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Enzyme Nomenclature
Information on EC 2.7.1.12 - gluconokinase
for references in articles please use BRENDA:EC2.7.1.12
Word Map on EC 2.7.1.12
- 2.7.1.12
- 6-phosphogluconate
-
entner-doudoroff
- pentose
- glucokinase
-
thermoresistant
-
embden-meyerhof
-
subsidiary
- 2-ketogluconate
-
gntii
- nutrition
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.7.1.12
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RECOMMENDED NAME
GeneOntology No.
gluconokinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-gluconate 6-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9030-55-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
physiological function
metabolism
-
phosphogluconate pathway, bacterial enzyme is active in young, non-inoculated mesquite seedlings growing under hydroponic conditions
metabolism
-
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
-
when azospirillum brasilense Cd bacteria are inoculated on the root system, the roots exhibit much higher activity of gluconokinase
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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
ATP + myelin basic protein kinase
ADP + phosphorylated myelin basic protein kinase
-
-
-
?
ITP + D-gluconate
IDP + 6-phospho-D-gluconate
-
60% of the activity with ATP
-
-
?
additional information
?
-
-
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
-
-
-
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
-
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
Escherichia coli B / ATCC 11303
-
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
-
strict specificity for D-gluconate
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
conversion of glucose to pyruvate
-
-
?
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
-
strict specificity for D-gluconate
-
-
?
GTP + D-gluconate
GDP + 6-phospho-D-gluconate
-
25% of the activity with ATP
-
-
?
UTP + D-gluconate
UDP + 6-phospho-D-gluconate
-
130% of the activity with ATP
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-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
-
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
Escherichia coli B / ATCC 11303
-
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
-
conversion of glucose to pyruvate
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
enzyme probably acts as a key enzyme in regulating glucose oxidation in the liver of fish
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
activates; inhibition above; Km: 1.68 mM; optimum concentration: 5-7 mM
Mg2+
-
activates; at each level of ATP the optimal molar concentration of Mg2+ is one-half that of ATP, higher concentration inhibits
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
-
at each level of ATP the optimal molar concentration of Mg2+ is one-half that of ATP, higher concentration inhibits
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activated His-tagged Cdc42Hs
stimulates mPAK-3 autophosphorylation and phosphorylation of myelin basic protein by mPAK-3 in vitro
-
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
30°C, 0.34-4.1 mM with D-gluconate as substrate, depending on organism
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additional information
additional information
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30°C, 0.34-4.1 mM with D-gluconate as substrate, depending on organism
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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
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additional information
additional information
-
method for quantification of D-gluconate by use of immobilized enzyme
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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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
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
-
35.1 microliter of CO2 per h per mg of protein
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1 - 8.4
-
pH 5.1: about 25% of activity maximum, pH 8.4: about 50% of activity maximum
5.4 - 6.8
6 - 9
-
pH 6: about 30% of activity maximum, pH 9: about 40% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM);
Q5FM28
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM);
Q5FM28
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
glucokinase is induced upon exposure to gluconic acid
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
method for quantification of D-gluconate in honeys, vinegars and noble rot wines by use of immobilized enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.12)
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