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Information on EC 2.7.1.12 - gluconokinase for references in articles please use BRENDA:EC2.7.1.12Word Map on EC 2.7.1.12
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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ATP + D-gluconate = ADP + 6-phospho-D-gluconate
ATP + D-gluconate = ADP + 6-phospho-D-gluconate
sequential probably random mechanism
-
ATP + D-gluconate = ADP + 6-phospho-D-gluconate
reaction follows a ternary complex mechanism, with ATP binding first
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ATP + D-gluconate = ADP + 6-phospho-D-gluconate
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phospho group transfer
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D-gluconate degradation
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L-idonate degradation
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sorbitol biosynthesis II
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ketogluconate metabolism
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Pentose phosphate pathway
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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ATP:D-gluconate 6-phosphotransferase
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gluconokinase (phosphorylating)
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-
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serine/threonine-protein kinase PAK 2
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serine/threonine-protein kinase PAK 3
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gluconate kinase
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gluconokinase
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gntK
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gene name
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eel
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Cd
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-
brenda
Cd
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-
brenda
carp
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-
brenda
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-
brenda
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SwissProt
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-
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-
brenda
rainbow trout
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brenda
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SwissProt
brenda
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-
-
brenda
-
-
-
brenda
baker's yeast and brewer's yeast
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brenda
yellowtail
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brenda
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brenda
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-
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brenda
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UniProt
brenda
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brenda
-
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-
brenda
K-12
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brenda
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UniProt
brenda
isoform 1; isoform 2
UniProt
brenda
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malfunction
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inactivation of the gluconate kinase gene leads to a 51.8% increase in intracellular NADPH concentration, which results in a 49.9% increase in L-ornithine production
metabolism
pentose phosphate pathway
metabolism
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phosphogluconate pathway, bacterial enzyme is active in young, non-inoculated mesquite seedlings growing under hydroponic conditions
metabolism
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phosphogluconate pathway, bacterial enzyme is active in young, non-inoculated mesquite seedlings growing under hydroponic conditions
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physiological function
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when azospirillum brasilense Cd bacteria are inoculated on the root system, the roots exhibit much higher activity of gluconokinase
physiological function
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when azospirillum brasilense Cd bacteria are inoculated on the root system, the roots exhibit much higher activity of gluconokinase
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ATP + D-gluconate
ADP + 6-phospho-D-gluconate
ATP + D-glucono-1,5-lactone
ADP + 6-phospho-D-glucono-1,5-lactone
-
-
-
-
?
ATP + myelin basic protein kinase
ADP + phosphorylated myelin basic protein kinase
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-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
CTP + D-gluconate
CDP + 6-phospho-D-gluconate
-
-
-
-
?
D-gluconate + ATP
6-phospho-D-gluconate + ADP
GTP + D-gluconate
GDP + 6-phospho-D-gluconate
ITP + D-gluconate
IDP + 6-phospho-D-gluconate
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60% of the activity with ATP
-
-
?
UTP + D-gluconate
UDP + 6-phospho-D-gluconate
additional information
?
-
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no substrates: D-glucose, D-galactose, D-fructose, D-mannose and D-glucosamine, D-ribose, D-ribulose, D-arabinose, D-xylulose, D-xylose and D-erythrose
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-
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ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme of the oxidative pathway in glucose-grown bacteria
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme of the oxidative pathway in glucose-grown bacteria
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
-
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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strict specificity for D-gluconate
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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and ATP
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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conversion of glucose to pyruvate
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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strict specificity for D-gluconate
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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-
-
-
?
D-gluconate + ATP
6-phospho-D-gluconate + ADP
-
-
-
-
?
D-gluconate + ATP
6-phospho-D-gluconate + ADP
-
-
-
-
?
D-gluconate + ATP
6-phospho-D-gluconate + ADP
-
-
-
?
GTP + D-gluconate
GDP + 6-phospho-D-gluconate
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-
-
-
?
GTP + D-gluconate
GDP + 6-phospho-D-gluconate
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25% of the activity with ATP
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-
?
UTP + D-gluconate
UDP + 6-phospho-D-gluconate
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-
-
-
?
UTP + D-gluconate
UDP + 6-phospho-D-gluconate
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130% of the activity with ATP
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-
?
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ATP + D-gluconate
ADP + 6-phospho-D-gluconate
D-gluconate + ATP
6-phospho-D-gluconate + ADP
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme of the oxidative pathway in glucose-grown bacteria
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme of the oxidative pathway in glucose-grown bacteria
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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-
-
-
-
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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-
-
-
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ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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conversion of glucose to pyruvate
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-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
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-
-
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D-gluconate + ATP
6-phospho-D-gluconate + ADP
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-
-
-
?
D-gluconate + ATP
6-phospho-D-gluconate + ADP
-
-
-
-
?
D-gluconate + ATP
6-phospho-D-gluconate + ADP
Q8NMT0
-
-
-
?
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Ca2+
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can partially replace Mg2+ in activation
Co2+
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can partially replace Mg2+ in activation
MgCl2
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10 mM are included in assay medium
Zn2+
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can partially replace Mg2+ in activation
Mg2+
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activates
Mg2+
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required, maximal activation at a Mg2+ : ATP ratio of 1.0-2.0
Mg2+
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activates; inhibition above; Km: 1.68 mM; optimum concentration: 5-7 mM
Mg2+
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activates; at each level of ATP the optimal molar concentration of Mg2+ is one-half that of ATP, higher concentration inhibits
Mn2+
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60% as effective as Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
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D-gluconate
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binds to an enzyme-ADP complex forming a dead-end complex
p-chloromercuribenzoate
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additional information
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not: iodoacetate
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Mg2+
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optimal activation at 5-7 mM, inhibition above
Mg2+
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at each level of ATP the optimal molar concentration of Mg2+ is one-half that of ATP, higher concentration inhibits
NaF
-
-
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activated His-tagged Cdc42Hs
stimulates mPAK-3 autophosphorylation and phosphorylation of myelin basic protein by mPAK-3 in vitro
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gluconate
6-phosphogluconate dehydrogenase, although constituvely expressed, shows a 3fold higher specific level in gluconate grown cells than those grown in fructose under similar conditions
gluconic acid
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gluconokinase is induced upon exposure to gluconic acid
His-tagged Rac
stimulates mPAK-3 autophosphorylation and phosphorylation of myelin basic protein by mPAK-3 in vitro
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additional information
additional information
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0.045
ATP
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-
0.344
ATP
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pH 7.2, temperature not specified in the publication
0.02
D-gluconate
-
-
0.042
D-gluconate
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25°C, pH 7
0.106
D-gluconate
-
pH 7.2, temperature not specified in the publication
0.212
D-gluconate
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25°C, pH 8, gene gntU
1.74
D-gluconate
-
30°C, pH 7.6
additional information
additional information
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30°C, 0.34-4.1 mM with D-gluconate as substrate, depending on organism
-
additional information
additional information
-
30°C, 0.34-4.1 mM with D-gluconate as substrate, depending on organism
-
additional information
additional information
-
30°C, 0.34-4.1 mM with D-gluconate as substrate, depending on organism
-
additional information
additional information
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30°C, 0.34-4.1 mM with D-gluconate as substrate, depending on organism
-
additional information
additional information
-
method for quantification of D-gluconate by use of immobilized enzyme
-
additional information
additional information
-
isothermal titration calorimetry to determine kinetic and thermodynamic properties. The KM for ATP lies in the range 0.1 to 0.3 mM at varying concentrations of Glcn. The KM of D-glucuronate is in the range 0.2 to 0.3 mM, pH 7.2, 25°C
-
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9.5
ATP
-
pH 7.2, temperature not specified in the publication
9.3
D-gluconate
-
pH 7.2, temperature not specified in the publication
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28
ATP
-
pH 7.2, temperature not specified in the publication
89
D-gluconate
-
pH 7.2, temperature not specified in the publication
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0.00035
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strain TUG287(pTC222)
0.00621
-
strain TUG287(pTC223)
0.047
activity of glucokinase in Corynebacterium glutamicum (ATCC 13032) culture in MCGC medium at 37°C, supplemented with 0.5% gluconate
0.388
activity of glucokinase expressed in Escherichia strain M1-8, supplemented with fructose as carbon source
0.6725
-
strain TUG287(pTC220)
1.429
transformed Escherichia coli cells (strain DH5alpha carrying the pTAEK plasmid), grown in Lb and collected during the exponential phase, then cultivated in CAA medium with 0.2% fructose as carbon source
2.894
transformed Escherichia coli cells (mutant TGN282 carrying the pTAEK plasmid), grown in Lb and collected during the exponential phase, then cultivated in CAA medium with 0.2% fructose as carbon source
250
-
thermoresistant gluconokinase encoded by th gntK
additional information
-
at six concentrations (4.6-90.6 mM) of gluconate added to culture medium for Azospirillum brasilense Cd grown in TYG medium, activity of gluconokinase activity is positively affected; gluconokinase activity significantly increases in inoculated mesquite plants incubated for 23 days, inoculation is not enhanced after 15 days of incubation; while increased gluconokinase activity results only in inoculated treatments, older non-inoculated seedlings maintained the same activity as younger seedlings and the sum of activities of the roots and the negative control is still lower than activity in inoculated plants
additional information
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35.1 microliter of CO2 per h per mg of protein
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6
-
-
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5.1 - 8.4
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pH 5.1: about 25% of activity maximum, pH 8.4: about 50% of activity maximum
6 - 9
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pH 6: about 30% of activity maximum, pH 9: about 40% of activity maximum
5.4 - 6.8
-
about 50% of activity maximum at pH 5.4 and 6.8
5.4 - 6.8
-
about 50% of activity maximum at pH 5.4 and 6.8
5.4 - 6.8
-
about 50% of activity maximum at pH 5.4 and 6.8
5.4 - 6.8
-
about 50% of activity maximum at pH 5.4 and 6.8
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45
-
thermoresistant gluconokinase encoded by th gntK
37
-
assay at
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brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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Escherichia coli (strain K12);
A3TPB6
Janibacter sp. HTCC2649;
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM);
Q92VK3
Rhizobium meliloti (strain 1021);
P46859
Escherichia coli (strain K12);
P46859
Escherichia coli (strain K12);
P46859
Escherichia coli (strain K12);
P46859
Escherichia coli (strain K12);
P46859
Escherichia coli (strain K12);
P46859
Escherichia coli (strain K12);
Q5FM28
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM);
Q5FM28
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM);
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18400
-
2 * 18400, SDS-PAGE
29500
-
alpha3, 3 * 29500
18000
-
-
18000
predicted from 167 amino acids of gluconate kinase
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dimer
-
and tetramer, 2 * 23326, calculated, 2 * 21800, SDS-PAGE
tetramer
-
and dimer, 4 * 23326, calculated, 4 * 21800, SDS-PAGE
trimer
-
alpha3, 3 * 29500
homodimer
-
2 * 18400, SDS-PAGE
homodimer
-
crystallization studies
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phosphoprotein
autophosphorylation
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hanging-drop vapour-diffusion method with polyethylene glycol 6000 and lithium chloride as precipitants, three crystal forms obtained, space group C2 with a : 75, b : 79.3, c : 70.2 A and beta : 105.3°, space group P212121 with a : 52, b : 79.3, c : 89.8 A and space group P21212 with a : 70.1, b : 74.1 and c : 78.9 A
-
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50
-
after 40 min, 50% loss of activity
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-15°C, 10% loss of activity after 3 weeks
-
3°C, 50% loss of activity after 3 weeks
-
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baker's yeast and brewer's yeast
-
-
-
partial
-
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expressed in in human HeLa cell lysates
expression in Escherichia coli
-
expression in Escherichia coli Hfr6GDELTAMD2, TUG287 and M6
-
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glucokinase is induced upon exposure to gluconic acid
glucokinase is induced upon exposure to gluconic acid
-
glucokinase is induced upon exposure to gluconic acid
-
-
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nutrition
-
method for quantification of D-gluconate in honeys, vinegars and noble rot wines by use of immobilized enzyme
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Diabetes Mellitus
Mice mutant for glucokinase regulatory protein exhibit decreased liver glucokinase: a sequestration mechanism in metabolic regulation.
Neoplasms
Inferring the metabolism of human orphan metabolites from their metabolic network context affirms human gluconokinase activity.
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Jakobi, R.; Chen, C.J.; Tuazon, P.T.; Traugh, J.A.
Molecular cloning and sequencing of the cytostatic G protein-activated protein kinase PAK I
J. Biol. Chem.
271
6206-6211
1996
Oryctolagus cuniculus (Q29502)
brenda
Bagrodia, S.; Taylor, S.J.; Creasy, C.L.; Chernoff, J.; Cerione, R.A.
Identification of a mouse p21Cdc42/Rac activated kinase
J. Biol. Chem.
270
22731-22737
1995
Mus musculus (Q61036)
brenda
Zachariou, M.; Scopes, R.K.
Gluconate kinase from Zymomonas mobilis: isolation and characteristics
Biochem. Int.
10
367-371
1985
Zymomonas mobilis
brenda
Nagayama, F.; Suzuki, H.; Oshima, T.
Gluconokinase of fish liver
Nippon Suisan Gakkaishi
46
783
1980
Anguilla japonica, Cyprinus carpio, Oncorhynchus mykiss, Seriola quinqueradiata
-
brenda
Szymona, M.; Kowalska, H.
ATP: D-gluconate 6-phosphotransferase of Mycobacterium phlei
Ann. Univ. Mariae Curie Sklodowska Med.
25
371-381
1970
Mycobacterium phlei
brenda
Cohen, S.S.
Gluconokinase and the oxidative path of glucose-6-phosphate utilization
J. Biol. Chem.
189
617-628
1951
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Sable, H.Z.; Guarino, A.J.
Phosphorylation of gluconate in yeast extracts
J. Biol. Chem.
196
395-402
1952
Saccharomyces cerevisiae
brenda
Narrod, S.A.; Wood, W.A.
Carbohydrate oxidation by pseudomonas fluorescens. V. Evidence for gluconokinase and 2-ketogluconokinase
J. Biol. Chem.
220
45-55
1956
Pseudomonas fluorescens
brenda
Leder, I.G.
Hog kidney gluconokinase
J. Biol. Chem.
225
125-136
1957
Sus scrofa
brenda
Coffee, C.J.; Hu, A.S.L.
The kinetic characterization of gluconokinase from a pseudomonad
Arch. Biochem. Biophys.
149
549-559
1972
Pseudomonas sp.
brenda
Tong, S.; Porco, A.; Isturiz, T.; Conway, T.
Cloning and molecular genetic characterization of the Escherichia coli gntR, gntK, and gntU genes of GntI, the main system for gluconate metabolism
J. Bacteriol.
178
3260-3269
1996
Escherichia coli
brenda
Izu, H.; Adachi, O.; Yamada, M.
Purification and characterization of the Escherichia coli thermoresistant glucokinase encoded by the gntK gene
FEBS Lett.
394
14-16
1996
Escherichia coli
brenda
Kraft, L.; Sprenger, G.A.; Lindqvist, Y.
Crystallization and preliminary X-ray crystallographic studies of recombinant thermoresistant gluconate kinase GntK from Escherichia coli
Acta Crystallogr. Sect. D
57
1159-1161
2001
Escherichia coli
brenda
Kraft, L.; Sprenger, G.A.; Lindqvist, Y.
Conformational changes during the catalytic cycle of gluconate kinase as revealed by X-ray crystallography
J. Mol. Biol.
318
1057-1069
2002
Escherichia coli
brenda
Tsukatani, T.; Matsumoto, K.
Fluorometric quantification of total D-gluconate by a flow-injection system using an immobilized-enzyme reactor
Anal. Chim. Acta
530
221-225
2005
Escherichia coli
-
brenda
Porco, A.; Gamero, E.E.; Mylonas, E.; Isturiz, T.
Gluconate as suitable potential reduction supplier in Corynebacterium glutamicum: cloning and expression of gntP and gntK in Escherichia coli
Biol. Res.
41
349-358
2008
Corynebacterium glutamicum, Corynebacterium glutamicum (Q8NMT0)
brenda
Leyva, L.A.; Bashan, Y.
Activity of two catabolic enzymes of the phosphogluconate pathway in mesquite roots inoculated with Azospirillum brasilense Cd
Plant Physiol. Biochem.
46
898-904
2008
Azospirillum brasilense, Azospirillum brasilense Cd
brenda
Rolfsson, O.; Paglia, G.; Magnusdottir, M.; Palsson, B.O.; Thiele, I.
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