pH 6.5, temperature not specified in the publication
0.226
ATP
pH 7.4, 25°C, recombinant enzyme at 0.001 mg/ml
0.239
ATP
-
control, pH 8.2, 25°C, 250 mM glucose
0.24
ATP
-
mutant L146R, 37°C, pH not specified in the puclication
0.24
ATP
-
enzyme from foot muscle, pH 7.5, 22°C
0.248
ATP
-
control, pH 8.2, 25°C
0.248
ATP
-
control, pH 8.2, 25°C, no glucose
0.257
ATP
-
control, pH 8.2, 5°C, 250 mM glucose
0.27
ATP
-
30°C, pH 7.5, N166R
0.28
ATP
-
30°C, mutant enzyme A456V
0.28
ATP
recombinant TbHK1
0.28
ATP
-
pH 7.4, temperature not specified in the publication
0.29
ATP
-
30°C, mutant enzyme >214C
0.29
ATP
-
37°C, pH 7.4, mutant enzyme A456V
0.29
ATP
deletion mutant lacking residue 71, pH 7.6, 25 °C
0.3
ATP
-
recombinant hexokinase I expressed in Escherichia coli
0.3
ATP
-
hexokinase II, at 30°C, pH 8.1
0.3
ATP
wild type enzyme, in 25 mM HEPES (pH 7.1), at 25°C
0.3
ATP
deletion mutant lacking residues 67-71, pH 7.6, 25 °C
0.3 - 0.4
ATP
-
pH and temperature not specified in the publication
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
0.33
ATP
-
frozen, pH 8.2, 25°C
0.33
ATP
-
frozen, pH 8.2, 25°C, no glucose
0.336
ATP
-
frozen, pH 8.2, 5°C, 250 mM glucose
0.342
ATP
-
frozen, pH 8.2, 25°C, 250 mM glucose
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
0.364
ATP
-
control, pH 8.2, 5°C, no glucose
0.38
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V455M
0.39
ATP
pH 7.4, 25°C, recombinant enzyme at 1.0 mg/ml
0.39
ATP
-
37°C, pH 7.4, wild-type enzyme
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
-
wild-type enzyme
0.41
ATP
-
30°C, wild-type enzyme
0.41
ATP
mutant enzyme K420E, glutathione S-transferase glucokinase B fusion protein
0.43
ATP
-
30°C, mutant enzyme A208G
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
0.45 - 0.47
ATP
-
HK I and its D84A mutant
0.46
ATP
-
mutant enzyme V62M
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
-
hexokinase III, at 30°C, pH 8.1
0.5
ATP
-
at 30°C, pH 7.5
0.5
ATP
-
reticulocyte and erythrocyte enzymes
0.5
ATP
-
reticulocyte hexokinase Ia and Ib, at 37°C, pH 8.1
0.5
ATP
mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C
0.5
ATP
wild-type, pH 7.6, 25 °C
0.505
ATP
-
frozen, pH 8.2, 5°C, no glucose
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
0.55
ATP
-
30°C, mutant enzyme A460R
0.55
ATP
-
enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C
0.56
ATP
-
ATP in form of MgATP2-
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
0.58 - 0.62
ATP
-
MgATP2-, hexokinases Ia, Ib and Ic, at 37°C, pH 7.2
0.6
ATP
-
MgATP2-, erythrocyte enzyme
0.6
ATP
-
MgATP, hexokinase I, at 37°C, pH 8.1
0.6
ATP
-
30°C, mutant enzyme K459L
0.61
ATP
-
mutant enzyme V62L
0.62
ATP
-
MgATP2-, at 37°C, pH 8.1
0.63
ATP
-
30°C, pH 7.5, wild-type
0.63
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S263P
0.65
ATP
-
30°C, mutant enzyme C457V
0.65
ATP
-
30°C, mutant enzyme Y215A
0.654
ATP
-
recombinant HXK2, at 30°C, pH 8
0.66 - 1.2
ATP
wild-type and nonaggregating interface mutant hexokinase I, pH 7.8
0.67
ATP
pH 7.2, 37°C, recombinant full length enzyme
0.67
ATP
ATP in form of MgATP2-
0.673
ATP
pH 7.5, temperature not specified in the publication
0.69
ATP
mutant enzyme A379V, glutathione S-transferase glucokinase B fusion protein
0.7
ATP
-
type II isozyme
0.7
ATP
-
wild type enzyme, at 25°C
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
0.71
ATP
-
hexokinase III
0.71
ATP
-
mutant enzyme V62F
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
0.81
ATP
-
30°C, mutant enzyme K458R
0.81
ATP
-
wild type hexokinase II
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
0.98
ATP
pH 7.2, 37°C, recombinant catalytic C-terminal domain
0.98
ATP
ATP in form of MgATP2-
1.08
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214C
1.09
ATP
-
pH 8.0, wild-type enzyme
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
-
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
1.16
ATP
-
pH 8.0, mutant enzyme A464P/E465G
1.2
ATP
deletion mutant lacking residues 70-71, pH 7.6, 25 °C
1.25
ATP
-
hexokinase III from lymphocytes, at 37°C, pH 8.1
1.3 - 1.4
ATP
-
HK I+ and its D84A mutant
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
1.51
ATP
-
pH 8.0, mutant enzyme Q466_H467insHMNLAEQ
1.52
ATP
-
30°C, pH 7.5, N166R-S151A
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
1.73
ATP
-
37°C, pH 7.4, mutant enzyme K414E
2.08
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant P417R
2.21
ATP
-
30°C, pH 7.5, S151A
2.26
ATP
-
30°C, pH 7.5, S151G
2.6
ATP
-
30°C, pH 7.5, S151C
2.71
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T
3.05
ATP
-
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
4.21
ATP
-
enzyme isolated from dehydrated frogs, pH 8.0, 22°C
12.6
ATP
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S336L
0.52
CTP
pH 7.5, 50°C, D-glucose as phosphoryl acceptor
5
CTP
-
MgCTP2-, hexokinase I, at 37°C, pH 8.1
0.025
D-fructose
pH 8.4, 30°C, recombinant isozyme hexokinase 2
0.035
D-fructose
recombinant TbHK1
0.15
D-fructose
-
90°C, pH 6.2
0.33
D-fructose
-
hexokinases PI and PII
0.47
D-fructose
-
isozyme HKII
0.5
D-fructose
-
41°C, pH 7.5
0.734
D-fructose
at 50°C, pH 7.5
0.9
D-fructose
-
at 30°C, pH 7.5
1.1
D-fructose
pH 7.5, 37°C
1.44
D-fructose
-
at 30°C, pH 8.1
1.5
D-fructose
-
hexokinase III, at 30°C, pH 8.1
2
D-fructose
-
25°C, pH 7.5
2.5
D-fructose
-
isozyme HKI
2.9
D-fructose
S-nitrosoglutathione treated enzyme
3.625
D-fructose
pH 7.0, 22°C
4
D-fructose
-
hexokinase Ia
4.5
D-fructose
-
at 37°C, pH 8.1
4.567
D-fructose
pH 7.6, 22°C
4.7
D-fructose
-
30°C, pH 7.5, N166R-S151A
5.145
D-fructose
pH 8.2, 22°C
5.2
D-fructose
30°C, pH 8.0
6.49
D-fructose
pH 7.5, temperature not specified in the publication
7.7
D-fructose
-
30°C, pH 7.5, S151G
9.3
D-fructose
-
hexokinase
10 - 13
D-fructose
-
hexokinases Ia, Ib and Ic, at 37°C, pH 7.2
11.4
D-fructose
-
hexokinase I, at 37°C, pH 8.1
13.76
D-fructose
wild-type, pH 9.0, 36°C
17.8
D-fructose
-
erythrocyte enzyme
25
D-fructose
-
hexokinase Ib
30
D-fructose
pH 7.5, 50°C, ATP as phosphoryl donor
57.3
D-fructose
-
30°C, pH 7.5, S151A
77
D-fructose
-
30°C, pH 7.5, N166R
79
D-fructose
pH 8.0, 30°C
157.7
D-fructose
-
30°C, pH 7.5
240
D-fructose
-
30°C, pH 7.5, wild-type and S151C
1510
D-fructose
pH 7.0, 50°C
0.06
D-glucosamine
-
at 30°C, pH 7.5
0.06
D-glucosamine
-
90°C, pH 6.2
0.116
D-glucosamine
-
at 30°C, pH 8.1
0.2
D-glucosamine
-
hexokinase III, at 30°C, pH 8.1
0.23
D-glucosamine
pH 7.5, 50°C, ATP as phosphoryl donor
0.4
D-glucosamine
-
at 37°C, pH 8.1
0.5
D-glucosamine
-
hexokinases Ib and Ic, at 37°C, pH 7.2
0.6
D-glucosamine
-
hexokinase I, at 37°C, pH 8.1
0.85
D-glucosamine
-
hexokinase Ia
1.3
D-glucosamine
-
hexokinase Ib
1.5
D-glucosamine
-
hexokinase Ia, at 37°C, pH 7.2
2
D-glucosamine
-
erythrocyte enzyme
0.003
D-glucose
-
type III isozyme
0.008
D-glucose
at 37°C, pH 7
0.009
D-glucose
recombinant TbHK1
0.012
D-glucose
-
at 30°C, pH 8.1
0.015
D-glucose
-
hexokinase III, at 30°C, pH 8.1
0.023
D-glucose
30°C, pH 8.0
0.025
D-glucose
-
hexokinase C
0.03
D-glucose
-
type I isozyme
0.032
D-glucose
-
recombinant hexokinase I expressed in Escherichia coli
0.032 - 0.034
D-glucose
-
HK I, at 25°C, pH 7.4
0.0338
D-glucose
pH 7.0, 22°C
0.034
D-glucose
-
hexokinase III from lymphocytes, at 37°C, pH 8.1
0.034
D-glucose
pH 8.2, 22°C
0.035
D-glucose
-
hexokinase III
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
0.03872
D-glucose
pH 7.6, 22°C
0.039
D-glucose
-
HK I, at 25°C, pH 7.4
0.04
D-glucose
-
reticulocyte hexokinase Ia
0.04
D-glucose
-
glucokinase
0.04
D-glucose
-
at 37°C, pH 8.1
0.04 - 0.06
D-glucose
-
pH and temperature not specified in the publication
0.043
D-glucose
natural hexokinase from epimastigotes, at pH 7.5
0.044
D-glucose
-
90°C, pH 6.2
0.045
D-glucose
pH 8.0, 30°C
0.046 - 0.048
D-glucose
-
hexokinases Ia, Ib and Ic, at 37°C, pH 7.2
0.047
D-glucose
-
recombinant HXK2, at 30°C, pH 8
0.047
D-glucose
pH 7.2, 37°C, recombinant catalytic C-terminal domain
0.05
D-glucose
-
at 30°C, pH 7.5
0.05
D-glucose
pH 7.5, 50°C, ATP as phosphoryl donor
0.05 - 0.053
D-glucose
-
HK I, HKI+ and their D84A mutants
0.057 - 0.061
D-glucose
wild-type and nonaggregating interface mutant hexokinase I, pH 7.8
0.058
D-glucose
at 50°C, pH 7.5
0.059
D-glucose
-
recombinant HXK1, at 30°C, pH 8
0.059
D-glucose
-
enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
0.06
D-glucose
-
erythrocyte enzyme
0.06
D-glucose
-
hexokinase I, at 37°C, pH 8.1
0.06
D-glucose
recombinant hexokinase expressed in Escherichia coli XL-1 Blue, at pH 7.5
0.06
D-glucose
pH 8.4, 30°C, recombinant isozyme hexokinase 2
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
0.065
D-glucose
-
pH 8.0, mutant enzyme A464P/E465G
0.072
D-glucose
pH 7.2, 37°C, recombinant full length enzyme
0.0732
D-glucose
-
pH 8.0, wild-type enzyme
0.08
D-glucose
-
at 37°C, pH 8.1
0.0841
D-glucose
-
pH 8.0, mutant enzyme Q466_H467insHMNLAEQ
0.091
D-glucose
-
enzyme from hepatopancreas, pH 7.5, 22°C
0.098
D-glucose
pH and temperature not specified in the publication
0.12
D-glucose
-
hexokinases PI and PII
0.125
D-glucose
-
at 37°C, pH 8.1
0.125
D-glucose
-
reticulocyte hexokinase Ib
0.129 - 0.137
D-glucose
-
HK II, at 25°C, pH 7.4
0.13
D-glucose
-
at pH 8.5
0.13
D-glucose
-
pH 7.5, 22°C
0.139
D-glucose
-
control, pH 8.2, 5°C, no glucose
0.144
D-glucose
-
control, pH 8.2, 25°C
0.144
D-glucose
-
control, pH 8.2, 25°C, no glucose
0.146
D-glucose
-
hexokinase II
0.15
D-glucose
-
hexokinase II, at 30°C, pH 8.1
0.15
D-glucose
-
30°C, pH 7.5, S151G and N1166R-S151A
0.15
D-glucose
-
enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C
0.15
D-glucose
-
enzyme from foot muscle, pH 7.5, 22°C
0.16
D-glucose
-
hexokinase B
0.183
D-glucose
pH 7.5, temperature not specified in the publication
0.196
D-glucose
pH 7.4, 25°C, recombinant enzyme at 0.001 mg/ml
0.23
D-glucose
-
mutant enzyme Y214C
0.248
D-glucose
-
frozen, pH 8.2, 25°C
0.248
D-glucose
-
frozen, pH 8.2, 25°C, no glucose
0.253
D-glucose
-
frozen, pH 8.2, 5°C, no glucose
0.26
D-glucose
pH 7.5, 37°C
0.28
D-glucose
pH 7.0, 50°C
0.3
D-glucose
-
type II isozyme
0.3
D-glucose
S-nitrosoglutathione treated enzyme
0.34
D-glucose
-
30°C, pH 7.5, S151A
0.37
D-glucose
-
wild type hexokinase II
0.42
D-glucose
pH and temperature not specified in the publication
0.451
D-glucose
pH 7.4, 25°C, recombinant enzyme at 1.0 mg/ml
0.63
D-glucose
-
wild type enzyme, at 25°C, in the presence of 0.02 mM activator LY-2121260
0.67
D-glucose
wild-type, pH 9.0, 36°C
0.74
D-glucose
-
pH 8.0, 22°C
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
0.98
D-glucose
-
hexokinase
1.25
D-glucose
-
isozyme HKI
1.83
D-glucose
-
enzyme isolated from dehydrated frogs, pH 8.0, 22°C
2
D-glucose
-
in presence of activator RO-28-1675
2 - 3
D-glucose
-
enzyme from active animals, S0.5 value, Hill coefficient 1.16, pH 7.8, 2°C
2.1
D-glucose
-
30°C, pH 7.5, S151C and N166R
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
3.8
D-glucose
-
30°C, pH 7.5
5.5
D-glucose
-
hexokinase IV
6
D-glucose
-
30°C, pH 7.5, wild-type
6.23
D-glucose
-
enzyme from active animals, S0.5 value, Hill coefficient 1.7, pH 7.8, 25°C
6.3
D-glucose
wild-type, K0.5 value, Hill coefficient 1.8, pH 7.6, 25 °C
7.4
D-glucose
-
31°C and pH 7.7, fetal glucokinase
7.7
D-glucose
-
31°C and pH 7.7, adult glucokinase
8.6
D-glucose
-
in absence of activator
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
16.9
D-glucose
mutant D217H, pH 9.0, 36°C
26.4
D-glucose
mutant N216K, pH 9.0, 36°C
45
D-glucose
-
enzyme from hibernating animals, S0.5 value, Hill coefficient 1.2, pH 7.8, 2°C
0.014
D-mannose
-
hexokinase III, at 30°C, pH 8.1
0.01911
D-mannose
pH 7.0, 22°C
0.02164
D-mannose
pH 7.6, 22°C
0.02339
D-mannose
pH 8.2, 22°C
0.024
D-mannose
-
at 30°C, pH 8.1
0.03
D-mannose
30°C, pH 8.0
0.03
D-mannose
recombinant TbHK1
0.04
D-mannose
-
glucokinase
0.043
D-mannose
at 50°C, pH 7.5
0.06
D-mannose
-
at 30°C, pH 7.5
0.07 - 0.1
D-mannose
-
hexokinases Ia, Ib and Ic, at 37°C, pH 7.2
0.08
D-mannose
-
30°C, pH 7.5, N166R-S151A
0.1
D-mannose
-
at 37°C, pH 8.1
0.1
D-mannose
-
at 37°C, pH 8.1
0.1
D-mannose
-
hexokinase Ia
0.1
D-mannose
-
hexokinase I
0.109
D-mannose
pH 7.5, temperature not specified in the publication
0.11
D-mannose
-
90°C, pH 6.2
0.12
D-mannose
-
30°C, pH 7.5, S151G
0.13
D-mannose
pH 7.5, 50°C, ATP as phosphoryl donor
0.149
D-mannose
pH 8.4, 30°C, recombinant isozyme hexokinase 2
0.15
D-mannose
-
hexokinase Ib
0.21
D-mannose
-
30°C, pH 7.5, S151A
0.37
D-mannose
pH 7.0, 50°C
0.71
D-mannose
-
erythrocyte enzyme
1.03
D-mannose
-
recombinant HXK1, at 30°C, pH 8
2
D-mannose
-
recombinant HXK2, at 30°C, pH 8
2.2
D-mannose
-
30°C, pH 7.5, N166R
3.74
D-mannose
-
30°C, pH 7.5, S151C
4.4
D-mannose
-
30°C, pH 7.5, wild-type
4.6
D-mannose
-
30°C, pH 7.5
25.41
D-mannose
wild-type, pH 9.0, 36°C
0.231
GTP
30°C, pH 8.0
1.9
ITP
-
MgITP2-, erythrocyte enzyme
2.5
ITP
-
hexokinase III, at 30°C, pH 8.1
4.5
ITP
-
MgITP2-, hexokinase Ib
10
ITP
-
MgITP2-, at 37°C, pH 8.1
12
ITP
-
MgITP2-, hexokinase Ia
16.6
ITP
-
MgITP2-, hexokinase I, at 37°C, pH 8.1
0.32
N-acetyl-D-glucosamine
pH 7.5, 50°C, ATP as phosphoryl donor
41.6
N-acetyl-D-glucosamine
-
erythrocyte enzyme
0.288
UTP
-
-
5
UTP
-
MgUTP2-, hexokinase I, at 37°C, pH 8.1
30
UTP
-
MgUTP2-, at 37°C, pH 8.1
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
values for isoenzymes
-
additional information
additional information
-
of HXK1 mutants with modified active site
-
additional information
additional information
kinetics of isozyme hexokinase 2
-
additional information
additional information
-
kinetics of isozyme hexokinase 2
-
additional information
additional information
-
kinetics, mass spectrometry-based assay, overview, the Mg2+ concentration influence the kinetics
-
additional information
additional information
-
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
-
stopped-flow steady-state kinetics, dissociation constants of the monomer-homodimer equilibria
-
additional information
additional information
-
wild-type and mutant enzymes, cooperative/sigmoidal glucose-dependent kinetics
-
additional information
additional information
-
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
-
additional information
additional information
kinetic parameters of hexokinase activity in wine yeast strains
-
additional information
additional information
-
kinetic parameters of hexokinase activity in wine yeast strains
-
additional information
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
29 - 33.7
2-deoxy-D-glucose
0.00091 - 483.3
D-glucose
additional information
additional information
-
29
2-deoxy-D-glucose
-
wild-type enzyme
33.7
2-deoxy-D-glucose
wild-type, pH 9.0, 36°C
0.61
ATP
-
mutant L146R, 37°C, pH not specified in the puclication
0.7
ATP
-
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
2 - 3.7
ATP
-
37°C, pH 7.4, mutant enzyme A456V
4.92
ATP
-
mutant enzyme V62E
6.42
ATP
-
mutant enzyme V62K
9.5
ATP
pH 7.5, temperature not specified in the publication
11
ATP
-
37°C, pH 7.4, mutant enzyme K414E
14.9
ATP
-
mutant enzyme V62Q
25.7
ATP
-
mutant enzyme V62T
33.7
ATP
-
mutant enzyme V62F
43.1
ATP
-
mutant enzyme V62A
53.2
ATP
-
37°C, pH 7.4, wild-type enzyme
53.6
ATP
-
mutant enzyme V62M
54
ATP
-
wild type enzyme, at 25°C
59.9
ATP
-
mutant enzyme V62L
62.3
ATP
-
wild-type enzyme
68.4
ATP
-
wild-type, 37°C, pH not specified in the puclication
68.4
ATP
-
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
84.9
ATP
-
37°C, pH 7.4, mutant enzyme A456V
5.9
beta-D-glucose
-
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
-
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
-
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
-
co-substrate: ATP, mutant W167F/W257F, pH and temperature not specified in the publication
9.43
beta-D-glucose
-
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
-
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
-
co-substrate: ATP, mutant W99R/W167F, pH and temperature not specified in the publication
12.7
beta-D-glucose
-
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
-
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
-
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
-
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
-
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
-
co-substrate: ATP, mutant W99R/W257F, pH and temperature not specified in the publication
83.7
beta-D-glucose
-
co-substrate: ATP, wild-type, pH and temperature not specified in the publication
91.3
beta-D-glucose
-
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
-
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
1.5
D-fructose
wild-type, pH 9.0, 36°C
3.69
D-fructose
30°C, pH 8.0
0.00091
D-glucose
-
mutant enzyme D205A, kcat less than 0.00091 s-1
0.007
D-glucose
-
mutant T228M, 37°C, pH not specified in the puclication
0.026
D-glucose
deletion mutant lacking residues 68-71, pH 7.6, 25 °C
0.037
D-glucose
deletion mutant lacking residues 66-71, pH 7.6, 25 °C
0.042
D-glucose
deletion mutant lacking residues 67-71, pH 7.6, 25 °C
0.18
D-glucose
-
truncated enzyme with removed helix alpha13
0.77
D-glucose
-
mutant L146R, 37°C, pH not specified in the puclication
1.06
D-glucose
-
pH 7.5, 22°C, soluble enzyme
1.67
D-glucose
-
pH 7.5, 22°C, immobilized enzyme
2 - 3.7
D-glucose
-
37°C, pH 7.4, mutant enzyme A456V
2.46
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S336L
3.3
D-glucose
30°C, pH 8.0
3.47
D-glucose
at 37°C, pH 7
5.01
D-glucose
30°C, pH 8.0
10.8
D-glucose
mutant N216K, pH 9.0, 36°C
11
D-glucose
-
37°C, pH 7.4, mutant enzyme K414E
17.4
D-glucose
mutant enzyme W167F, in 25 mM HEPES (pH 7.4), at 37°C
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
D-glucose
-
wild type enzyme
29
D-glucose
deletion mutant lacking residues 70-71, pH 7.6, 25 °C
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
33
D-glucose
deletion mutant lacking residue 71, pH 7.6, 25 °C
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
D-glucose
-
glucokinase with C-terminal 5 alanine addition
37.7
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M298K
38
D-glucose
-
wild-type enzyme
38
D-glucose
-
glucokinase with C-terminal 10 alanine addition
39
D-glucose
-
mutant enzyme Y214C
39.7
D-glucose
mutant D217H, pH 9.0, 36°C
40
D-glucose
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K140E
40.1
D-glucose
wild-type, pH 7.6, 25 °C
42.1
D-glucose
mutant enzyme W257F, in 25 mM HEPES (pH 7.4), at 37°C
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
46.8
D-glucose
mutant enzyme W99F, in 25 mM HEPES (pH 7.4), at 37°C
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
53.2
D-glucose
-
37°C, pH 7.4, wild-type enzyme
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
60.4
D-glucose
wild type enzyme, in 25 mM HEPES (pH 7.4), at 37°C
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
-
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
67.6
D-glucose
-
wild-type, 37°C, pH not specified in the puclication
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
-
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
84.9
D-glucose
-
37°C, pH 7.4, mutant enzyme A456V
93.39
D-glucose
pH and temperature not specified in the publication
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
195
D-glucose
-
recombinant HXK2, at 30°C, pH 8
219
D-glucose
wild-type, pH 9.0, 36°C
284
D-glucose
-
recombinant HXK1, at 30°C, pH 8
483.3
D-glucose
recombinant TbHK1
0.025
D-mannose
wild-type, pH 9.0, 36°C
3.78
D-mannose
30°C, pH 8.0
12.1
D-mannose
pH 7.5, temperature not specified in the publication
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
6000/min, wild-type and nonaggregating interface mutant hexokinase I
-
additional information
additional information
-
6000/min, wild-type and nonaggregating interface mutant hexokinase I
-
additional information
additional information
natural hexokinase: 68160/min, recombinant hexokinase expressed in Escherichia coli XL-1 Blue: 18913/min, at pH 7.5
-
additional information
additional information
-
natural hexokinase: 68160/min, recombinant hexokinase expressed in Escherichia coli XL-1 Blue: 18913/min, at pH 7.5
-
additional information
additional information
-
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
-
additional information
additional information
-
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
-
additional information
additional information
kinetic parameters of hexokinase activity in wine yeast strains
-
additional information
additional information
-
kinetic parameters of hexokinase activity in wine yeast strains
-
additional information
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
32.8 - 36
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
0.0004 - 0.0012
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
0.0005 - 0.0028
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
0.01 - 32
1,5-Anhydro-D-glucitol 6-phosphate
5 - 14
2,3-diphosphoglycerate
0.0028 - 0.006
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
0.34 - 40.7
2-deoxy-D-glucose
13 - 14
2-phosphoglycerate
1.99
3-bromo-2-oxopropionic acid
-
-
12 - 21
3-phosphoglycerate
0.1 - 0.4
5-thio-D-glucose
50
6-deoxy-D-glucose
-
at 37°C, pH 7.4
0.015
atorvastatin
pH 8.5, 37°C
4.5
Cr(III)-ATP
-
pH 6.9, 30°C, versus MgATP2-
0.23
D-fructose
-
inhibition with respect to glucose
2.5 - 4.6
D-fructose 1,6-diphosphate
0.5 - 0.88
D-fructose 6-phosphate
0.033 - 3
D-Glucose 1,6-bisphosphate
0.04 - 22
D-glucose 1,6-diphosphate
0.015 - 4.1
D-glucose 6-phosphate
0.06
D-mannose
-
glucokinase
2.5
dihydroxyacetonephosphate
-
hexokinase III, at 30°C, pH 7.2
0.0000128 - 0.000113
GK regulatory protein
-
0.4
glucose 1,6-disphosphate
-
IC50
13 - 15
glucose 6-phosphate
-
hexokinase Ia, Ib and Ic, at 37°C, pH 7.2
0.015
indomethacin
pH 8.5, 37°C
0.3 - 0.7
N-acetyl-D-glucosamine
0.63 - 0.8
N-acetylglucosamine
50
N-acetylmannosamine
-
at 37°C, pH 7.4
0.0035 - 1.6
palmitoyl-CoA
8
phosphoenolpyruvate
-
hexokinase III, at 30°C, pH 7.2
0.012
trehalose 6-phosphate
pH 7.5, 37°C
3020 - 3021
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
22 - 2282
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
additional information
additional information
-
32.8
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
against ATP, Kis
33.3
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
against D-glucose, Kis
34.3
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
Kii
36
(2-pyridin-4-ylethane-1,1-diyl)bis(phosphonic acid)
-
against D-glucose, Kii
0.0004
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis
0.0006
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis
0.0012
(3-bromo-phenyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kii
0.0005
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis
0.0017
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis
0.0028
(9-ethyl-9H-3-carbazolyl)-aminomethylene-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kii
0.01 - 0.02
1,5-Anhydro-D-glucitol 6-phosphate
-
catalytically active 51 kDa C fragment of hexokinase
0.0107
1,5-Anhydro-D-glucitol 6-phosphate
-
pH 8.0, mutant enzyme A464P/E465G
0.0108
1,5-Anhydro-D-glucitol 6-phosphate
-
pH 8.0, mutant enzyme Q466_H467insHMNLAEQ
0.014
1,5-Anhydro-D-glucitol 6-phosphate
recombinant wild-type hexokinase I
0.0164
1,5-Anhydro-D-glucitol 6-phosphate
-
pH 8.0, wild-type enzyme
0.018
1,5-Anhydro-D-glucitol 6-phosphate
recombinant D84E mutant hexokinase I
0.028
1,5-Anhydro-D-glucitol 6-phosphate
recombinant D84K mutant hexokinase I
0.033
1,5-Anhydro-D-glucitol 6-phosphate
recombinant D84A mutant hexokinase I
0.5
1,5-Anhydro-D-glucitol 6-phosphate
-
at pH 8.5
5 - 6
1,5-Anhydro-D-glucitol 6-phosphate
-
HK I+ and its D84A mutant
15
1,5-Anhydro-D-glucitol 6-phosphate
nonaggregating interface mutant hexokinase I, pH 7.8
16
1,5-Anhydro-D-glucitol 6-phosphate
-
HK I
23
1,5-Anhydro-D-glucitol 6-phosphate
wild-type hexokinase I, pH 7.8
32
1,5-Anhydro-D-glucitol 6-phosphate
-
D84A mutant of HK I
5
2,3-diphosphoglycerate
-
hexokinase III, at 30°C, pH 7.2
14
2,3-diphosphoglycerate
-
at 30°C, pH 8.1
0.0028
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis
0.0033
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis
0.0043
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kii
0.006
2-(pyridin-4-yl)-1-hydroxyethane-1,1-bisphosphonate
-
varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kii
0.34
2-deoxy-D-glucose
pH 7.5, temperature not specified in the publication
0.5
2-deoxy-D-glucose
fructose as substrate
4
2-deoxy-D-glucose
fructose as substrate
40.7
2-deoxy-D-glucose
-
pH 8.0, 30°C, versus MgATP2-
13
2-phosphoglycerate
-
hexokinase III, at 30°C, pH 7.2
14
2-phosphoglycerate
-
at 30°C, pH 8.1
12
3-phosphoglycerate
-
hexokinase III, at 30°C, pH 7.2
21
3-phosphoglycerate
-
at 30°C, pH 8.1
0.1
5-thio-D-glucose
-
inhibition of fructose phosphorylation, at 37°C, pH 7.4
0.018
ADP
pH 7.5, 50°C
0.03
ADP
-
non-cytosolic hexokinase from root
0.03
ADP
-
root, non-cytosolic enzyme
0.036
ADP
-
recombinant HXK1, at 30°C, pH 8
0.122
ADP
-
pH 7.5, 22°C, versus ATP, dependennt on Mg2+ concentration
0.193
ADP
-
recombinant HXK2, at 30°C, pH 8
0.5
ADP
-
hexokinase III, at 30°C, pH 7.2
0.55
ADP
Q56VN6
substrate glucose
0.723
ADP
-
inhibition with respect to ATP
1.3
ADP
natural hexokinase from epimastigotes, at pH 7.5
1.5
ADP
-
competitive to ATP
1.5
ADP
-
versus MgATP2-, at 30°C, pH 8.1
3.6
ADP
-
versus glucose, at 30°C, pH 8.1
7
ADP
-
noncompetitive to glucose
0.00065
AMP
-
recombinant HXK1, at 30°C, pH 8
0.031
AMP
-
recombinant HXK2, at 30°C, pH 8
0.5
ATP
-
uncomplexed ATP4-, hexokinase III, at 30°C, pH 7.2
1.5
ATP
-
uncomplexed ATP, erythrocyte enzyme, competitive to MgATP2-
3.6
ATP
-
at 30°C, pH 8.1
2.5
D-fructose 1,6-diphosphate
-
hexokinase III, at 30°C, pH 7.2
4.6
D-fructose 1,6-diphosphate
-
at 30°C, pH 8.1
0.5
D-fructose 6-phosphate
-
hexokinase III, at 30°C, pH 7.2
0.88
D-fructose 6-phosphate
-
at 30°C, pH 8.1
2.1
D-glucosamine
fructose as substrate
11
D-glucosamine
fructose as substrate
0.033
D-Glucose 1,6-bisphosphate
pH 7.2, 37°C, recombinant catalytic C-terminal domain, versus MgATP2-
0.036
D-Glucose 1,6-bisphosphate
pH 7.2, 37°C, recombinant full length enzyme, versus MgATP2-
3
D-Glucose 1,6-bisphosphate
-
-
0.04
D-glucose 1,6-diphosphate
-
hexokinase III, at 30°C, pH 7.2
0.05 - 0.059
D-glucose 1,6-diphosphate
-
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
0.127
D-glucose 1,6-diphosphate
-
at 30°C, pH 8.1
21 - 22
D-glucose 1,6-diphosphate
-
hexokinase Ia, Ib and Ic, at 37°C, pH 7.2
0.015
D-glucose 6-phosphate
-
ATP
0.02
D-glucose 6-phosphate
-
type I and type II isozymes
0.025
D-glucose 6-phosphate
-
-
0.026
D-glucose 6-phosphate
-
hexose
0.029 - 0.037
D-glucose 6-phosphate
-
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
0.034
D-glucose 6-phosphate
-
at 30°C, pH 8.1
0.045
D-glucose 6-phosphate
pH 7.2, 37°C, recombinant full length enzyme
0.066
D-glucose 6-phosphate
pH 7.2, 37°C, recombinant catalytic C-terminal domain
0.1
D-glucose 6-phosphate
-
type III isozyme
0.12
D-glucose 6-phosphate
-
hexokinase III, at 30°C, pH 7.2
0.13
D-glucose 6-phosphate
-
catalytically active recombinant carboxyl-domain of hexokinase III, at 37°C, pH 7.2
0.15
D-glucose 6-phosphate
-
at pH 8.5
0.18
D-glucose 6-phosphate
-
hexokinase C, versus ATP, at 0.2 mM glucose
0.226
D-glucose 6-phosphate
-
hexokinase III from lymphocytes, at 37°C, pH 7.2
0.24
D-glucose 6-phosphate
-
wild type hexokinase II
0.43
D-glucose 6-phosphate
-
inhibition with respect to glucose
0.7
D-glucose 6-phosphate
-
inhibition with respect to ATP
1.4
D-glucose 6-phosphate
-
-
4
D-glucose 6-phosphate
pH 7, hexokinase 1
4.1
D-glucose 6-phosphate
-
HK1, at pH 7
0.85
D-xylose
-
glucokinase
25
D-xylose
-
hexokinase PI
80
D-xylose
-
hexokinase PII
0.009
diphosphate
Q56VN6
-
0.011
diphosphate
pH 8.0, 30°C
0.035
diphosphate
-
inhibition with respect to ATP
0.5
diphosphate
natural hexokinase from epimastigotes, at pH 7.5
0.7
diphosphate
recombinant hexokinase expressed in Escherichia coli, at pH 7.5
0.0000128
GK regulatory protein
-
steady-state Ki value, pH 7.1, 25°C
-
0.000113
GK regulatory protein
-
initial Ki value, pH 7.1, 25°C
-
0.5
mannoheptulose
-
non-cytoslic hexokinase from root
0.5
mannoheptulose
-
non-cytosolic enzyme
20
mannoheptulose
-
cytosolic enzyme
20
mannoheptulose
-
cytosolic hexokinase from root
9
Mg2+
-
erythrocyte enzyme, uncomplexed Mg2+
30
Mg2+
-
uncomplexed, hexokinase III, at 30°C, pH 7.2
36
Mg2+
-
at 30°C, pH 8.1
3
MgADP-
-
erythrocyte enzyme, mixed inhibitor versus MgATP2-
7.8
MgADP-
-
erythrocyte enzyme, mixed inhibitor versus glucose
0.3
N-acetyl-D-glucosamine
-
-
0.7
N-acetyl-D-glucosamine
-
erythrocyte enzyme, competitive to glucose
0.63
N-acetylglucosamine
-
pH 8.0, 30°C, versus 2-deoxyglucose
0.8
N-acetylglucosamine
-
pH 8.0, 30°C, versus MgATP2-
4.87
Ni2+
-
pH 7.6, 37°C, versus ATP
9.97
Ni2+
-
pH 7.6, 37°C, versus D-glucose
0.0035
palmitoyl-CoA
-
-
5.3
phosphate
-
-
6
phosphate
-
catalytically active 51 kDa C fragment of hexokinase, versus ATP
7.8
phosphate
-
hexokinase III, at 30°C, pH 7.2
13
phosphate
recombinant D84K mutant hexokinase I
15
phosphate
recombinant D84E mutant hexokinase I
17
phosphate
recombinant wild-type hexokinase I
17.9
phosphate
-
at 30°C, pH 8.1
18
phosphate
recombinant D84A mutant hexokinase I
33
phosphate
-
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
35
phosphate
-
intact hexokinase I
60
phosphate
-
catalytically active 51 kDa C fragment of hexokinase, versus glucose
3020
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
-
against D-glucose, Kis
3021
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
-
against ATP, Kii
3021
[[(3-bromophenyl)amino]methylene]bis(phosphonic acid)
-
against ATP, Kis
22 - 83
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
against ATP, Kii
2281
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
against D-glucose, Kis
2282
[[(9-ethyl-9H-carbazol-3-yl)amino]methylene]bis(phosphonic acid)
-
against ATP, Kis
additional information
additional information
-
-
-
additional information
additional information
-
inhibition kinetics, overview
-
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0.0274
(1R)-6-bromo-3-ethenyl-1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol
Plasmodium falciparum
pH 7.9, 22°C
0.00206
(22E,24R)-6beta-methoxyergosta-7,9(11),22-triene-3beta,5alpha-diol
Homo sapiens
pH and temperature not specified in the publication
0.00102
2,5-dihydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00027 - 0.0011
2-(4-chlorophenyl)-1,2-benzothiazol-3(2H)-one
0.00016 - 0.0038
2-(4-chlorophenyl)-5-fluoro-1,2-benzothiazol-3(2H)-one
5.75
2-deoxy-D-glucose
Cryptosporidium parvum
pH 7.5, temperature not specified in the publication
0.00207
2-hydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00023 - 0.002
2-phenyl-1,2-benzothiazol-3(2H)-one
0.000025 - 0.000032
2-[([1,1'-biphenyl]-3-carbonyl)amino]-2,6-dideoxy-6-[(2,3-dichlorobenzene-1-sulfonyl)amino]-D-glucopyranose
0.01452
22E-6beta-methoxyergosta-7,22-diene-3beta,5alpha-diol
Homo sapiens
pH and temperature not specified in the publication
0.00419
3-(methanesulfonyl)-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
3.39
3-bromo-2-oxopropionic acid
Saccharomyces cerevisiae
-
-
0.026
3-Bromopyruvate
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00108
3-chloro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00589
3-methoxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
-
0.0007
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00151
4-(2-hydroxyethoxy)-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00332
4-(methanesulfonyl)-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00115
4-butyl-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00117
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00098
4-chloro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00516
4-fluoro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00521
4-methoxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00053
4-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0031
5-fluoro-N-phenyl-2-sulfanylbenzamide
Plasmodium falciparum
pH and temperature not specified in the publication
0.0023
5-hydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-2,3-dihydro-1H-indole-2-carbohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00001 - 0.00002
5-[[(2R,3S,4R,5R,6S)-5-[(3-bromophenyl)carbonylamino]-3,4,6-tris(oxidanyl)oxan-2-yl]methylsulfamoyl]-2-methyl-furan-3-carboxylic acid
0.00126
6-hydroxy-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.044
atorvastatin
Homo sapiens
pH 8.5, 37°C
0.00552
Benserazide
Homo sapiens
pH and temperature not specified in the publication
0.077
chlorpromazine
Homo sapiens
pH 8.5, 37°C
0.006
clozapine
Homo sapiens
pH 8.5, 37°C
0.033
diltiazem
Homo sapiens
pH 8.5, 37°C
0.0011
dimethyl 2-[[(2E)-3-(4-ethoxyphenyl)prop-2-enoyl]amino]-5,6-dihydro-4H-cyclopenta[b]thiophene-3,4-dicarboxylate
Plasmodium falciparum
pH 7.9, 22°C
0.0019
dimethyl 2-[[4-(3-methylphenoxy)butanoyl]amino]-5,6-dihydro-4H-cyclopenta[b]thiophene-3,4-dicarboxylate
Plasmodium falciparum
pH 7.9, 22°C
0.00001 - 0.00005
ebselen
0.01
enalaprilat
Homo sapiens
pH 8.5, 37°C
0.03
gabapentin
Homo sapiens
pH 8.5, 37°C
0.008
gatifloxacin
Homo sapiens
pH 8.5, 37°C
0.005
indomethacin
Homo sapiens
pH 8.5, 37°C
0.0758
lauric acid
Trypanosoma brucei
IC50: 0.0758 mM, TbHK1
0.85
lonidamine
Trypanosoma brucei
-
recombinant enzyme
0.086
mangiferin
Eimeria tenella
pH 9.0, 36°C
0.0784
myristic acid
Trypanosoma brucei
IC50: 0.0784 mM, TbHK1
0.00074
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00108
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00172
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]pyridine-3-carbohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00643
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]pyridine-4-carbohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00069
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]quinoline-2-carbohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0048
N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]thiophene-2-carbohydrazide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00026
N,N'-[furan-2,5-diylbis(2-chloro-4,1-phenylene)]diguanidine
Homo sapiens
pH and temperature not specified in the publication
0.00202
N-(4-[(2E)-2-[(2,3,4-trihydroxyphenyl)methylidene]hydrazinecarbonyl]phenyl)cyclopropanecarboxamide
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0624
palmitic acid
Trypanosoma brucei
IC50: 0.0624 mM, TbHK1
0.007
quercetin
Eimeria tenella
pH 9.0, 36°C
0.034
Valproic acid
Homo sapiens
pH 8.5, 37°C
0.00817
ZINC03232404
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00939
ZINC03233449
Homo sapiens
pH 8.0, temperature not specified in the publication
0.0101
ZINC39948337
Homo sapiens
pH 8.0, temperature not specified in the publication
0.00027
2-(4-chlorophenyl)-1,2-benzothiazol-3(2H)-one
Plasmodium falciparum
pH and temperature not specified in the publication
0.0011
2-(4-chlorophenyl)-1,2-benzothiazol-3(2H)-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00016
2-(4-chlorophenyl)-5-fluoro-1,2-benzothiazol-3(2H)-one
Plasmodium falciparum
pH and temperature not specified in the publication
0.0038
2-(4-chlorophenyl)-5-fluoro-1,2-benzothiazol-3(2H)-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00023
2-phenyl-1,2-benzothiazol-3(2H)-one
Plasmodium falciparum
pH and temperature not specified in the publication
0.002
2-phenyl-1,2-benzothiazol-3(2H)-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.000025
2-[([1,1'-biphenyl]-3-carbonyl)amino]-2,6-dideoxy-6-[(2,3-dichlorobenzene-1-sulfonyl)amino]-D-glucopyranose
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000032
2-[([1,1'-biphenyl]-3-carbonyl)amino]-2,6-dideoxy-6-[(2,3-dichlorobenzene-1-sulfonyl)amino]-D-glucopyranose
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00001
5-[[(2R,3S,4R,5R,6S)-5-[(3-bromophenyl)carbonylamino]-3,4,6-tris(oxidanyl)oxan-2-yl]methylsulfamoyl]-2-methyl-furan-3-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00002
5-[[(2R,3S,4R,5R,6S)-5-[(3-bromophenyl)carbonylamino]-3,4,6-tris(oxidanyl)oxan-2-yl]methylsulfamoyl]-2-methyl-furan-3-carboxylic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
4.2
ADP
Trypanosoma brucei
-
pH 6.5, temperature not specified in the publication
10
ADP
Trypanosoma brucei
-
pH 7.4, temperature not specified in the publication
0.00001
ebselen
Plasmodium falciparum
pH and temperature not specified in the publication
0.00005
ebselen
Trypanosoma brucei
-
pH and temperature not specified in the publication
260
KCl
Littorina littorea
-
enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
260
KCl
Littorina littorea
-
enzyme from hepatopancreas, pH 7.5, 22°C
280
KCl
Littorina littorea
-
enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C
280
KCl
Littorina littorea
-
enzyme from foot muscle, pH 7.5, 22°C
240
NaCl
Littorina littorea
-
enzyme from hepatopancreas, pH 7.5, 22°C
280
NaCl
Littorina littorea
-
enzyme from foot muscle, pH 7.5, 22°C
290
NaCl
Littorina littorea
-
enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
300
NaCl
Littorina littorea
-
enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C
190
NH4Cl
Littorina littorea
-
enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C
210
NH4Cl
Littorina littorea
-
enzyme from foot muscle, pH 7.5, 22°C
230
NH4Cl
Littorina littorea
-
enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
230
NH4Cl
Littorina littorea
-
enzyme from hepatopancreas, pH 7.5, 22°C
0.0045
Urea
Lithobates sylvaticus
-
frozen, pH 8.2, 25°C
0.0053
Urea
Lithobates sylvaticus
-
control, pH 8.2, 25°C
990
Urea
Littorina littorea
-
enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C
1170
Urea
Littorina littorea
-
enzyme from foot muscle, pH 7.5, 22°C
1230
Urea
Xenopus laevis
-
pH 8.0, 22°C
1310
Urea
Littorina littorea
-
enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C
1380
Urea
Xenopus laevis
-
enzyme isolated from dehydrated frogs, pH 8.0, 22°C
1490
Urea
Littorina littorea
-
enzyme from hepatopancreas, pH 7.5, 22°C
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drug target
given the absence of energy stores in this parasite and the key role of the Plasmodium falciparum hexose transporter, the pathway involving Plasmodium falciparum hexokinase and the bifunctional glucose-6-phosphate dehydrogenase 6-phosphogluconolactonase is promising as a pharmacotherapeutic target, particularly because Plasmodium falciparum hexokinase shows a low sequence identity with human hexokinases
drug target
-
glucokinase activators are being developed for the treatment of type 2 diabetes mellitus. Glucokinase activators have risks of hypoglycemia caused by over-activation of glucokinase in islet cells and dyslipidemia caused by over-activation of intrahepatic glucokinase. In the effort to mitigate risks of hypoglycemia and dyslipidemia while maintaining the promising efficacy of glucokinase activator. tert-Butyl (S)-2-(3-(4-(azetidine-1-carbonyl)phenoxy)-5-((1-methoxypropan-2-yl)oxy)benzamido)-6,7-dihydrothiazolo[5,4-c]pyridine-5(4H)-carboxylate shows a good balance between in vitro potency and enzyme kinetic parameters, and protects beta-cells from streptozotocin-induced apoptosis. Chronic treatment of this compound demonstrates its potent activity in regulation of glucose homeostasis and low risk of dyslipidemia with diabetic db/db mice in oral glucose tolerance test. Acute treatment of this compound does not induce hypoglycemia in C57BL/6J mice even at 200 mg/kg via oral administration
drug target
the enzyme is a promising target for cancer therapy
drug target
the identification of structural and biochemical differences between HK2 and other human hexokinase isozymes could potentially be used in the development of new anticancer therapies
malfunction
-
defect in the activation of glucokinase is potential contributing factor to the dysregulation of hepatic glucose metabolism in type 2 diabetes
malfunction
-
defect in the activation of glucokinase is potential contributing factor to the dysregulation of hepatic glucose metabolism in type 2 diabetes
malfunction
-
defect in the activation of glucokinase is potential contributing factor to the dysregulation of hepatic glucose metabolism in type 2 diabetes
malfunction
-
heterozygous inactivating mutations in glucokinase cause maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
malfunction
-
heterozygous or homozygous loss of function in the glucokinase gene causes either mild diabetes (maturity onset diabetes of the young type 2 [MODY2]) or severe neo-natal onset diabetes, respectively
malfunction
-
knockdown of hexokinase II increases the apoptotic susceptibility of tuberous sclerosis complex 2-deficient cells to serum deprivation
malfunction
-
after silencing NtHXK1 using RNAi plants show stunted growth and leaf chlorosis
malfunction
an glucose-dependent root hair morphology is readily observed in Arabidopsis lines that overexpress HKL1 protein and in an HXK1-deficient line, gin2-1. Seedlings of these lines produce bulbous root hairs with an enlarged base after transfer from agar plates with normal medium to plates with 6% glucose. Seedling transfer to plates with 2% glucose plus 1-aminocyclopropane-1-carboxylic acid mimics the high-glucose effect in the HKL1 overexpression line but not in HXK1-deficient line gin2-1
malfunction
-
D-allose activates AtABI5 expression in transgenic gin2 (mutant glucose-insensitive2-1 (gin2), which has a null mutation in the glucose sensor gene of AtHXK1) over-expressing wild-type AtHXK1 but not in gin2 over-expressing the catalytic mutant AtHXK1S177A, indicating that the D-allose phosphorylation by HXK to D-allose 6-phosphate (A6P) is the first step for the up-regulation of AtABI5 gene expression as well as D-allose-induced growth inhibition
malfunction
-
D-allose inhibits Arabidopsis growth but fails to trigger growth retardation in the AtHXK1 loss-of function mutant (gin2 mutant)
malfunction
-
depletion of HK2 in GBM cells restores oxidative glucose metabolism and increases sensitivity to cell death inducers such as radiation and temozolomide. Intracranial xenografts of HK2-depleted GBM cells shows decreased proliferation and angiogenesis, but increased invasion, as well as diminished expression of hypoxia inducible factor 1alpha and vascular endothelial growth factor
malfunction
glucose-dependent developmental arrest of hkl1-1 mutants can not be rescued in the presence of 1-aminocyclopropane-1-carboxylic acid
malfunction
-
hypoxia-inducible factor (HIF)-1-regulated glycolytic enzyme hexokinase II (HKII) acts as a molecular switch that determines cellular fate by regulating both cytoprotection and induction of apoptosis based on the metabolic state. Together with phosphoprotein enriched in astrocytes (PEA15), HKII inhibits apoptosis after hypoxia. In contrast, HKII accelerates apoptosis in the absence of PEA15 and under glucose deprivation
malfunction
-
overexpression of NtHXK1 results in elevated glucose phosphorylation activity in leaf extracts or chloroplasts. NtHXK1 is able to complement the glucose-insensitive Arabidopsis mutant gin2-1 suggesting that NtHXK1 can take over glucose sensing functions
malfunction
A9RE08, A9RIW3, A9S3H4, A9S9F8, A9SJG4, A9SV13, A9TDS4, A9TLJ2, A9U0F4, A9U189, Q6X271 PpHXK3 is able to complement a hexokinase-deficient yeast strain
malfunction
A9RE08, A9RIW3, A9S3H4, A9S9F8, A9SJG4, A9SV13, A9TDS4, A9TLJ2, A9U0F4, A9U189, Q6X271 PpHXK3 is not able to complement a hexokinase-deficient yeast strain
malfunction
-
the repressive effects of glucose and chloramphenicol on LHCB expression are inhibited in plastid hexokinase (phxk) mutants
malfunction
-
transgenic Solanum tuberosum roots are altered in their hexokinase activity by transformation with an hexokinase cDNA in sense or antisense orientation. Altering root hexokinase activity levels impacts on growth rate and hexokinase has a high flux control coefficient over glucose phosphorylation but does not control glycolytic flux or respiration rate. It is concluded that futile cycling of hexose-phosphate can be partially responsible for the differences in energetic status in roots with high and low hexokinase activity and possibly cause the observed alterations in growth in transgenic roots
malfunction
DELTAFgHXK1 leads to inhibited vegetative growth and conidiation. DELTAFgHXK1 mutants lose virulence on wheat head and corn stigma. They show no change in sexual reproduction
malfunction
-
in contrast to wild-type, glucose-treated hxk1 mutants do not shut off photosynthesis or accumulate astaxanthin, triacylglycerols, or cytoplasmic lipid droplets
malfunction
knockdown of hexokinase 2 or pharmacological inhibition of hexokinase 2 activity with Lonidamine decreased TGF-beta-stimulated fibrogenic processes, including profibrotic gene expression, cell migration, colony formation, and activation of the transcription factors YAP and TAZ, with no apparent effect on cellular viability
malfunction
-
DELTAFgHXK1 leads to inhibited vegetative growth and conidiation. DELTAFgHXK1 mutants lose virulence on wheat head and corn stigma. They show no change in sexual reproduction
-
metabolism
-
HKI exclusively promotes glycolysis
metabolism
-
HKII promotes glycolysis when bound to mitochondria. Promotes glycogen synthesis when located in the cytosol
metabolism
-
after proteasome inhibition glucokinase activity is significantly reduced in MIN6 cells, whereas the protein content is increased. Enhancing the availability of chaperones by cyclohexamide can induce refolding and restores glucokinase activity. Glucokinase aggregation due to proteasome blocking with MG132, bortezomib, epoxomicin or lactacystin can be detected in MIN6 cells, primary beta-cells and hepatocytes. Glucokinase aggresome formation proceeds microtubule-assisted and is avoided by cyclohexamide
metabolism
-
glucokinase contributes to the reprogramming of energy metabolism in cancer cells. Activating glucokinase variations substantially increase affinity of the enzyme to glucose, disrupt the otherwise characteristic sigmoidal response to glucose and/or prolong the enzyme half-life. This, combined, facilitates glucose phosphorylation, thus supporting glycolysis and associated pathways
metabolism
hexokinase 2 connects telomerase to autophagy. Hexokinase 2 inhibition in HepG2 cells suppress TERT induced autophagy activation and further enhancement by glucose deprivation. TERT promotes autophagy through an HK2-mTOR pathway. TERC plays a role similar to that of TERT, and simultaneous expression of TERT and TERC synergistically enhances HK2 expression and autophagy
metabolism
hexokinase 2 couples glycolysis with the profibrotic actions of TGF-beta
metabolism
-
hexokinase 2 serves as a hinge that connects the Src/AKT pathway with glycolysis and anoikis
metabolism
hexokinase II serves as a hinge that connects the Src/AKT pathway with glycolysis and anoikis
metabolism
hexokinase III overexpression in O/N starved cells increases cell survival following H2O2 application and increases ATP levels both before and after challenge with 0.5 mM H2O2. The overexpression of hexokinase III in H2O2-treated cells also decreases the mitochondrial superoxide levels
metabolism
hexokinase is a rate-limiting enzyme in deoxynivalenol biosynthesis and plays a critical role in fungal development
metabolism
hexokinase is a rate-limiting enzyme in deoxynivalenol biosynthesis and plays a critical role in fungal development. FgHXK1 is involved in conidiation and germination
metabolism
-
hexokinase is functionally coupled to mitochondrial respiration
metabolism
key glycolytic enzyme. The enzyme is a key factor that increases the anaerobic rate, and is probably involved in the HIF-1 pathway related to highly active metabolism during hypoxia
metabolism
Plasmodium falciparum hexokinase activity is important for the NADPH-dependent reduction of oxidized glutathione in the parasite by providing glucose-6-phosphate, which allows glucose-6-phosphate dehydrogenase to generate NADPH for downstream redox reactions
metabolism
rate-limiting enzyme in the first step of glycolysis pathway
metabolism
the enzyme (HXK1) regulates cell proliferation and expansion early during leaf development. HXK1 is involved in sucrose-induced leaf growth stimulation, independent of GPT2 (GLUCOSE-6-PHOSPHATE/PHOSPHATE TRANSPORTER2) induction or repression of chloroplast differentiation. KINgamma is a HXK1-interacting protein
metabolism
the enzyme is required for profibrotic TGF-beta signaling and YAP/TAZ activation
metabolism
-
the green alga Chromochloris zofingiensis reversibly switches off photosynthesis in the presence of glucose in the light and augments production of biofuel precursors (triacylglycerols) and the high-value antioxidant astaxanthin. This photosynthetic and metabolic switch is mediated by the glycolytic enzyme hexokinase. The enzyme is critical for the regulation of genes related to photosynthesis, ketocarotenoid synthesis and fatty acid biosynthesis. The enzyme is essential for the accumulation of cytoplasmic lipid droplets near the plasma membrane
metabolism
the high proliferation rate of tumor cells demands high energy and metabolites that are sustained by a high glycolytic flux known as the Warburg effect. The activation and further metabolism of glucose is initiated by hexokinase, a focal point of metabolic regulation
metabolism
-
hexokinase is a rate-limiting enzyme in deoxynivalenol biosynthesis and plays a critical role in fungal development. FgHXK1 is involved in conidiation and germination
-
physiological function
-
glucokinase acts as a hepatic glucose sensor that permits hepatic metabolism to respond appropriately to changes in plasma glucose concentrations
physiological function
-
glucokinase acts as a hepatic glucose sensor that permits hepatic metabolism to respond appropriately to changes in plasma glucose concentrations
physiological function
-
glucokinase acts as a hepatic glucose sensor that permits hepatic metabolism to respond appropriately to changes in plasma glucose concentrations
physiological function
-
glucokinase is a key regulatory enzyme in the pancreatic beta-cell, it plays a crucial role in the regulation of insulin secretion and has been termed the glucose sensor in pancreatic beta-cells
physiological function
-
glucokinase regulates glucose storage and disposal in the liver, altered glucokinase regulation in liver enhances glycolytic flux, promoting hepatic glucose metabolism and elevating concentrations of malonyl-CoA, a substrate for de novo lipogenesis
physiological function
-
overexpressed glucokinase due to its structural similarity with Mlc, the repressor of malT, binds to the glucose transporter (PtsG), releasing Mlc and thus increasing malT repression
physiological function
-
part of pentose phosphate pathway
physiological function
-
pHXK is a node of convergence for sugar-mediated and plastid gene expression (PGE)-derived signals in Arabidopsis thaliana
physiological function
-
both genes hxk1 and hxk2 are able to complement a hexokinase-deficient yeast triple mutant (hxk1, hxk2, glk1)
physiological function
Branchiostoma japonicum hexokinase is the archetype of vertebrate hexokinases IV, i.e. glucokinases. Recombinant enzyme shows functional enzyme activity resembling vertebrate hexokinases I, II, III and IV. Glucokinase activity in the hepatic caecum is markedly reduced by fasting,whereas it is considerably increased by feeding. The enzyme represents the archetype of glucokinases, from which vertebrate hexokinase gene family has evolved by gene duplication, and the hepatic caecum plays a role in the control of glucose homeostasis in amphioxus
physiological function
-
dephosphorylation and activation of hepatopancreas hexokinase during anoxia may allow for increased shunting of glucose-6-phosphate into the pentose phosphate pathway, thereby producing reducing equivalents of NADPH. The activation of endogenous protein kinase C and AMP-activated protein kinase increase the Km for glucose for anoxic hepatopancreas hexokinase to a value that is similar to the control Km for glucose. Stimulation of endogenous protein kinase C, protein kinase G, and Calcium/calmodulin activated protein kinase for foot muscle hexokinase increase the Km for ATP to a value similar to that seen for the anoxic enzyme form. In both tissues, activation of endogenous phosphatases reverses the effects of protein kinases
physiological function
downregulation of activity reduces cell viability and delays pupaldevelopment by reducing metabolic activity and increasing reactive oxygen species activity. The transcription factors CREB, c-Myc, and POU are specifically binding the hexokinase gene promoter and regulating its activity. POU and c-Myc are specific transcription factors for hexokinase expression, whereas CREB is nonspecific. Low ecdysone levels in diapause-destined individuals lead to low POU and c-Myc expression levels, ultimately repressing hexokinase expression and inducing entry into diapause or lifespan extension
physiological function
-
entrance of ground squirrels into hibernation from their active state is accompanied by a sharp decrease in blood glucose level (from 14 to 2.9 mM) and with a 7fold decrease of glucokinase activity in the liver cytoplasm. The dependence of glucokinase activity upon glucose concentration for the enzyme from active ground squirrel liver shows a pronounced sigmoid character (Hill coefficient, h = 1.70 and S0.5 = 6.23 mM). On decreasing the temperature to 2°C (simulation of hibernation conditions), this dependency becomes almost hyperbolic (h = 1.16) and glucokinase affinity for substrate is reduced (S0.5 = 23 mM). These parameters for hibernating ground squirrels (body temperature 5°C) at 25°C are practically equal to the corresponding values obtained for glucokinase from the liver of active animals
physiological function
enzyme is able to complement a yeast mutant lacking the ability to phosphorylate glucose and fructose
physiological function
-
hexokinase from the muscle of dehydrated frogs shows a 3.4 fold higher Vmax and 2.4fold higher Km for glucose compared with control, while the Km for ATP is unaltered. Hexokinase from dehydrated frogs also shows greater phosphoserine content (20% increase) and lower phosphothreonine (22% decrease) content compared to control. Control hexokinase has a higher melting temperature than from dehydrated frogs
physiological function
hexokinase-7 enhances the glucose-dependent repression of rice alpha-amylase gene RAmy3D in the mesophyll protoplasts of maize, but its catalytically inactive mutant alleles do not. The expression of hexokinase-7, but not its catalytically inactive alleles, complements the Arabidopsis thaliana glucose insensitive gin2-1 mutant, thereby resulting in wild type characteristics of glucose-dependent repression, seedling development, and plant growth. Hexokinase-7-mediated glucose-dependent repression is abolished in the O2-deficient mesophyll protoplasts of maize. Hexokinase-7 functions in sugar signaling via a glycolysis-dependent manner under normal conditions, but its signaling role is suppressed when O2 is deficient. The germination of two hexokinase-7 null OsHXK7 mutants is affected by O2 deficiency, but overexpression enhances germination in rice
physiological function
-
in animals with normal levels of glucokinase, glucokinase regulatory protein is mainly localized to the nuclei of hepatocytes. In liver-specific glucokinase gene knockout mice (animals that lack or have reduced levels of glucokinase protein), glucokinase regulatory protein is found primarily in the cytoplasm. Varying the level of glucokinase protein has no effect on total cellular glucokinase regulatory protein protein levels
physiological function
-
in animals with normal levels of glucokinase, glucokinase regulatory protein is mainly localized to the nuclei of hepatocytes. In seven-day old rats, glucokinase regulatory protein is found primarily in the cytoplasm. Varying the level of glucokinase protein has no effect on total cellular glucokinase regulatory protein protein levels
physiological function
in fasted rats, glucokinase activity is specifically increased in the arcuate nucleus but not other regions of the hypothalamus. Pharmacologic and genetic activation of glucokinase in the arcuate nucleus of rodent models increases glucose ingestion, while decreased arcuate nucleus glucokinase activity reduces glucose intake. ATP-sensitive potassium channel and P/Q calcium channel activity are required for glucokinase-mediated glucose intake. Altered glucokinase activity affects release of the orexigenic neurotransmitter neuropeptide Y in response to glucose
physiological function
-
in frog oocytes, glycogen synthesis through the direct pathway is under the control of hexokinase. Phosphoglucomutase and UDPG-pyrophosphorylase have a modest influence, while the control exerted by glycogen synthase is null. Compared with phosphoglucomutase, UDPG-pyrophosphorylase and glycogen synthase, hexokinase has the lowest activity (0.06 mU/oocyte)
physiological function
increased expression of Arabidopsis hexokinase-1 decreases the expression of photosynthetic genes and the rate of transpiration and inhibits growth. Hexokinase-1 also decreases root and stem hydraulic conductivity and leaf mesophyll CO? conductance. Expression of Nicotiana tabacum aquaporin AQP1 significantly improves growth and increases the transpiration rates of hexokinase-expressing plants. This complementation occurs when both genes are expressed simultaneously in the shoot. Yet, AQP1 has only a marginal effect on the hydraulic conductivity of the double-transgenic plants
physiological function
-
inhibiting Ca2+ release from the endoplasmic reticulum decouples glucokinase activation from receptor stimulation. Pharmacological release of endoplasmic reticulum Ca2+ stimulates activation of a glucokinase optical biosensor and potentiates glucose metabolism. An optimized glucokinase biosensor using circularly permuted mCerulean3 proteins sensitively reports activation in response to insulin, glucagon-like peptide 1, and agents that raise cAMP levels. Transient, glucose-stimulated glucokinase activation is observed in TC3 and MIN6 cells. Half-maximal activation of the FRET-glucokinase sensor is estimated to occur at400 nM Ca2+. When expressed in islets, fluctuations in glucokinase activation are observed in response to glucose, and posttranslational activation of GCK enhances glucose metabolism by about 35%
physiological function
inhibition of hexokinase-II diminishes, while overexpression of hexokinase-II potentiates autophagy induced by glucose deprivation in cardiomyocyte and noncardiomyocyte cells. Hexokinase-II binds to and inhibits the autophagy suppressor, mTOR complex 1 (TORC1), and this binding is increased by glucose deprivation. Mutating the TOS motif, a scaffold sequence responsible for binding TORC1 substrates, in hexokinase-II blocks its ability to bind to TORC1 and regulate protective autophagy. The transition from glycolysis to autophagy appears to be regulated by a decrease in glucose-6 phosphate
physiological function
-
liver-specific glucokinase knockout mice exhibit impaired glucose tolerance, decreased hepatic glycogen content, and reduced Pklr and Fas gene expression in the liver. The liver-specific knockout mice display neither altered expression of thermogenesis-related genes in brown adipose tissue nor impaired insulin secretion by beta-cells under a normal chow diet
physiological function
Overexpression of the HXK1 gene leads to increased hexokinase activity (6.5-12 times higher), a pronounced reduction in cell filamentation in overexpressing strains grown in fructose-based media, and improved biomass production. All overexpressing strains show improved lipid yield and production when grown on fructose, although th eeffect is strain-dependent (23-55% improvement)
physiological function
-
phosphorylation of hexoses by hexokinase is an essential component in the glucose-dependent expression of cell wall invertase and sucrose synthase. Mannoheptulose, a specific inhibitor of hexokinase, blocks the repression induced by glucose cell wall invertase and sucrose synthase expression
physiological function
hexokinase 2 is overexpressed in all aggressive tumors and predominantly found on the outer mitochondrial membrane, where interactions through its N-terminus initiates and maintains tumorigenesis
physiological function
hexokinase III plays a role in hypoxia
physiological function
the antioxidant function of hexokinase II is independent of its enzymatic activity
physiological function
the enzyme is important during pregnancy in the regulation of glucose homeostasis
physiological function
-
both genes hxk1 and hxk2 are able to complement a hexokinase-deficient yeast triple mutant (hxk1, hxk2, glk1)
-
additional information
in Zea mays, nine members of the hexokinase gene family are distributed on 3 of the 10 maize chromosomes
additional information
in Zea mays, nine members of the hexokinase gene family are distributed on 3 of the 10 maize chromosomes
additional information
-
in Zea mays, nine members of the hexokinase gene family are distributed on 3 of the 10 maize chromosomes
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S177A
-
D-allose activates AtABI5 expression in transgenic gin2 (mutant glucose-insensitive2-1 (gin2), which has a null mutation in the glucose sensor gene of AtHXK1) over-expressing wild-type AtHXK1 but not in gin2 over-expressing the catalytic mutant AtHXK1S177A, indicating that the D-allose phosphorylation by HXK to D-allose 6-phosphate (A6P) is the first step for the up-regulation of AtABI5 gene expression as well as D-allose-induced growth inhibition
D217H
about 7% of wild-type activity
N216K
about 2% of wild-type activity
S159P
complete loss of activity
A188E
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased kcat, decreased Km for ATP
A188W
-
kinetic mutation effects are increased S0.5, decreased kcat, decreased Km for ATP
A208G
-
mutant displays a slightly higher glucose affinity and similar ATP affinity to the wild type enzyme. The activity of the enzyme at 5 mM glucose is moderately higher than the wild type activity
A208W
-
kinetic mutation effects are increased S0.5, decreased kcat, decreased Hill number, increased Km for ATP
A378V
-
kinetic mutation effects are increased S0.5, increased Km for ATP
A379S
-
mutation isolated in a type 2 diabetes patient
A379T
kcat(1/sec): 61.2, D-glucose S05 (mM): 12.3, Km (ATP): 0.87 mM, relative inhibition of glucokinase activity through GKRP alone: 17% and GKRP plus 10 microM sorbitol 6-phosphate: 53%
A379V
mutations is associated with mature-onset diabetes of the young, type 2 (MODY2). Vmax is 65% of maximal activity, Km-value for ATP is 1.5fold higher than wild-type enzyme
A460R
-
mutation increases the affinity of the enzyme for glucose
A464P/E465G
-
mutant with a helix breaker embedded in the interdomain alpha-helix has a smaller magnitude of phosphate alleviation than the wild type
A53S
-
the mutant shows wild type kinetics, is thermolabile
A8L
-
mutant maintains binding to mitochondrial-like membrane structures
C220Y
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
C457V
-
the mutant enzyme shows a slightly higher glucose level than the wild type and a slightly lower affinity for ATP. The activity of the enzymes at 5 mM glucose is higher than the wild type activity
C5A
mutation abrogates palmitoylation of protein
C5S
mutation abrogates palmitoylation of protein
D158A
-
naturally occurring mutation, activity and kinetics are similar to the wild-type enzyme
D209A
glucose binding enhances the stability of the wild-type enzyme and the single mutant D657A of the C-domain, but it does not increase the stability of the D209A mutant of the N-domain
D400Y
-
mutation isolated in a type 2 diabetes patient
D657A
glucose binding enhances the stability of the wild-type enzyme and the single mutant D657A of the C-domain, but it does not increase the stability of the D209A mutant of the N-domain
D78A/D158A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E256A
the mutation in the L-domain results in enzyme form that does not bind alpha-D-glucose at 200 mM and is essentially catalytically inactive (2.6% relative activity compared to the wild type enzyme)
E256K
the mutation in the L-domain results in enzyme form that does not bind alpha-D-glucose at 200 mM and is essentially catalytically inactive
E279Q
-
kinetic mutation effects are increased S0.5, decreased kcat
E280A
hexokinase I mutation eliminates hydrogen bonds between monomers of crystallographic dimers, triple mutant E280A/R283A/G284Y: nonaggregating mutant of recombinant hexokinase I, engineered by directed mutation to block dimerization, exhibits wild-type activity
E290A
the mutant 45.9% relative activity compared to the wild type enzyme
E300A
-
mutation isolated in a type 2 diabetes patient
E300K
-
mutant shows kinetics same as wild type and decreased thermostability
E300Q
-
kinetic mutation effect is increased S0.5
E339G
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
E339K
crystal structure of E339K glucokinase in complex with glucose is shown. This mutation results in a conformational change of His416, spatially interfering with adenosine-triphosphate (ATP) binding
E356K
-
kinetic mutation effects are decreased S0.5, decreased kcat
E395A
-
mutation isolated in a type 2 diabetes patient
E395G
-
mutation isolated in a type 2 diabetes patient
E397L
-
kinetic mutation effect is decreased thermostability
E442K
kcat(1/sec): 52.6, D-glucose S05 (mM): 5.24, Km (ATP): 1.5 mM, relative inhibition of glucokinase activity through GKRP alone: 14% and GKRP plus 10 microM sorbitol 6-phosphate: 40%
E70K
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased kcat
F419L
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
G175E
-
kinetic mutation effects are increased S0.5, decreased kcat
G175R
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased kcat
G227A/D158A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
G261R
-
kinetic mutation effects are increased S0.5, increased Hill number, increased Km for ATP, decreased kcat
G264S
-
mutant shows near normal kinetics, mild elevation of S0.5, slight decrease in Hill number, slightly decreased thermostability
G284Y
hexokinase I mutation introduces steric hindrance, triple mutant E280A/R283A/G284Y: nonaggregating mutant of recombinant hexokinase I, engineered by directed mutation to block dimerization, exhibits wild-type activity
G299R
-
kinetic mutation effects are decreased S0.5, decreased Km for ATP, decreased kcat
G2A
mutant protein lacks myristoylation
G2A/C5S
mutation abrogates both myristoylation and palmitoylation of protein
G44S
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased Km for ATP, decreased kcat
G68K
kcat(1/sec): 43.2, D-glucose S05 (mM): 2.34, Km (ATP): 0.39 mM, relative inhibition of glucokinase activity through GKRP alone: 2% and GKRP plus 10 microM sorbitol 6-phosphate: 20.5%
G80A
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased kcat
H137R
-
mutant shows wild type kinetics
H380N
-
mutation isolated in a type 2 diabetes patient
H5P
-
mutation abolishes binding to mitochondrial-like membrane structures, and a greater than 4fold decrease in H5P protein levels as compared with wild-type protein levels is found in the cytoplasmic fraction
I348N
-
mutation isolated in a type 2 diabetes patient
I366F
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
K102A/D158A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
K140E
kcat(1/sec): 40, D-glucose S05 (mM): 10.8, Km (ATP): 0.35 mM, relative inhibition of glucokinase activity through GKRP alone: 9% and GKRP plus 10 microM sorbitol 6-phosphate: 10.5%
K169A
inactive, Lys169 enhances the binding of glucokinase with both ATP and glucose by serving as a bridge between ATP and glucose, Lys169 directly participates in the glucose phosphorylation as a general acid catalyst
K458R
-
mutation results in an enzyme with lower glucose affinity and lower ATP affinity than the wild type enzyme. Activity of the K458R mutant at 5 mM glucose is lower than the wild type activity
K459L
-
the mutant enzyme shows a slightly higher glucose than the wild type and a slightly lower affinity for ATP. The activity of the enzymes at 5 mM glucose is higher than the wild type activity
K90A/D158A
-
site-directed mutagenesis, 2fold increased activity compared to the wild-type enzyme
L165F
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat, decreased thermostability
L301M
-
mutation isolated in a type 2 diabetes patient
L309P
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
M197E
kcat(1/sec): 17.7, D-glucose S05 (mM): 41.6, Km (ATP): 0.4 mM, relative inhibition of glucokinase activity through GKRP alone: 13.5% and GKRP plus 10 microM sorbitol 6-phosphate: 18.5%
M197I/A397T
kcat(1/sec): 50.2, D-glucose S05 (mM): 5.81, Km (ATP): 2.71 mM, relative inhibition of glucokinase activity through GKRP alone: 18% and GKRP plus 10 microM sorbitol 6-phosphate: 37%
M197L
kcat(1/sec): 62.6, D-glucose S05 (mM): 4.03, Km (ATP): 1.31 mM, relative inhibition of glucokinase activity through GKRP alone: 15% and GKRP plus 10 microM sorbitol 6-phosphate: 37%
M210K
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
M210W
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased kcat
M224R
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
M235V
-
kinetic mutation effects are thermostability, decreased kcat
M235W
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased Km for ATP, decreased kcat
M298I
-
mutation isolated in a type 2 diabetes patient
M381G
-
mutation isolated in a type 2 diabetes patient
M402R
-
mutation isolated in a type 2 diabetes patient
N166R
-
increased affinity for glucose and ATP by a factor of 3
N166R-S151-A
-
lowers the KM-value for glucose by a factor of 40 and increases the KM-value for ATP
N204A
the mutation in the L-domain results in enzyme form that does not bind alpha-D-glucose at 200 mM and is essentially catalytically inactive (8.9% relative activity compared to the wild type enzyme)
N231A
the mutant shows 0.03% relative activity compared to the wild type enzyme
P417R
kcat(1/sec): 48.3, D-glucose S05 (mM): 6.59, Km (ATP): 2.08 mM, relative inhibition of glucokinase activity through GKRP alone: 10% and GKRP plus 10 microM sorbitol 6-phosphate: 39%
Q287V
the mutant 57.9% relative activity compared to the wild type enzyme
Q466_H467insHMNLAEQ
-
mutant has a smaller magnitude of phosphate alleviation than the wild type
R275C
-
mutant shows near wild type kinetics
R283A
hexokinase I mutation eliminates hydrogen bonds between monomers of crystallographic dimers, triple mutant E280A/R283A/G284Y: nonaggregating mutant of recombinant hexokinase I, engineered by directed mutation to block dimerization, exhibits wild-type activity
R308K
-
mutation isolated in a type 2 diabetes patient
R308W
-
kinetic mutation effects are increased S0.5, decreased kcat, decreased thermostability
R345X
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
R36W
-
kinetic mutation effects are edecreased S0.5, decreased Km for ATP, decreased kcat
R377C
-
kinetic mutation effects are increased S0.5, decreased kcat
R394P
-
mutation isolated in a type 2 diabetes patient
R397S
-
mutation isolated in a type 2 diabetes patient
S127P
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
S131P
-
kinetic mutation effects are increased S0.5, increased Km for ATP, decreased kcat
S151A
-
lowers the KM-value for glucose by a factor of 26, increases the KM-value for ATP and decreases the KM-value for mannose and fructose
S151C
-
lowers the KM-value for glucose by a factor of 2, increases the KM-value for ATP and decreases the KM-value for mannose and fructose
S151G
-
lowers the KM-value for glucose by a factor of 40, increases the KM-value for ATP and decreases the KM-value for mannose and fructose
S383L
-
kinetic mutation effects are increased S0.5, increased Km for ATP, decreased Hill number, decreased kcat
S398R
-
mutation isolated in a type 2 diabetes patient
S411A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
S411F
-
kinetic mutation effects are decreased S0.5, increased Km for ATP, decreased Hill number, decreased kcat
S411L
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
S453L
-
kinetic mutation effects are increased S0.5, increased Km for ATP, decreased Hill number, decreased kcat
S4L
-
mutant maintains binding to mitochondrial-like membrane structures, a greater than 6fold increase in S4L mutant protein is found in the mitochondrial fraction
S64P
kcat(1/sec): 83.3, D-glucose S05 (mM): 2.07, Km (ATP): 0.32 mM, relative inhibition of glucokinase activity through GKRP alone: 5% and GKRP plus 10 microM sorbitol 6-phosphate: 4%
S64R/E67D/S69T
3fold increase in activity, no change in cooperativity
T168G
the mutant shows 9.4% relative activity compared to the wild type enzyme
T206M
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
T228A/D158A
-
site-directed mutagenesis, very highly reduced activity compared to the wild-type enzyme
T228M
-
mutant shows a 9000fold reduced activity
T82A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
V182M
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased kcat, decreased Km for ATP
V203A
-
kinetic mutation effects are increased S0.5, decreased kcat, increased Km for ATP
V226M
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
V367M
-
the mutant shows wild type kinetics
V389L
kcat(1/sec): 67.1, D-glucose S05 (mM): 3.45, Km (ATP): 0.76 mM, relative inhibition of glucokinase activity through GKRP alone: 67% and GKRP plus 10 microM sorbitol 6-phosphate: 75%
V452L
kcat(1/sec): 122, D-glucose S05 (mM): 2.27, Km (ATP): 0.53 mM, relative inhibition of glucokinase activity through GKRP alone: 19% and GKRP plus 10 microM sorbitol 6-phosphate: 38%
V455E
-
kinetic mutation effects are increased S0.5, decreased kcat
V62E
-
kcat for ATP is 8% of wild-type value
V62F
-
no inhibition by glucokinase regulatory protein. kcat for ATP is 54% of wild-type value
V62K
-
no inhibition by glucokinase regulatory protein. kcat for ATP is 10% of wild-type value
V62L
-
no inhibition by glucokinase regulatory protein. kcat for ATP is 96% of wild-type value
V62Q
-
no inhibition by glucokinase regulatory protein. kcat for ATP is 24% of wild-type value
V62T
-
kcat for ATP is 41% of wild-type value
V91L
kcat(1/sec): 60.6, D-glucose S05 (mM): 1.66, Km (ATP): 0.48 mM, relative inhibition of glucokinase activity through GKRP alone: 6% and GKRP plus 10 microM sorbitol 6-phosphate: 22.5%
W167F
the mutant exhibits 24fold reduction in catalytic efficiency
W167F/W257F
-
W99 kcat values are markedly lowered compared to wild-type, Km (ATP) increased compared to wild-type, kcat only moderately increased in the presence of glucokinase activator drug
W168A
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP
W168P
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
W206M
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased kcat
W209M
-
kinetic mutation effects are decreased S0.5, increased Km for ATP, decreased kcat
W228A
-
kinetic mutation effects are decreased S0.5, decreased Hill number
W257F
the mutant exhibits slightly reduced affinity for D-glucose
W257R
-
kinetic mutation effects are decreased S0.5, decreased kcat
W65I
-
kinetic mutation effects are decreased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
W99F
the mutant shows a small increase in both affinity and catalytic efficiency
W99L
-
kinetic mutation effects are decreased S0.5, increased kcat
W99R/W167F
-
W257 kcat values are markedly lowered compared to wild-type, Km (ATP) increased compared to wild-type
W99R/W257F
-
W167 kcat values onlye weakly lowered compared to wild-type, Km (ATP) weakly increased compared to wild-type, kcat increased in the presence of glucokinase activator drug
Y108C
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased Km for ATP, decreased kcat
Y214A
kcat(1/sec): 117, D-glucose S05 (mM): 1.41, Km (ATP): 0.92 mM, relative inhibition of glucokinase activity through GKRP alone: 24% and GKRP plus 10 microM sorbitol 6-phosphate: 53%
Y214A/V452A
kcat(1/sec): 23.1, D-glucose S05 (mM): 0.55, Km (ATP): 1.42 mM, relative inhibition of glucokinase activity through GKRP alone: 11.5% and GKRP plus 10 microM sorbitol 6-phosphate: 20%
Y273X
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
A456V
-
mutant enzyme is as stable as the wild-type enzyme. Ability of glucokinase regulatory protein to inhibit mutant enzyme A456V is less than that of the wild type enzyme. Mutant shows 37.9% of the wild-type activity. KM-value for ATP is 1.3fold lower than wild-type value. Glucokinase A456V/A456V mice are viable and have similar plasma triglycerides, free fatty acid levels, and similar or slightly lower body weight when compared with control mice
K414E
-
mutant enzyme is thermolabile. Mutant shows 0.32% of the wild-type activity. KM-value for ATP is 4.4fold higher than wild-type value. Glucokinase K414E/K414E mice die within a few days after birth of severe hyperglycemia
S177A
-
D-allose activates AtABI5 expression in transgenic gin2 (mutant glucose-insensitive2-1 (gin2), which has a null mutation in the glucose sensor gene of AtHXK1) over-expressing wild-type AtHXK1 but not in gin2 over-expressing the catalytic mutant AtHXK1S177A, indicating that the D-allose phosphorylation by HXK to D-allose 6-phosphate (A6P) is the first step for the up-regulation of AtABI5 gene expression as well as D-allose-induced growth inhibition
G76D
catalytic activity of the mutant enzyme is abolished
S148A
catalytic activity of the mutant enzyme is reduced by 20% as compared to wild-type enzyme
W256A
the catalytic activity of the mutant enzyme is not affected
D84E
HK I mutant, slightly increased Ki value for the inhibitory 1,5-anhydro-D-glucitol 6-phosphate, antagonistic effect of phosphate is drastically reduced, no effect on the inhibition by phosphate at higher concentrations
D84K
HK I mutant, increased Ki value for the inhibitory 1,5-anhydro-D-glucitol 6-phosphate, antagonistic effect of phosphate is abolished, slightly decreased Ki value for inhibition by phosphate at higher concentrations
F199A
mutation in mTOR signaling motif. While overexpressed wild-type enzyme associates with mTOR and raptor, mutant F199A does not show association above control levels
L309R/N313Y
-
significantly reduced interaction with glucokinase regulatory protein
L355R/N350Y
-
mutant has a fivefold-higher binding affinity for glucokinase regulatory protein than wild-type glucokinase
L58R
-
7fold reduced interaction with glucokinase regulatory protein
L58R/N204Y
-
10fold reduced interaction with glucokinase regulatory protein. Mutant lacks glucose-dependent translocation by glucokinase regulatory protein
N204Y
-
12fold reduced interaction with glucokinase regulatory protein
F159Y
mutant isolated in a sreen for variants with increased resistance to autophosphorylation by xylose. The mutant has 64% higher catalytic activity in the presence of xylose compared to the wild-type and is expected to be a key component for increasing the productivity of recombinant xylose-fermenting strains for bioethanol production from lignocellulosic feedstocks
N469D
inactive mutant protein, TbHK1
A456V
-
mutation leads to increased enzyme activity, associated with hyperinsulinism and hypoglycemia
A456V
-
activating glucokinase mutation
A456V
-
inactivating mutation in glucokinase causing hyperinsulinemic hypoglycemia subtype glucokinase
A456V
-
kinetic mutation effects are decreased S0.5, thermostable, decreased Km for ATP, decreased Hill number, increased kcat
A456V
kcat(1/sec): 65.6, D-glucose S05 (mM): 1.91, Km (ATP): 0.35 mM, relative inhibition of glucokinase activity through GKRP alone: 11% and GKRP plus 10 microM sorbitol 6-phosphate: 28%
C213R
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
C213R
kcat(1/sec): 50, D-glucose S05 (mM): 21.6, Km (ATP): 0.89 mM, relative inhibition of glucokinase activity through GKRP alone: 19% and GKRP plus 10 microM sorbitol 6-phosphate: 43%
C233R
mutations is associated with mature-onset diabetes of the young, type 2 (MODY2). Mutation affects a critical residue of the active center of the enzyme and rendered a protein with undetectable enzymatic activity
C233R
-
mutant shows wild type kinetics
C252Y
-
kinetic mutation effects are increased S0.5, increased Hill number, increased Km for ATP
C252Y
kcat(1/sec): 29.3, D-glucose S05 (mM): 31.6, Km (ATP): 0.75 mM, relative inhibition of glucokinase activity through GKRP alone: 4% and GKRP plus 10 microM sorbitol 6-phosphate: 4%
D205A
-
mutant shows almost no activity
D205A
the mutation in the L-domain results in enzyme form that does not bind alpha-D-glucose at 200 mM and is essentially catalytically inactive
E265K
mutations is associated with mature-onset diabetes of the young, type 2 (MODY2). Vmax is 86% of maximal activity, Km-value for ATP is 1.13fold lower than wild-type enzyme
E265K
-
kinetic mutation effects are increased S0.5, decreased thermostability, increased Km for ATP
G68V
-
kinetic mutation effects are decreased S0.5, decreased Hill number, decreased Km for ATP, increased kcat
G68V
kcat(1/sec): 62.7, D-glucose S05 (mM): 2.2, Km (ATP): 0.31 mM, relative inhibition of glucokinase activity through GKRP alone: 15% and GKRP plus 10 microM sorbitol 6-phosphate: 32.5%
G72R
-
kinetic mutation effects are decreased S0.5, decreased Hill number, increased Km for ATP, decreased kcat, slightly decreased thermostabiliy
G72R
mutant enzymes shows reduced rates of turnover (20% relative activity at 30°C, 10% relative activity at 37°C) and reduced glucose affinity relative to wild type, the mutant loses the stabilizing protein interactions with glucokinase regulatory protein, which may contribute to lower activity in vivo, the mutation associates with hyperglycemia in humans
G72R
kcat(1/sec): 29.8, D-glucose S05 (mM): 7.38, Km (ATP): 0.72 mM, relative inhibition of glucokinase activity through GKRP alone: 5% and GKRP plus 10 microM sorbitol 6-phosphate: 6.5%
K169N
naturally occurring mutation in the glucokinase gene associated with familial mild fasting hyperglycemia
K169N
the mutant shows 0.03% relative activity compared to the wild type enzyme
K414E
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
K414E
-
kinetic mutation effects are increased S0.5, increased Hill number, increased Km for ATP, decreased thermostability, decreased kcat. decreased S0.5
K414E
kcat(1/sec): 19.9, D-glucose S05 (mM): 5.69, Km (ATP): 1.53 mM, relative inhibition of glucokinase activity through GKRP alone: 13.5% and GKRP plus 10 microM sorbitol 6-phosphate: 49%
K420E
mutations is associated with mature-onset diabetes of the young, type 2 (MODY2). Vmax is 94% of maximal activity, Km-value for ATP is 1.1fold lower than wild-type enzyme
K420E
-
kinetic mutation effects are increased S0.5, increased Hill number
L146R
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased Km for ATP, decreased kcat
L146R
-
mutant shows a 100fold reduced kcat and a 40fold increase in [S]0.5 value for D-glucose. Km (ATP) is slightly increased compared to wild-type
M197I
-
kinetic mutation effects are decreased S0.5, decreased kcat, increased Km for ATP
M197I
kcat(1/sec): 58.1, D-glucose S05 (mM): 2.49, Km (ATP): 1.39 mM, relative inhibition of glucokinase activity through GKRP alone: 47% and GKRP plus 10 microM sorbitol 6-phosphate: 59%
M298K
-
kinetic mutation effects are increased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
M298K
kcat(1/sec): 37.7, D-glucose S05 (mM): 10.8, Km (ATP): 3.32 mM, relative inhibition of glucokinase activity through GKRP alone: 20% and GKRP plus 10 microM sorbitol 6-phosphate: 44%
S263P
-
kinetic mutation effects are Increased S0.5, decreased Hill number, decreased thermostability, increased Km for ATP
S263P
kcat(1/sec): 44.6, D-glucose S05 (mM): 9.7, Km (ATP): 0.63 mM, relative inhibition of glucokinase activity through GKRP alone: 19% and GKRP plus 10 microM sorbitol 6-phosphate: 49.5%
S336L
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S336L
-
kinetic mutation effects are decreased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
S336L
kcat(1/sec): 2.46, D-glucose S05 (mM): 4.75, Km (ATP): 12.6 mM
S64Y
-
mutation results in an increased affinity for the substrate glucose
S64Y
-
kinetic mutation effects are decreased S0.5, decreased Hill number, increased Km for ATP, decreased kcat
S64Y
kcat(1/sec): 114, D-glucose S05 (mM): 1.89, Km (ATP): 1.59 mM, relative inhibition of glucokinase activity through GKRP alone: 19% and GKRP plus 10 microM sorbitol 6-phosphate: 15%
T228A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
T228A
-
inactivating mutation in glucokinase causing maturity-onset diabetes of the young (MODY) subtype glucokinase, characterized by mild fasting hyperglycemia
T65I
-
mutant shows reduced activity (41%) compared to the wild type enzyme
T65I
kcat(1/sec): 22.6, D-glucose S05 (mM): 1.69, Km (ATP): 0.57 mM, relative inhibition of glucokinase activity through GKRP alone: 7.5% and GKRP plus 10 microM sorbitol 6-phosphate: 23%
V182L
mutations is associated with mature-onset diabetes of the young, type 2 (MODY2). Vmax is 38% of maximal activity, Km-value for ATP is 2.8fold lower than wild-type enzyme
V182L
-
kinetic mutation effects are increased S0.5, increased Hill number, decreased Km for ATP
V455M
-
mutation leads to increased enzyme activity, associated with hyperinsulinism and hypoglycemia
V455M
-
kinetic mutation effects are decreased S0.5, increased Km for ATP, decreased Hill number, decreased kcat
V455M
-
mutant shows increased activity (108%) compared to the wild type enzyme
V455M
kcat(1/sec): 61.8, D-glucose S05 (mM): 3.24, Km (ATP): 0.38 mM, relative inhibition of glucokinase activity through GKRP alone: 26% and GKRP plus 10 microM sorbitol 6-phosphate: 52%
V62A
-
kcat for ATP is 70% of wild-type value
V62A
-
kinetic mutation effects are increased S0.5, decreased Hill number, decreased Km for ATP, decreased kcat
V62M
-
mutation may cause hyperglycemia by a complex defect of GCK regulation involving instability in combination with loss of control by a putative endogenous activator and/or glucokinase regulatory protein. wild type enzyme is slightly activated after 30-min incubation as the temperature is raised from 30°C to 47.5°C. The activity of V62M GST-glucokinase increases similarly as that of the wild type enzyme but decreases abruptly at temperatures above 42.5°C. V62M GCK does not respond to RO0281675, nor does it respond to the hepatic glucokinase regulatory protein. kcat for ATP is 86% of wild-type value
V62M
-
kinetic mutation effects are increased S0.5, decreased thermostability, decreased Hill number, decreased kcat
V62M
mutant enzymes shows reduced rates of turnover (70% relative activity at 30°C, 40% relative activity at 37°C) and reduced glucose affinity relative to wild type, the mutant loses the stabilizing protein interactions with glucokinase regulatory protein, which may contribute to lower activity in vivo, the mutation associates with hyperglycemia in humans
V62M
kcat(1/sec): 47.2, D-glucose S05 (mM): 5.9, Km (ATP): 0.52 mM, relative inhibition of glucokinase activity through GKRP alone: 8.5% and GKRP plus 10 microM sorbitol 6-phosphate: 11.5%
W99R
-
kinetic mutation effects are decreased S0.5, decreased Hill number, increased Km for ATP, increased kcat
W99R
-
mutant shows slightly increased activity (219%) compared to the wild type enzyme
Y214C
-
the glucose binding affinity is increased while its cooperativity is decreased
Y214C
-
kinetic mutation effect is decreased S0.5, decreased Hill number, increased Km for ATP, increased kcat
Y214C
kcat(1/sec): 65.3, D-glucose S05 (mM): 1.35, Km (ATP): 1.08 mM, relative inhibition of glucokinase activity through GKRP alone: 19% and GKRP plus 10 microM sorbitol 6-phosphate: 41%
Y215A
-
mutation increases the affinity of the enzyme for glucose
Y215A
kcat(1/sec): 44.7, D-glucose S05 (mM): 2.07, Km (ATP): 0.58 mM, relative inhibition of glucokinase activity through GKRP alone: 6% and GKRP plus 10 microM sorbitol 6-phosphate: 4.5%
Y61S
mutations is associated with mature-onset diabetes of the young, type 2 (MODY2). Vmax is 16% of maximal activity, Km-value for ATP is 2.1fold lower than wild-type enzyme
Y61S
-
kinetic mutation effects are increased S0.5, decreased Km for ATP
D84A
-
HK I mutant with 2fold increased Ki value for the inhibitory 1,5-anhydro-D-glucitol 6-phosphate, mutation diminishes the ability of phosphate to antagonize inhibition, but has no effect on the inhibition by phosphate at higher concentrations
D84A
HK I mutant with 2fold increased Ki value for the inhibitory 1,5-anhydro-D-glucitol 6-phosphate, mutation diminishes the ability of phosphate to antagonize inhibition, but has no effect on the inhibition by phosphate at higher concentrations
additional information
-
HXK1 mutants with modified active sites
additional information
-
HXK1 mutants with modified active sites
-
additional information
construction of N-terminal deletion hepatic enzyme mutants lacking 11 or 15 amino acid residues, respectively
additional information
-
removal of helix alpha13 abolishes cooperativity and restores Michaelis-Menten kinetics, while reducing the kcat value of the wild type enzyme by 160fold, the impaired catalytic activity of the truncated enzyme is not rescued by the trans-addition of a synthetic alpha13 peptide
additional information
-
hexokinase-II binds to the voltage-dependent anion channel located on the mitochondrial outer membrane. When bound, hexokinase-II is blocking a major cell death pathway. A series of truncations and point mutations to the N-terminal end of hexokinase-II identify the binding site to the channel within the first 10 amino acids
additional information
sequential, single amino acid deletions from the C-terminus of connecting loop I cause systematic decreases in cooperativity. Deleting up to two loop residues leaves the kcat value unchanged, removing three or more residues reduces kcat by 1000fold. In contrast, the glucose K0.5 and KD values are unaffected by shortening the connecting loop by up to six residues. Substituting alanine or glycine for proline66 does not alter cooperativity. Replacing connecting loop I with the corresponding loop sequence from the catalytic domain of the noncooperative isozyme human hexokinase I eliminates cooperativity without impacting the kcat and glucose K0.5 values
additional information
-
sequential, single amino acid deletions from the C-terminus of connecting loop I cause systematic decreases in cooperativity. Deleting up to two loop residues leaves the kcat value unchanged, removing three or more residues reduces kcat by 1000fold. In contrast, the glucose K0.5 and KD values are unaffected by shortening the connecting loop by up to six residues. Substituting alanine or glycine for proline66 does not alter cooperativity. Replacing connecting loop I with the corresponding loop sequence from the catalytic domain of the noncooperative isozyme human hexokinase I eliminates cooperativity without impacting the kcat and glucose K0.5 values
additional information
construction of transgenic tobacco plants overexpressing isozyme hexokinase 2 via Agrobacterium tumefaciens infection system
additional information
-
construction of transgenic tobacco plants overexpressing isozyme hexokinase 2 via Agrobacterium tumefaciens infection system
additional information
-
hex1 mutants with decreased hexokinase activity, hex2 mutants with increased hexokinase activity
additional information
-
deletion mutant is unable to grow on fructose as the sole carbon source, but still grows on glucose, deletion mutants prevent glucose repression of invertase and maltase
additional information
replacing the last 18 amino acids of TbHK1 with the corresponding residues of TbHK2 yields an inactive recombinant protein
additional information
-
replacing the last 18 amino acids of TbHK1 with the corresponding residues of TbHK2 yields an inactive recombinant protein
additional information
replacing the last 18 amino acids of TbHK2 with the corresponding residues of TbHK1 yields an active recombinant protein with kinetic properties similar to those of TbHK1
additional information
-
replacing the last 18 amino acids of TbHK2 with the corresponding residues of TbHK1 yields an active recombinant protein with kinetic properties similar to those of TbHK1
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