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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
-