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Information on EC 2.7.1.12 - gluconokinase
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EC Tree
2.7.1.12 gluconokinaseSpecify your search results
Word Map
- 2.7.1.12
- 6-phosphogluconate
-
entner-doudoroff
- glucokinase
-
thermoresistant
-
embden-meyerhof
-
subsidiary
- gntii
- 2-ketogluconate
- nutrition
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gluconate kinase, gluconokinase, c9orf103, idn1 gluconate kinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
gluconate kinase
gluconokinase
gluconokinase (phosphorylating)
-
-
-
-
gntK
Idn1 gluconate kinase
gluconate kinase
-
-
-
-
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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
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 SOURCE
PATHWAYS
BRENDA
KEGG
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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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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 + D-glucono-1,5-lactone
ADP + 6-phospho-D-glucono-1,5-lactone
-
-
-
?
ITP + D-gluconate
IDP + 6-phospho-D-gluconate
-
60% of the activity with ATP
-
-
?
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
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
-
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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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-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
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
-
-
?
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+
-
at each level of ATP the optimal molar concentration of Mg2+ is one-half that of ATP, higher concentration inhibits
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INHIBITOR
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
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
-
gluconokinase is induced upon exposure to gluconic acid
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Gluconokinase IDNK Promotes Cell Proliferation and Inhibits Apoptosis in Hepatocellular Carcinoma.
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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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
-
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
-
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
-
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
additional information
-
gluconokinase activity significantly increases in inoculated mesquite plants incubated for 23 days, inoculation is not enhanced after 15 days of incubation
additional information
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the strain is lacking the zinc-responsive transcriptional repressor Loz1 with the goal of identifying metabolic pathways that are altered by cellular zinc status
SwissProt
brenda
the strain is lacking the zinc-responsive transcriptional repressor Loz1 with the goal of identifying metabolic pathways that are altered by cellular zinc status
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
gluconokinase IDNK plays a key role in the proliferation and apoptosis of HCC cells. It may be a candidate therapeutic target for hepatocellular carcinoma
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
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
metabolism
-
phosphogluconate pathway, bacterial enzyme is active in young, non-inoculated mesquite seedlings growing under hydroponic conditions
-
metabolism
-
6-phosphogluconate dehydrogenase (Gcd1) and gluconate kinase (Idn1) act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase
-
physiological function
-
when azospirillum brasilense Cd bacteria are inoculated on the root system, the roots exhibit much higher activity of gluconokinase
physiological function
gluconokinase IDNK promotes cell proliferation and inhibits apoptosis in hepatocellular carcinoma
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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PDB
SCOP
CATH
UNIPROT
ORGANISM