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Information on EC 2.7.1.12 - gluconokinase
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2.7.1.12 gluconokinaseSpecify your search results
Word Map
- 2.7.1.12
- 6-phosphogluconate
-
entner-doudoroff
-
thermoresistant
-
embden-meyerhof
-
gntii
-
subsidiary
- 2-ketogluconate
- nutrition
The enzyme appears in viruses and cellular organisms
Synonyms
C9orf103, C9orf103 isoform I, C9orf103 isoform II, gluconate kinase, gluconokinase, gluconokinase (phosphorylating), gntK, IdnK, serine/threonine-protein kinase PAK 2, serine/threonine-protein kinase PAK 3, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
gluconate kinase
gluconokinase
gluconokinase (phosphorylating)
-
-
-
-
gntK
gluconate kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + D-gluconate = ADP + 6-phospho-D-gluconate
-
-
-
-
ATP + D-gluconate = ADP + 6-phospho-D-gluconate
sequential probably random mechanism
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ATP + D-gluconate = ADP + 6-phospho-D-gluconate
reaction follows a ternary complex mechanism, with ATP binding first
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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 + myelin basic protein kinase
ADP + phosphorylated myelin basic protein kinase
-
-
-
?
ITP + D-gluconate
IDP + 6-phospho-D-gluconate
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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
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enzyme of the oxidative pathway in glucose-grown bacteria
-
-
?
ATP + D-gluconate
ADP + 6-phospho-D-gluconate
Escherichia coli B / ATCC 11303
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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
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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 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
-
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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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
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
-
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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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
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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
-
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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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
physiological function
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
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SUBUNIT
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Mycolicibacterium 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.
Inferring the metabolism of human orphan metabolites from their metabolic network context affirms human gluconokinase activity
Biochem. J.
449
427-435
2013
Homo sapiens, Homo sapiens (Q5T6J7)
brenda
Hwang, G.H.; Cho, J.Y.
Implication of gluconate kinase activity in L-ornithine biosynthesis in Corynebacterium glutamicum
J. Ind. Microbiol. Biotechnol.
39
1869-1874
2012
Corynebacterium glutamicum
brenda
Rohatgi, N.; Gudmundsson, S.; Rolfsson, O.
Kinetic analysis of gluconate phosphorylation by human gluconokinase using isothermal titration calorimetry
FEBS Lett.
589
3548-3555
2015
Homo sapiens, Homo sapiens (Q5T6J7)
brenda
Rohatgi, N.; Nielsen, T.; Bjorn, S.; Axelsson, I.; Paglia, G.; Voldborg, B.; Palsson, B.; Rolfsson, O.
Biochemical characterization of human gluconokinase and the proposed metabolic impact of gluconic acid as determined by constraint based metabolic network analysis
PLoS ONE
9
e98760
2014
Homo sapiens, Homo sapiens (Q5T6J7)
brenda
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