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Information on EC 2.7.1.2 - glucokinase
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2.7.1.2 glucokinaseIUBMB Comments
A group of enzymes found in invertebrates and microorganisms that are highly specific for glucose.
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Word Map
- 2.7.1.2
- insulin
- diabetes
- pancreatic
- islet
- hepatocytes
- hexokinase
- glycogen
- beta-cell
- mellitus
- hyperglycemia
- glucose-6-phosphatase
- phosphoenolpyruvate
- pancreas
-
carboxykinase
-
maturity-onset
- fructose
- glucagon
- 6-phosphate
-
phosphofructokinase
-
glucose-induced
-
gluconeogenesis
-
glucose-stimulated
-
non-insulin-dependent
-
glut-2
- insulinoma
-
antidiabetic
-
hypoglycemic
- pepck
- sulfonylurea
-
glucose-sensing
- g6pase
-
monogenic
-
gluconeogenic
- niddm
-
glucose-responsive
- substrate-2
- diazoxide
- fructokinase
-
ins-1e
- hyperinsulinism
-
2.7.1.1
-
glucose-lowering
-
insulin-producing
- glp-1
-
2,6-bisphosphate
-
glucose-dependent
- medicine
-
perivenous
-
kcnj11
-
insulin-secreting
- pharmacology
- c-peptide
The enzyme appears in viruses and cellular organisms
Synonyms
ATP-GLK, GCK, GK, GlcK, glk, Glk1, GlkB, glucokinase, glucokinase (phosphorylating), glucokinase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GCK
GK
glk
glucokinase
glucokinase (phosphorylating)
-
-
-
-
glucokinase 1
hexokinase IV
kinase, gluco- (phosphorylating)
-
-
-
-
NagC
TTE0090
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-glucose = ADP + D-glucose 6-phosphate
-
-
-
-
ATP + D-glucose = ADP + D-glucose 6-phosphate
ordered mechanism in which glucose binds first and glucose 6-phosphate dissociates last
-
ATP + D-glucose = ADP + D-glucose 6-phosphate
the enzyme activity requires 3 cysteine residues C175, C177, and C182 within the motif CXCGX(2)GCXE that discriminates microbial glucokinases into two lineages
ATP + D-glucose = ADP + D-glucose 6-phosphate
catalytic mechanism, substrate D-glucose interacts with Asn99, Asp100, Glu157, His160, and Glu187
ATP + D-glucose = ADP + D-glucose 6-phosphate
rapid equilibrium-ordered bi bi sequential mechanism, formation of a ternary complex of enzyme-D-glucose-MgATP2-
ATP + D-glucose = ADP + D-glucose 6-phosphate
rapid equilibrium-ordered bi bi sequential mechanism, formation of a ternary complex of enzyme-D-glucose-MgATP2-
-
ATP + D-glucose = ADP + D-glucose 6-phosphate
using intrinsic tryptophan fluorescence a conformational change induced by the binding of adenine nucleotides to human pancreatic glucokinase is determined. The molecular dynamic simulations indicate that the binding triggers molecular motion of the flexible surface /active site loop and partial closure of the interdomain active site cleft. The modelled structure of the hGK-ATP binary complex shows the residue contacts involved in ATP binding at the active site
-
ATP + D-glucose = ADP + D-glucose 6-phosphate
cutting-edge high-resolution nuclear magnetic resonance methods are used to explore the kinetic properties of glucokinase. Glucokinase samples a range of conformational states in the absence of glucose. In the presence of glucose or a small-molecule activator, the enzyme population shifts towards a more narrow, well-structured ensemble of states
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
1,3-propanediol biosynthesis (engineered), Bifidobacterium shunt, GDP-glucose biosynthesis, glucose and glucose-1-phosphate degradation, glycogen degradation I, glycogen degradation II, glycolysis III (from glucose), heterolactic fermentation, sucrose biosynthesis II, sucrose degradation III (sucrose invertase), trehalose degradation I (low osmolarity), trehalose degradation II (cytosolic), trehalose degradation IV, trehalose degradation V, UDP-N-acetyl-D-galactosamine biosynthesis II, UDP-N-acetyl-D-glucosamine biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-glucose 6-phosphotransferase
A group of enzymes found in invertebrates and microorganisms that are highly specific for glucose.
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CAS REGISTRY NUMBER
COMMENTARY
9001-36-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-N-[N-(6-aminohexhyl)carbamoyl]ATP + D-glucose
6-N-[N-(6-aminohexhyl)carbamoyl]ADP + D-glucose 6-phosphate
adenosine 5'-triphosphate-polyamidoamine dendrimer + D-glucose
adenosine 5'-diphosphate-polyamidoamine dendrimer + D-glucose 6-phosphate
-
-
-
-
ir
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
-
no reaction with the recombinant enzyme
-
-
-
ATP + mannoheptulose
?
-
sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
-
-
?
CTP + D-glucose
ADP + D-glucose 6-phosphate
38% of the velocity with ATP
-
-
?
6-N-(carboxyethyl)ATP + D-glucose
6-N-(carboxyethyl)ADP + D-glucose 6-phosphate
-
-
-
-
?
6-N-(carboxyethyl)ATP + D-glucose
6-N-(carboxyethyl)ADP + D-glucose 6-phosphate
-
-
-
-
?
6-N-(carboxymethyl)ATP + D-glucose
6-N-(carboxymethyl)ADP + D-glucose 6-phosphate
-
-
-
-
?
6-N-(carboxymethyl)ATP + D-glucose
6-N-(carboxymethyl)ADP + D-glucose 6-phosphate
-
-
-
-
?
6-N-(succinyl)ATP + D-glucose
6-N-(succinyl)ADP + D-glucose 6-phosphate
-
-
-
-
?
6-N-(succinyl)ATP + D-glucose
6-N-(succinyl)ADP + D-glucose 6-phosphate
-
-
-
-
?
6-N-[N-(6-aminohexhyl)carbamoyl]ATP + D-glucose
6-N-[N-(6-aminohexhyl)carbamoyl]ADP + D-glucose 6-phosphate
-
-
-
-
?
6-N-[N-(6-aminohexhyl)carbamoyl]ATP + D-glucose
6-N-[N-(6-aminohexhyl)carbamoyl]ADP + D-glucose 6-phosphate
-
-
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
3% of the velocity with ATP
-
-
?
ADP + D-glucose
AMP + D-glucose 6-phosphate
3% of the velocity with ATP
-
-
?
ATP + 2-deoxy-D-glucose
ADP + 2-deoxy-D-glucose 6-phosphate
-
no reaction with the recombinant enzyme
-
-
-
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
-
26% of the activity with D-glucose
-
-
ir
ATP + D-fructose
ADP + D-fructose 6-phosphate
-
no reaction with the recombinant enzyme
-
-
-
ATP + D-fructose
ADP + D-fructose 6-phosphate
3% of the velocity with D-glucose
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
3% of the velocity 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
-
highly specific for D-glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
specific for D-glucose, substrate binding site structure
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
highly specific for 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
-
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
-
sugar binding to recombinant wild-type and mutant glucokinase monitored by kinetic measurement and tryptophan fluorescence
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
enzyme is only able to phosphorylate glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
ATP is the most efficient phosphoryl donor
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
ATP is the most efficient phosphoryl donor
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the enzyme initiates the intracellular glucose catabolism/metabolism, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the enzyme initiates the intracellular glucose catabolism/metabolism, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
highly specific for D-glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the enzyme catalyzes the first step of the Embden-Meyerhoff pathway and the Entner-Douderoff pathway
-
-
ir
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the enzyme is specific for D-glucose
-
-
ir
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
enzyme is only able to phosphorylate glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
highly specific for D-glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
phosphorylates alpha-D-glucose and beta-D-glucose equally fast
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
-
no reaction with the recombinant enzyme
-
-
-
ATP + D-mannose
ADP + D-mannose 6-phosphate
99% of the velocity with D-glucose
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
99% of the velocity with D-glucose
-
-
?
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 + N-acetyl-alpha-D-glucosamine
ADP + N-acetyl-alpha-D-glucosamine 6-phosphate
-
at pH 7.6: 50% of the activity with alpha-D-glucose, at pH 9.0: 5% of the activity with alpha-D-glucose
-
-
?
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
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
10% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
less than 10% of the activity with ATP
-
-
?
CTP + D-glucose
CDP + D-glucose 6-phosphate
-
5% of the activity with ATP as phosphoryl donor
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
no reaction with the recombinant enzyme
-
-
-
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
30% of the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
less than 10% of ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
-
12% of the activity with ATP as phosphoryl donor
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
75% 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
-
30% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
less than 10% of the activity with ATP
-
-
?
ITP + D-glucose
IDP + D-glucose 6-phosphate
-
20% of the activity with ATP as phosphoryl donor
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
no reaction with the recombinant enzyme
-
-
-
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
32% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
12% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
less than 10% of the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
-
12% of the activity with ATP as phosphoryl donor
-
-
?
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
?
-
-
no substrate: N-acetyl-D-glucosamine, D-galactose
-
-
-
additional information
?
-
no substrate: N-acetyl-D-glucosamine, D-galactose
-
-
-
additional information
?
-
no substrate: N-acetyl-D-glucosamine, D-galactose
-
-
-
additional information
?
-
-
not: mannose, fructose, 2-deoxyglucose, UTP, ITP, GTP
-
-
-
additional information
?
-
-
recombinant enzymes NanK and YajF also utilize N-acetyl-D-mannosamine and D-fructose as substrates, respectively
-
-
-
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
?
-
-
less than 10% of the activity with ATP: TTP
-
-
-
additional information
?
-
-
less than 10% of the activity with ATP: TTP
-
-
-
additional information
?
-
-
less than 10% of the activity with ATP: TTP
-
-
-
additional information
?
-
-
less than 10% of the activity with ATP: TTP
-
-
-
additional information
?
-
comparison of the biochemical properties to those of the enzyme from Streptomyces peucetius var. caesius
-
-
-
additional information
?
-
-
comparison of the biochemical properties to those of the enzyme from Streptomyces coelicolor
-
-
-
additional information
?
-
-
no activity with D-mannose and D-fructose as phosphoryl acceptors, no activity with UDP, ADP, acetyl phosphate, and diphosphate as phosphoryl donors
-
-
-
additional information
?
-
-
no activity with fructose, galactose, and mannose, development of a coupled assay method with glucose 6-phosphate dehydrogenase stable at pH 6.8-8.5 and 75-90°C, overview
-
-
-
additional information
?
-
-
enzyme reacts equally well with ATP, UTP, GTP, ITP and CTP
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
the enzyme initiates the intracellular glucose catabolism/metabolism, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the enzyme initiates the intracellular glucose catabolism/metabolism, overview
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
the enzyme catalyzes the first step of the Embden-Meyerhoff pathway and the Entner-Douderoff pathway
-
-
ir
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
-
?
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
adenosine 5'-triphosphate-polyamidoamine dendrimer, polymer-bound ATP by direct coupling, kinetics and initial reaction rates differ from ATP
-
ATP
-
as MgATP2-, binding site structure, ATP binding involves residues Asp78, Thr82, Gly227, Thr228, and S336
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
0.4% of the activity with Mg2+
Mg2+
Mn2+
Ni2+
Zn2+
Ca2+
13.4% of the activity with Mg2+
Co2+
-
more efficient than Mg2+ in activation, relative rate 264%
Mg2+
required, best activating cation
Mg2+
-
absolute requirement for divalent cation, 78% of the activity with Mn2+; Km: 0.27 mM
Mn2+
-
more efficient than Mg2+ in activation, relative rate 173%
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-deoxy-2-([[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]amino)-beta-D-glucopyranose
-
-
2-deoxy-2-[[3-(4-hydroxyphenyl)propanoyl]amino]-alpha-D-glucopyranose
-
186fold selectivity for Trypanosoma cruzi over human enzyme
2-[[(benzyloxy)carbonyl]amino]-2-deoxy-beta-D-glucopyranose
-
245fold selectivity for Trypanosoma cruzi over human enzyme
6-Amino-6-deoxy-D-glucose
-
noncompetitive to ATP and competitive to glucose
adenosine 5'-diphosphate-polyamidoamine dendrimer
-
product inhibition
-
beta,gamma-methyleneadenosine 5'-thiophosphate
-
noncompetitive to ATP and uncompetitive to glucose
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
-
human glucokinase regulatory protein
-
inhibition is reversed by activator RO-28-1675
-
palmitoyl-CoA
-
glucokinase is inhibited by endogenous long-chain fatty acyl-CoA in islets from omega3-depleted rats
D-glucose 6-phosphate
-
competitive inhibitor to glucose and noncompetitive to ATP
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
-
of human or rat origin, inhibits the wild-type enzyme in presence or absence of sorbitol 6-phosphate, no inhibition of mutant V62M by both proteins
-
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
-
additional information
-
not: glucose or ATP up to 15 mM, mannose, fructose, 2-deoxyglucose, GDP, IDP, CDP, UDP, adenosine monophosphate, deoxyadenosine monophosphate, 3',5'-adenosine monophosphate, inorganic phosphate
-
additional information
-
catabolite repression of the glucokinase pathway and the TOL pathway is triggered by two different catabolite repression systems, repression of the glucokinase pathway is channeled through Crc
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
(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)-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-[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-(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-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
-
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-[4-(methylsulfonyl)phenyl]-3-(tetrahydro-2H-pyran-4-yl)-N-(1,3-thiazol-2-yl)propanamide
-
activation: 2.45fold
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
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
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-tert-butylthiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)-propanamide
-
activation: 1.29fold
N-(5-bromo-4-isopropylthiazol-2-yl)-2-(4-(cyclopropylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.67fold
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-fluorobenzo[d]thiazol-2-yl)-2-(4-(methylsulfonyl)phenyl)-3-(tetrahydro-2H-pyran-4-yl)propanamide
-
activation: 1.3fold
RO-0274375
-
synthetic activator, activation of wild-type enzyme and mutants V62A, V62T, and V62L, no activation of mutants V62Q, V62E, V62F, and V62K
-
RO-028165
-
synthetic activator, activation of wild-type enzyme and mutants V62A, V62T, and V62L, no activation of mutants V62Q, V62E, V62F, and V62K
-
RO-0283946
-
synthetic activator, activation of wild-type enzyme and mutants V62A, V62T, and V62L, no activation of mutants V62Q, V62E, V62F, and V62K
-
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
-
the enzyme is 2.12fold induced by growth on glucose compared to citrate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00000049
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; 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; 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
0.16
ATP
mutant enzyme V182L, glutathione S-transferase glucokinase B fusion protein
0.16
ATP
-
wild-type, 37°C, pH not specified in the puclication; 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
0.2
ATP
-
deletion mutant lacking residues 66-71, pH 7.6, 25 °C; deletion mutant lacking residues 68-71, pH 7.6, 25 °C
0.21
ATP
mutant enzyme Y61S, glutathione S-transferase glucokinase B fusion protein
0.31
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant 454-Ala; 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
0.35
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A456V; pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K140E
0.38
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V455M
0.39
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G68K
0.4
ATP
mutant enzyme E265K, glutathione S-transferase glucokinase B fusion protein
0.4
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197E
0.41
ATP
mutant enzyme K420E, glutathione S-transferase glucokinase B fusion protein
0.45
ATP
wild-type glutathione S-transferase glucokinase B fusion protein
0.46
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, wild-type
0.48
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V91L
0.5
ATP
-
mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C; wild-type, pH 7.6, 25 °C
0.52
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V62M
0.53
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V452L
0.57
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant T65I
0.58
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y215A
0.63
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S263P
0.69
ATP
mutant enzyme A379V, glutathione S-transferase glucokinase B fusion protein
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
0.87
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A379T
0.89
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant C213R
0.92
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214A
1.08
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214C
1.31
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197L
1.39
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I
1.42
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y214A/V452A
1.5
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant E442K
1.53
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K414E
1.59
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64Y
2.08
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant P417R
2.71
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T
3.32
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M298K
12.6
ATP
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S336L
2 - 3
D-glucose
-
enzyme from active animals, S0.5 value, Hill coefficient 1.16, pH 7.8, 2°C
2.5
D-glucose
-
deletion mutant lacking residues 68-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25 °C
3.1
D-glucose
-
deletion mutant lacking residue 71, K0.5 value, Hill coefficient 1.5, pH 7.6, 25 °C
3.2
D-glucose
-
deletion mutant lacking residues 67-71, K0.5 value, Hill coefficient 1.1, pH 7.6, 25 °C
3.3
D-glucose
-
mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C
3.6
D-glucose
-
deletion mutant lacking residues 66-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25 °C
6.23
D-glucose
-
enzyme from active animals, S0.5 value, Hill coefficient 1.7, pH 7.8, 25°C
9
D-glucose
-
enzyme from hibernating animals, S0.5 value, Hill coefficient 1.6, pH 7.8, 25°C
10.6
D-glucose
-
deletion mutant lacking residues 70-71, K0.5 value, Hill coefficient 1.3, pH 7.6, 25 °C
45
D-glucose
-
enzyme from hibernating animals, S0.5 value, Hill coefficient 1.2, pH 7.8, 2°C
additional information
additional information
-
wild-type and mutant enzymes, cooperative/sigmoidal glucose-dependent kinetics
-
additional information
additional information
-
kinetics with cofactor ATP and with adenosine 5'-triphosphate-polyamidoamine dendrimer as cofactor, overview
-
additional information
additional information
-
kinetic analysis, wild-type and mutant enzymes, overview
-
additional information
additional information
-
activation energy, kinetics
-
additional information
additional information
kinetic mechanism
-
additional information
additional information
-
kinetic mechanism
-
additional information
additional information
-
positive cooperation, mechanism, kinetic model
-
additional information
additional information
-
kinetic constants of TcGlcK obtained for different anomer solutions of D-glucose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
68.4
ATP
-
wild-type, 37°C, pH not specified in the puclication; wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 60 mM D-glucose
5.9
beta-D-glucose
-
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
2.46
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S336L
17.7
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197E
19.9
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K414E
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
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
37.7
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M298K
40
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant K140E
43.2
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G68K
44.6
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S263P
44.7
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant Y215A
47.2
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V62M
48.3
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant P417R
50
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant C213R
50.2
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T
52.2
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant 454-Ala
52.6
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant E442K
56
D-glucose
-
mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C
58.1
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I
60.6
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V91L
61.2
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
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
83.3
D-glucose
-
pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant S64P
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0041
2-deoxy-2-([[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]amino)-beta-D-glucopyranose
-
His-tagged recombinant protein, pH 7.2, 22°C
0.0013
2-deoxy-2-[[3-(4-hydroxyphenyl)propanoyl]amino]-alpha-D-glucopyranose
-
His-tagged recombinant protein, pH 7.2, 22°C
0.00071
2-[[(benzyloxy)carbonyl]amino]-2-deoxy-beta-D-glucopyranose
-
His-tagged recombinant protein, pH 7.2, 22°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.57
-
rat hepatocytes treated with adenovirus containing the entire coding sequence of rat liver glucokinase
additional information
additional information
-
activity of the enzyme in isogenic mutants with mutations in the glucose metabolism network, overview
additional information
-
determination of glucokinase activity in glucose metabolism, KT2440 metabolizes glucose and toluene simultaneously, the effect of toluene on glucose metabolism is directed to the glucokinase branch repressing glucokinase activity, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
7.5
7.6
7.8
8.5 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10.5
-
pH 6.0: about 30% of activity maximum, pH 10.5: about 80% of activity maximum
6 - 9
-
pH 6.0: about 55% of activity maximum, pH 9.0: about 75% of activity maximum
additional information
-
development of an assay method stable at pH 6.8-8.5 and 75-90°C, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38 - 98
-
below 10% of maximal activity at 38°C, about 90% of maximal activity at 98°C
additional information
-
development of an assay method stable at pH 6.8-8.5 and 75-90°C, overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
641068, 660810, 660963, 661567, 663393, 685006, 687771, 721535, 721735, 721827, 721837, 722237, 723509, 737327, 738711
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
glk is a nonessential gene that is constitutively expressed during logarithmic growth and has slightly reduced expression in the stationary phase
brenda
-
the rate of glucose phosphorylation in hepatocytes is determined by the subcellular location of glucokinase and by its association with its regulatory protein (GKRP) in the nucleus. Elevated glucose concentrations and precursors of fructose 1-phosphate (e.g., sorbitol) cause dissociation of glucokinase from GKRP and translocation to the cytoplasm. Mechanisms downstream of AMPK activation, involving phosphorylation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and GKRP are involved in the ATP-independent inhibition of glucose-induced glucokinase translocation by 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside in hepatocytes
brenda
-
glucokinase is inhibited by endogenous long-chain fatty acyl-CoA in islets from omega3-depleted rats. Such an inhibition probably participates to the alteration of D-glucose catabolism prevailing in these islets
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
over 96% of the enzyme content in the cell
brenda
-
over 96% of the enzyme content in the cell
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
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
the abundance enzme is attenuated when culture temperature is elevated and is almost undetectable at 80°C. The glucokinase interacts with heat shock protein HSP60 at 60°C and 75°C
metabolism
-
the abundance enzme is attenuated when culture temperature is elevated and is almost undetectable at 80°C. The glucokinase interacts with heat shock protein HSP60 at 60°C and 75°C
-
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
-
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
-
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
-
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
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
Lactococcus lactis subsp. lactis (strain IL1403)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Trypanosoma cruzi (strain CL Brener)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
43000
-
x * 43000, the enzyme may occur as a monomer or dimer, dependent on the protein concentration, SDS-PAGE
46000
70000
recombinant enzyme, oxidative conditions, PAGE, the wild-type and mutant enzymes occur as both monomer and homodimer
86000
35000
recombinant enzyme, oxidative conditions, PAGE, the wild-type and mutant enzymes occur as both monomer and homodimer
46000
x * 46000, the enzyme may occur as a monomer or dimer, dependent on the protein concentration, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
tetramer
additional information
?
x * 46000, the enzyme may occur as a monomer or dimer, dependent on the protein concentration, SDS-PAGE
?
-
x * 43000, the enzyme may occur as a monomer or dimer, dependent on the protein concentration, SDS-PAGE
dimer
2 * 35200, about, mass spectrometry, 2 * 35000, recombinant enzyme, PAGE under oxidative conditions or SDS-PAGE in absence of reductants, the wild-type and mutant enzymes occur as both monomer and homodimer
monomer
1 * 35200, about, mass spectrometry, 1 * 35000, recombinant enzyme, PAGE under reducing conditions or SDS-PAGE in absence of reductants, the wild-type and mutant enzymes occur as both monomer and homodimer
tetramer
-
SgGlkA is divided into a small alpha/beta domain and a large alpha + beta domain, and it forms a dimer-of-dimer tetrameric configuration
additional information
the active site is located in a deep cleft between the 2 domains of each subunit, monomer and dimer structures, overview
additional information
-
determination of active open and inactive closed enzyme conformation and structure, folding patterns, conformational changes, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
glucokinase is modified by O-GlcNAcylation. siRNA-mediated O-linked N-acetylglucosamine transferase knock-down not only decreases O-GlcNAc content but also glucokinase protein level
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant selenomethionine-labeled enzyme free or in complex with D-glucose, hanging drop vapour diffusion method, 0.002 ml enzyme solution containing 6.8 mg/ml protein mixed with 0.004 ml reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, and 1.7 M ammonium sulfate for the apo-enzyme or 18.5-20% PEG 6000 with 2 mM D-glucose and 2-3 mM ADP for the glucose-bound enzyme, X-ray diffraction structure determination and analysis at 2.3-2.2 A resolution
homology modeling of structure reveals high structural homology with human glucokinase
first structures of a glucokinase-glucose complex without activator, of glucokinase-glucose-AMP-PNP and of glucokinase-glucose-AMP-PNP with a bound activator are reported. All structures are extremely similar, thus demonstrating that binding of GK activators does not result in conformational changes of the active protein but in stabilization of the active form of glucokinase
-
molecular docking of glucose and synthetic ligands (allosteric activators). Predicted position of glucose coincides with its position in the crystallographic complex. Glucose interacts with the residues of large (Ile225, Gly229, Cys230, Asn231, Glu256, Gln287, Glu290) and small (Ser151, Phe152, Pro153, Thr168, Lys169) domains and with the residues of connecting region Asn204, Asp205. Hydrogen bonds with Asp205, Glu256 and Glu290 stabilize this complex. The allosteric site formed by the small and large domains and two loops connecting them is located approximately 20 A away from the glucose binding site. There are two stable positions of glucokinase activators and approximately five sites of ligand binding with less favorable interaction energy. Predicted position of glucose coincides with its position in the crystallographic complex
-
purified recombinant hepatic wild-type and deletion mutant enzymes in complex with either D-glucose or the synthetic activator 2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-thiazol-2-yl-benzamide, hanging drop vapour diffusion method, 10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, 5 mM Tris(2-carboxyethyl)phosphine hydrochloride, and 20 mM D-glucose, or 0.3 mM compound A, 0.0015-0.003 ml of the solution is mixed with an equal volume of precipitant solution containing 28-30% PEG 1500, 0.1 M HEPES-NaOH, pH 6.0, equilibration against 1 ml precipitant solution, 1 week, crystallization of the free hepatic enzyme by using precipitant solution containing 50 mM NaCl, 1.5-1.6 M ammonium sulfate, and 0.1 M bicine-NaOH, pH 8.7, 1 week, X-ray diffraction structure determination and analysis at 2.3 and 3.4 A resolution, respectively, molecular replacement
-
homology modeling of structure. Staphylococcus aureus glucokinase exhibits very close homology with Enterococcus faecalis and Clostridium difficle while with other bacteria it show a high degree of variations both in domain and nondomain regions. Glucose interacts with residues V77, N114, S161 and G160 forming a total of eight hydrogen bonds. Glucose docking score is -12.3697 kcal/mol
crystal structures of apo-SgGlkA, SgGlkA in complex with glucose, and SgGlkA in complex with glucose and adenylyl imidodiphosphate (AMPPNP) are reported. SgGlkA is divided into a small alpha/beta domain and a large alpha + beta domain, and it forms a dimer-of-dimer tetrameric configuration
-
crystallized using the sitting-drop vapour-diffusion method. A crystal of SgGlkA in complex with glucose is obtained and diffracted X-rays to 1.84 A resolution
-
crystal structures in complexes with inhibitors 2-[[(benzyloxy)carbonyl]amino]-2-deoxy-beta-D-glucopyranose, 2-deoxy-2-[[3-(4-hydroxyphenyl)propanoyl]amino]-alpha-D-glucopyranose, 2-deoxy-2-([[(1,1-dioxido-1-benzothiophen-2-yl)methoxy]carbonyl]amino)-beta-D-glucopyranose. The analogues all share a common glucose moietythat preserves key enzyme-substrate hydrogen bonding interactions with the monosaccharide hydroxyl groups from C1, C3, C4,and C6. The C2 hydroxyl is replaced by a NH group and also par-ticipates in the key hydrogen bonding
-
crystals of TcGlcK in complex with D-glucose and ADP are obtained by the hanging-drop, vapor-diffusion method, using PEG3350 as precipitant agent and diammonium hydrogen citrate as additive. A complete native dataset is collected to 2.1 A maximum resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C166A
site-directed mutagenesis, mutant shows activity similar to the wild-type enzyme
C175A
site-directed mutagenesis, inactive active site residue mutant
C177A
site-directed mutagenesis, inactive active site residue mutant
C182A
site-directed mutagenesis, inactive active site residue mutant
C282A
site-directed mutagenesis, mutant shows slightly increased enzyme activity compared to the wild-type enzyme, conformational changes different from the wild-type enzyme, overview
C321A
site-directed mutagenesis, mutant shows 5fold increased enzyme activity compared to the wild-type enzyme, conformational changes different from the wild-type enzyme, overview
D10K
site-directed mutagenesis, ATP binding site mutant, inactive mutant
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
A456V
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
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%
D158A
-
naturally occurring mutation, activity and kinetics are similar to the wild-type enzyme
D78A/D158A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
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
E300K
-
site-directed mutagenesis, mutant shows decreased activity and increased thermolability compared to the wild-type enzyme
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
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%
G227A/D158A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
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%
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
-
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%
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%
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
K90A/D158A
-
site-directed mutagenesis, 2fold increased activity compared to the wild-type enzyme
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
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
-
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%
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%
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%
N166R-S151-A
-
lowers the KM-value for glucose by a factor of 40 and increases the KM-value for ATP
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%
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