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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
- pancreatic
- islet
- hepatocytes
- hexokinase
- mellitus
- glycogen
- beta-cell
- hyperglycemia
- glucose-6-phosphatase
- fructose
- pancreas
-
carboxykinase
-
maturity-onset
- phosphoenolpyruvate
- glucagon
-
glucose-stimulated
- 6-phosphate
-
glucose-induced
- triglyceride
-
gluconeogenesis
-
monogenic
-
hypoglycemic
-
phosphofructokinase
-
gluconeogenic
- pepck
-
non-insulin-dependent
-
antidiabetic
- c-peptide
-
insulin-secreting
- insulinomas
- sulfonylurea
- niddm
- hyperinsulinemia
-
insulin-producing
- glp-1
- g6pase
-
glucose-dependent
-
glucose-sensing
-
ins-1e
-
glut-2
- hyperinsulinism
-
kcnj11
- diazoxide
-
2.7.1.1
-
glucose-responsive
- substrate-2
-
perivenous
-
2,6-bisphosphate
-
glucose-lowering
- fructokinase
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
ATP-dependent glucokinase, ATP-GLK, GK, GlcK, glk, Glk1, glucokinase (phosphorylating), glucokinase 1, kinase, gluco- (phosphorylating), KlGlk1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP-dependent glucokinase
ATP-GLK
glk
glucokinase (phosphorylating)
-
-
-
-
glucokinase 1
kinase, gluco- (phosphorylating)
-
-
-
-
KlGlk1
KLLA0C01155g
NagC
Sw0678
Sw2155
Sw3773
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
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
the enzyme activity requires 3 cysteine residues C175, C177, and C182 within the motif CXCGX(2)GCXE that discriminates microbial glucokinases into two lineages
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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-alpha-D-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-sorbitol
ADP + ?
at 10% of the activity as compared to D-glucose
-
-
?
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
-
-
?
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
-
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-fructose
ADP + D-fructose 6-phosphate
at 70% of the activity as compared to D-glucose
-
-
?
ATP + D-fructose
ADP + D-fructose 6-phosphate
at 70% of the activity as compared to D-glucose
-
-
?
ATP + D-galactose
ADP + D-galactose
at 11% of the activity as compared to D-glucose
-
-
?
ATP + D-galactose
ADP + D-galactose
at 11% of the activity as compared to D-glucose
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
-
no reaction with the recombinant enzyme
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
D-glucose and D-glucosamine with nearly equal activity
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
D-glucose and D-glucosamine with nearly equal activity
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
-
-
-
?
ATP + D-glucosamine
ADP + D-glucosamine 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
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
no activity with fructose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
no activity with fructose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
enzyme is only able to phosphorylate glucose
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
D-glucose and D-glucosamine with nearly equal activity
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
D-glucose and D-glucosamine with nearly equal activity
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
no activity with CTP, ADP, PPi or polyP
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
no activity with CTP, ADP, PPi or polyP
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
limited hexose substrate range, with the greatest activity observed with 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
the enzyme phosphorylates various hexoses with a marked preference for glucose. ATP is the most preferred phosphoryl group donor. No activity with ADP or AMP as phosphoryl group donor
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
-
-
-
?
ATP + D-glucose
ADP + D-glucose 6-phosphate
the enzyme phosphorylates various hexoses with a marked preference for glucose. ATP is the most preferred phosphoryl group donor. No activity with ADP or AMP as phosphoryl group donor
-
-
?
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
at 30% of the activity as compared to D-glucose
-
-
?
ATP + D-mannose
ADP + D-mannose 6-phosphate
at 30% of the activity as compared to D-glucose
-
-
?
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
71% compared to the activity with ATP
-
-
?
GTP + D-glucose
GDP + D-glucose 6-phosphate
71% compared to 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
85% compared to the activity with ATP
-
-
?
UTP + D-glucose
UDP + D-glucose 6-phosphate
85% compared to 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
?
-
fructose, xylose, galactose, sucrose, lactose, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate or fructose-6-phosphate as a phosphate acceptor. GTP, CTP, UTP, ADP or PPi does not serve as a phosphoryl donor
-
-
-
additional information
?
-
fructose, xylose, galactose, sucrose, lactose, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate or fructose-6-phosphate as a phosphate acceptor. GTP, CTP, UTP, ADP or PPi does not serve as a phosphoryl donor
-
-
-
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
-
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
-
-
?
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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
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
CaCl2
MnCl2 yields 9% of the activity observed when MgCl2 is included in the assay
Cd2+
Co2+
Cu2+
Mg2+
MgCl2
the enzyme functions best when MgCl2 is included in the assay
Mn2+
MnCl2
MnCl2 yields 40% of the activity observed when MgCl2 is included in the assay
Ni2+
Sr2+
Zn2+
additional information
CuCl2, CoCl2, ZnCl2 or CaCl2 have no appreciable effect on the enzyme activity
Ca2+
13.4% of the activity with Mg2+
Co2+
-
more efficient than Mg2+ in activation, relative rate 264%
Cu2+
0.4% of the activity with Mg2+
Mg2+
required, best activating cation
Mg2+
highest activity is observed in the presence of 5 mM of MgCl2
Mg2+
-
absolute requirement for divalent cation, 78% of the activity with Mn2+
Mg2+
clear requirement for a divalent metal ion and a strong preference for Mg2+
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
4-(4-tert-butylbenzamido)-3',4',6-trichloro[1,1'-biphenyl]-3-carboxylic acid
-
4-(4-tert-butylbenzamido)-3',6-dichloro-4'-fluoro[1,1'-biphenyl]-3-carboxylic acid
-
4-(4-tert-butylbenzamido)-3',6-dichloro[1,1'-biphenyl]-3-carboxylic acid
-
4-(4-tert-butylbenzamido)-6-chloro-3'-nitro[1,1'-biphenyl]-3-carboxylic acid
-
4-(4-tert-butylbenzamido)-6-chloro-4'-(trifluoromethoxy)[1,1'-biphenyl]-3-carboxylic acid
-
4-(4-tert-butylbenzamido)-6-chloro-4'-(trifluoromethyl)[1,1'-biphenyl]-3-carboxylic acid
-
6-Amino-6-deoxy-D-glucose
-
noncompetitive to ATP and competitive to glucose
adenosine 5'-diphosphate-polyamidoamine dendrimer
-
product inhibition
-
ATP
the enzyme exists in two states with different catalytic activity, with an apparent transition point at 0.045 mM ATP. At higher ATP concentrations, strong inhibition takes place
beta,gamma-methyleneadenosine 5'-thiophosphate
-
noncompetitive to ATP and uncompetitive to glucose
D-glucose 6-phosphate
-
competitive inhibitor to glucose and noncompetitive to ATP
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
not affected by glucose 6-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
additional information
-
the enzyme is 2.12fold induced by growth on glucose compared to citrate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
D-glucose
pH and temperature not specified in the publication
6.61
D-glucose
pH and temperature not specified in the publication
additional information
additional information
kinetic mechanism
-
additional information
additional information
-
kinetic mechanism
-
additional information
additional information
-
activation energy, kinetics
-
additional information
additional information
-
kinetics with cofactor ATP and with adenosine 5'-triphosphate-polyamidoamine dendrimer as cofactor, overview
-
additional information
additional information
kinetic constants of TcGlcK obtained for different anomer solutions of D-glucose
-
additional information
additional information
-
kinetic constants of TcGlcK obtained for different anomer solutions of D-glucose
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
150
D-glucose
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
0.0569
hydroxyphenyloxopropyl glucosamine
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0029
4-(4-tert-butylbenzamido)-3',4',6-trichloro[1,1'-biphenyl]-3-carboxylic acid
Naegleria fowleri
pH and temperature not specified in the publication
0.0059
4-(4-tert-butylbenzamido)-3',6-dichloro-4'-fluoro[1,1'-biphenyl]-3-carboxylic acid
Naegleria fowleri
pH and temperature not specified in the publication
0.0065
4-(4-tert-butylbenzamido)-3',6-dichloro[1,1'-biphenyl]-3-carboxylic acid
Naegleria fowleri
pH and temperature not specified in the publication
0.0093
4-(4-tert-butylbenzamido)-6-chloro-3'-nitro[1,1'-biphenyl]-3-carboxylic acid
Naegleria fowleri
pH and temperature not specified in the publication
0.005
4-(4-tert-butylbenzamido)-6-chloro-4'-(trifluoromethoxy)[1,1'-biphenyl]-3-carboxylic acid
Naegleria fowleri
pH and temperature not specified in the publication
0.006
4-(4-tert-butylbenzamido)-6-chloro-4'-(trifluoromethyl)[1,1'-biphenyl]-3-carboxylic acid
Naegleria fowleri
pH and temperature not specified in the publication
0.00088
ebselen
Naegleria fowleri
pH and temperature not specified in the publication
0.0007
N,N'-[furan-2,5-diylbis(2-chloro-4,1-phenylene)]diguanidine
Naegleria fowleri
pH and temperature not specified in the publication
0.002
N,N'-[furan-2,5-diylbis(3-chloro-4,1-phenylene)]diguanidine
Naegleria fowleri
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
7.5
7.8
8.5
8.5 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
pH 4.5: about 45% of maximal activity, pH 8.5: about 45% of maximal activity
5 - 9.5
active in a wide range pH 5 to 9.5, sharp loss of activity above pH 9.5
6 - 10.5
-
pH 6.0: about 30% of activity maximum, pH 10.5: about 80% of activity maximum
6 - 8.5
pH 6.0: about 55% of maximal activity, pH 8.5: about 40% of maximal activity
6 - 9
-
pH 6.0: about 55% of activity maximum, pH 9.0: about 75% of activity maximum
6.5 - 8.5
pH 6.5: about 55% of maximal activity, pH 8.5: about 55% of maximal activity
7.5 - 9.5
pH 7.5: about 65% of maximal activity, pH 9.5: about 30% of maximal activity
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
42
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
25 - 50
25°C: about 45% of maximal activity, 50°C: about 25% of maximal activity
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
25 - 45
25°C: about 60% of maximal activity, 45°C: about 40% of maximal activity
25 - 45
25°C: about 65% of maximal activity, 45°C: about 80% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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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
drug target
glucokinase from pathogenic protozoa of the genus Leishmania is a potential drug target for the chemotherapeutic treatment against leishmaniasis because this enzyme is located at a nodal point between two critically important metabolic pathways, glycolysis and the pentose phosphate pathway
malfunction
metabolism
malfunction
chromosomal deletion of the glk gene resulted in a loss of glucokinase activity and retardation of growth as well as in a decrease of intracellular glycogen content
malfunction
-
chromosomal deletion of the glk gene resulted in a loss of glucokinase activity and retardation of growth as well as in a decrease of intracellular glycogen content
-
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 enzyme implicated in the regulation of glycogen biosynthesis and degradation in an obligate methanotroph
metabolism
the enzyme is an essential component required for glucose signaling
metabolism
the enzyme is located at a nodal point between two critically important metabolic pathways, glycolysis and the pentose phosphate pathway
metabolism
the enzyme plays a role in metabolism of nutrients acquired from the environment through either predation or directly from the sediment
metabolism
-
the enzyme is an essential component required for glucose signaling
-
metabolism
-
the enzyme implicated in the regulation of glycogen biosynthesis and degradation in an obligate methanotroph
-
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
-
Show AA Sequence and Transmembrane Helices (24172 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106500
gradient electrophoresis, non-denaturation conditions, trimer
142000
gradient electrophoresis, non-denaturation conditions, tetramer
177500
gradient electrophoresis, non-denaturation conditions, pentamer
213000
gradient electrophoresis, non-denaturation conditions, hexamer
35000
43000
x * 43000, the enzyme may occur as a monomer or dimer, dependent on the protein concentration, SDS-PAGE
46000
70000
71000
gradient electrophoresis, non-denaturation conditions, dimer
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
70000
recombinant enzyme, oxidative conditions, PAGE, the wild-type and mutant enzymes occur as both monomer and homodimer
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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 * 35500, SDS-PAGE, multimeric protein consisting of di-, tri-, tetra-, penta- and hexamers
?
-
x * 35500, SDS-PAGE, multimeric protein consisting of di-, tri-, tetra-, penta- and hexamers
-
?
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
homodimer
each subunit (both in open conformations) includes the typical small and large domains
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
-
the active site is located in a deep cleft between the 2 domains of each subunit, monomer and dimer structures, overview
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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
the enzyme is crystallized in an apo form. Sitting-drop vapor diffusion at room temperature
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
additional information
additional information
-
construction of an enzyme-deficient glk mutant strain BM5340(DE3), the mutant strain can be complemented by expression of Escherichia coli genes nanK, yajF, and ycfX, which express proteins with 4fold lower glucokinase activity and ambiguous substrate specificities, overview
additional information
-
site-specific homologous inactivation of gene glk to construct a mutant strain, activity of the enzyme in isogenic mutants with mutations in the glucose metabolism network, glk mutants exhibit a lower total carbon consumption rate than the parental strain, overview
additional information
-
site-specific homologous inactivation of gene glk to construct a mutant strain, activity of the enzyme in isogenic mutants with mutations in the glucose metabolism network, glk mutants exhibit a lower total carbon consumption rate than the parental strain, overview
-
additional information
-
construction of gene sll0593 deletion mutant, does not respond to glucose level in the growth medium, M1 and M2 show reduced activity in glucose growth medium, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
70
75
-
about 25% loss of activity in 30 min, presence of 0.01 M glucose + 0.2 M NaCl, about 90% loss of activity, presence of 0.01 M glucose absence of NaCl
additional information
70
-
about 10% loss of activity in 30 min, presence of 0.01 M glucose + 0.2 M NaCl
additional information
-
glucose or DTT protects against thermal inactivation at 25°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
urea
guanidine-HCl
no significant change in the CD spectra and enzyme activity after overnight incubation in the presence of 8 M urea or 1 M guanidinium chloride
guanidine-HCl
-
no significant change in the CD spectra and enzyme activity after overnight incubation in the presence of 8 M urea or 1 M guanidinium chloride
-
urea
no significant change in the CD spectra and enzyme activity after overnight incubation in the presence of 8 M urea or 1 M guanidinium chloride
urea
-
no significant change in the CD spectra and enzyme activity after overnight incubation in the presence of 8 M urea or 1 M guanidinium chloride
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
room temperature, 1 mM DTT, 5 mM MgCl2, stable for 1 week , 4°C, suspended precipitate in a 60% saturated solution of ammonium sulfate, stable for at least 3 months
room temperature, 1 mM DTT, 5 mM MgCl2, stable for 1 week , 4°C, suspended precipitate in a 60% saturated solution of ammonium sulfate, stable for at least 3 months
-
room temperature, 1 mM DTT, 5 mM MgCl2, stable for 1 week , 4°C, suspended precipitate in a 60% saturated solution of ammonium sulfate, stable for at least 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged recombinant TcGlcK is expressed in the Escherichia coli BL21 strain and purified to homogeneity by nickel affinity chromatography
recombinant enzyme
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment and Ni2+ chelating affinity chromatography
-
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain RB791 by nickel affinity chromatography
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3) by ultracentrifugation, nickel affinity chromatography, and gel filtration to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli. Expression of the gene is low resulting in a poor yield of the recombinant protein. A single site directed mutation in Pcal_1032 gene (Nucleotide G at position 11 is replaced by A), without altering the amino acid sequence, results in approximately tenfold higher expression
expression of genes nanK, yajF, and ycfX in glk-deficient mutant strain BM5340(DE3)
-
gene glcK, phylogenetic analysis and tree, functional complementation of enzyme-deficient Escherichia coli strain UE26, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain RB791 as soluble proteins
gene glk is organized in gene clusters, transcriptomic analysis of KT2440 in response to glucose, overview
-
gene TM 1469 or glk, functional expression of the soluble His-tagged in Escherichia coli strain BL21(DE3)
-
glcK open reading frame is cloned from Bacillus sphaericus strain C3-41 and then expressed in Escherichia coli
heterologous expression in Escherichia coli BL21 (DE3) as a C-terminal His6 version in an IPTG-inducible expression vector
the KLLA0C01155g gene is codon optimized for improved expression in Escherichia coli. Expression in Escherichia coli BL21 (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baumann, P.
Glucokinase of Dictyostelium discoideum
Biochemistry
8
5011-5015
1969
Dictyostelium discoideum
brenda
Porter, E.V.; Chassy, B.M.; Holmlund, C.E.
Purification and kinetic characterization of a specific glucokinase from Streptococcus mutans OMZ70 cells
Biochim. Biophys. Acta
709
178-186
1982
Streptococcus mutans
brenda
Porter, V.; Chassy, B.M.
Glucokinase from Streptococcus mutans
Methods Enzymol.
90
25-30
1982
Streptococcus mutans
-
brenda
Scopes, R.K.; Testolin, V.; Stoter, A.; Griffiths-Smith, K.; Algar, E.M.
Simultaneous purification and characterization of glucokinase, fructokinase and glucose-6-phosphate dehydrogenase from Zymomonas mobilis
Biochem. J.
228
627-634
1985
Zymomonas mobilis
brenda
Doelle, H.W.
Kinetic characteristics and regulatory mechanisms of glucokinase and fructokinase from Zymomonas mobilis
Eur. J. Appl. Microbiol. Biotechnol.
14
241-246
1982
Zymomonas mobilis
-
brenda
Hengartner, H.; Zuber, H.
Isolation and characterization of a thermophilic glucokinase from Bacillus stearothermophilus
FEBS Lett.
37
212-216
1973
Geobacillus stearothermophilus
brenda
Klein, D.P.; Charles, A.M.
Purification and physical properties of glucokinase from Thiobacillus versutus (A2)
Can. J. Microbiol.
32
937-941
1986
Paracoccus versutus, Paracoccus versutus A2
-
brenda
Goward, C.R.; Hartwell, R.; Atkinson, T.; Scawen, M.D.
The purification and characterization of glucokinase from the thermophile Bacillus stearothermophilus
Biochem. J.
237
415-420
1986
Geobacillus stearothermophilus
brenda
Sakuraba, H.; Mitani, Y.; Goda, S.; Kawarabayasi, Y.; Ohshima, T.
Cloning, expression, and characterization of the first archaeal ATP-dependent glucokinase from aerobic hyperthermophilic archaeon Aeropyrum pernix
J. Biochem.
133
219-224
2003
Aeropyrum pernix
brenda
Tomita, K.; Ikeda, T.; Takahashi, T.
Synthesis of adenosine 5'-triphosphate derivatives and their substrate activities to thermostable glucokinases
Ann. N. Y. Acad. Sci.
864
548-551
1998
Geobacillus stearothermophilus, Zymomonas mobilis
-
brenda
Arora, K.K.; Pedersen, P.L.
Glucokinase of Escherichia coli: induction in response to the stress of overexpressing foreign proteins
Arch. Biochem. Biophys.
319
574-579
1995
Escherichia coli
brenda
Meyer, D.; Schneider-Fresenius, C.; Horlacher, R.; Peist, R.; Boos, W.
Molecular characterization of glucokinase from Escherichia coli K-12
J. Bacteriol.
179
1298-1306
1997
Escherichia coli
brenda
Laht, S.; Karp, H.; Kotka, P.; Jarviste, A.; Alamae, T.
Cloning and characterization of glucokinase from a methylotrophic yeast Hansenula polymorpha: different effects on glucose repression in H. polymorpha and Saccharomyces cerevisiae
Gene
296
195-203
2002
Aspergillus niger (Q92407), Aspergillus niger, Saccharomyces cerevisiae (P17709), Saccharomyces cerevisiae, Yarrowia lipolytica
brenda
Scopes, R.K.; Bannon, D.R.
Kinetic analysis of the activation of Zymomonas mobilis glucokinase by phosphate
Biochim. Biophys. Acta
1249
173-179
1995
Zymomonas mobilis
brenda
McCarthy, J.K.; O'Brien, C.E.; Eveleigh, D.E.
Thermostable continuous coupled assay for measuring glucose using glucokinase and glucose-6-phosphate dehydrogenase from the marine hyperthermophile Thermotoga maritima
Anal. Biochem.
318
196-203
2003
Thermotoga maritima
brenda
Abdelmoez, W.; Bobe, I.; Ishimi, K.; Yasuda, M.; Ishikawa, H.
Kinetics of the reaction catalyzed by Bacillus stearothermophilus glucokinase using the carboxy-terminated PAMAM-bound adenine nucleotides as cofactors
Biochem. Eng. J.
20
35-38
2004
Geobacillus stearothermophilus
-
brenda
Miller, B.G.; Raines, R.T.
Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases
Biochemistry
43
6387-6392
2004
Escherichia coli K-12
brenda
Mesak, L.R.; Mesak, F.M.; Dahl, M.K.
Bacillus subtilis GlcK activity requires cysteines within a motif that discriminates microbial glucokinases into two lineages
BMC Microbiol.
4
6-13
2004
Bacillus subtilis (P54495), Bacillus subtilis
brenda
Hansen, T.; Schonheit, P.
ATP-dependent glucokinase from the hyperthermophilic bacterium Thermotoga maritima represents an extremely thermophilic ROK glucokinase with high substrate specificity
FEMS Microbiol. Lett.
226
405-411
2003
Thermotoga maritima
brenda
Lunin, V.V.; Li, Y.; Schrag, J.D.; Iannuzzi, P.; Cygler, M.; Matte, A.
Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose
J. Bacteriol.
186
6915-6927
2004
Escherichia coli (P0A6V9), Escherichia coli
brenda
Lee, J.M.; Ryu, J.Y.; Kim, H.H.; Choi, S.B.; Tandeau de Marsac, N.; Park, Y.I.
Identification of a glucokinase that generates a major glucose phosphorylation activity in the cyanobacterium Synechocystis sp. PCC 6803
Mol. Cell
19
256-261
2005
Synechocystis sp.
brenda
Imriskova, I.; Arreguin-Espinosa, R.; Guzman, S.; Rodriguez-Sanoja, R.; Langley, E.; Sanchez, S.
Biochemical characterization of the glucose kinase from Streptomyces coelicolor compared to Streptomyces peucetius var. caesius
Res. Microbiol.
156
361-366
2005
Streptomyces coelicolor (P0A4E1), Streptomyces peucetius subsp. caesius
brenda
Han, B.; Liu, H.; Hu, X.; Cai, Y.; Zheng, D.; Yuan, Z.
Molecular characterization of a glucokinase with broad hexose specificity from Bacillus sphaericus strain C3-41
Appl. Environ. Microbiol.
73
3581-3586
2007
Lysinibacillus sphaericus C3-41 (A0SZU9)
brenda
Rui, O.; Hahn, M.
The Botrytis cinerea hexokinase, Hxk1, but not the glucokinase, Glk1, is required for normal growth and sugar metabolism, and for pathogenicity on fruits
Microbiology
153
2791-2802
2007
Botrytis cinerea (A1Z0M6), Botrytis cinerea
brenda
Späth, C.; Kraus, A.; Hillen, W.
Contribution of glucose kinase to glucose repression of xylose utilization in Bacillus megaterium
J. Bacteriol.
179
7603-7605
1997
Priestia megaterium (O31392)
brenda
del Castillo, T.; Ramos, J.L.; Rodriguez-Herva, J.J.; Fuhrer, T.; Sauer, U.; Duque, E.
Convergent peripheral pathways catalyze initial glucose catabolism in Pseudomonas putida: genomic and flux analysis
J. Bacteriol.
189
5142-5152
2007
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
del Castillo, T.; Ramos, J.L.
Simultaneous catabolite repression between glucose and toluene metabolism in Pseudomonas putida is channeled through different signaling pathways
J. Bacteriol.
189
6602-6610
2007
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Cordeiro, A.T.; Caceres, A.J.; Vertommen, D.; Concepcion, J.L.; Michels, P.A.; Versees, W.
The crystal structure of Trypanosoma cruzi glucokinase reveals features determining oligomerization and anomer specificity of hexose-phosphorylating enzymes
J. Mol. Biol.
372
1215-1226
2007
Trypanosoma cruzi (Q4E4E1), Trypanosoma cruzi
brenda
Caceres, A.J.; Quinones, W.; Gualdron, M.; Cordeiro, A.; Avilan, L.; Michels, P.A.; Concepcion, J.L.
Molecular and biochemical characterization of novel glucokinases from Trypanosoma cruzi and Leishmania spp
Mol. Biochem. Parasitol.
156
235-245
2007
Trypanosoma cruzi (Q4E4E1), Trypanosoma cruzi, Leishmania major (Q4Q1I9), Leishmania major
brenda
Miyazono, K.; Tabei, N.; Marushima, K.; Ohnishi, Y.; Horinouchi, S.; Tanokura, M.
Purification, crystallization and preliminary X-ray analysis of glucokinase from Streptomyces griseus in complex with glucose
Acta Crystallogr. Sect. F
67
914-916
2011
Streptomyces griseus (B1VZT1), Streptomyces griseus
brenda
Miyazono, K.; Tabei, N.; Morita, S.; Ohnishi, Y.; Horinouchi, S.; Tanokura, M.
Substrate recognition mechanism and substrate-dependent conformational changes of an ROK family glucokinase from Streptomyces griseus
J. Bacteriol.
194
607-616
2012
Streptomyces griseus (B1VZT1), Streptomyces griseus
brenda
Qian, Z.; Zhao, J.; Bai, X.; Tong, W.; Chen, Z.; Wei, H.; Wang, Q.; Liu, S.
Thermal stability of glucokinases in Thermoanaerobacter tengcongensis
BioMed Res. Int.
2013
646539
2013
Caldanaerobacter subterraneus subsp. tengcongensis (Q8RDE9), Caldanaerobacter subterraneus subsp. tengcongensis, Caldanaerobacter subterraneus subsp. tengcongensis DSM 15242 (Q8RDE9)
brenda
Kumar, P.S.; Kumar, Y.N.; Prasad, U.V.; Yeswanth, S.; Swarupa, V.; Vasu, D.; Venkatesh, K.; Srikanth, L.; Rao, V.K.; Sarma, P.V.
Comparative structural and functional analysis of Staphylococcus aureus glucokinase with other bacterial glucokinases
Indian J. Pharm. Sci.
76
430-436
2014
Staphylococcus aureus (H6UH58), Staphylococcus aureus, Staphylococcus aureus ATCC 12600 (H6UH58)
brenda
DAntonio, E.L.; Deinema, M.S.; Kearns, S.P.; Frey, T.A.; Tanghe, S.; Perry, K.; Roy, T.A.; Gracz, H.S.; Rodriguez, A.; DAntonio, J.
Structure-based approach to the identification of a novel group of selective glucosamine analogue inhibitors of Trypanosoma cruzi glucokinase
Mol. Biochem. Parasitol.
204
64-76
2015
Trypanosoma cruzi (Q4E4E1), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4E4E1)
brenda
Milanes, J.E.; Suryadi, J.; Abendroth, J.; Van Voorhis, W.C.; Barrett, K.F.; Dranow, D.M.; Phan, I.Q.; Patrick, S.L.; Rozema, S.D.; Khalifa, M.M.; Golden, J.E.; Morris, J.C.
Enzymatic and structural characterization of the Naegleria fowleri glucokinase
Antimicrob. Agents Chemother.
63
e02410-18
2019
Naegleria fowleri (A0A384E136), Naegleria fowleri
brenda
Mustakhimov, I.I.; Rozova, O.N.; Solntseva, N.P.; Khmelenina, V.N.; Reshetnikov, A.S.; Trotsenko, Y.A.
The properties and potential metabolic role of glucokinase in halotolerant obligate methanotroph Methylomicrobium alcaliphilum 20Z
Antonie van Leeuwenhoek
110
375-386
2017
Methylomicrobium alcaliphilum (G4T1H4), Methylomicrobium alcaliphilum 20Z (G4T1H4)
brenda
Conway, L.P.; Liu, F.F.; Li, Q.; Voglmeir, J.
The Shewanella woodyi galactokinase pool phosphorylates glucose at the 6-position
Carbohydr. Res.
455
39-44
2018
Shewanella woodyi (B1KD89), Shewanella woodyi (B1KDE7), Shewanella woodyi (B1KRG2), Shewanella woodyi ATCC 51908 (B1KD89), Shewanella woodyi ATCC 51908 (B1KDE7), Shewanella woodyi ATCC 51908 (B1KRG2)
brenda
Bibi, T.; Ali, M.; Rashid, N.; Muhammad, M.A.; Akhtar, M.
Enhancement of gene expression in Escherichia coli and characterization of highly stable ATP-dependent glucokinase from Pyrobaculum calidifontis
Extremophiles
22
247-257
2018
Pyrobaculum calidifontis (A3MUZ0), Pyrobaculum calidifontis, Pyrobaculum calidifontis JCM 11548 (A3MUZ0)
brenda
Zak, K.M.; Kalilska, M.; Wator, E.; Kuska, K.; Krutyholowa, R.; Dubin, G.; Popowicz, G.M.; Grudnik, P.
Crystal structure of Kluyveromyces lactis glucokinase (KlGlk1)
Int. J. Mol. Sci.
20
4821
2019
Kluyveromyces lactis (Q6CUZ3), Kluyveromyces lactis, Kluyveromyces lactis ATCC 8585 (Q6CUZ3)
brenda
Buechner, G.S.; Millington, M.E.; Perry, K.; DAntonio, E.L.
The crystal structure of glucokinase from Leishmania braziliensis
Mol. Biochem. Parasitol.
227
47-52
2019
Leishmania braziliensis (A4HPA0), Leishmania braziliensis
brenda
Reshetnikov, A.; Solntseva, N.; Rozova, O.; Mustakhimov, I.; Trotsenko, Y.; Khmelenina, V.
ATP-and polyphosphate-dependent glucokinases from aerobic methanotrophs
Microorganisms
7
52
2019
Methylomonas methanica (A0A3G4RI75), Methylomonas methanica 12 (A0A3G4RI75)
brenda
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