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Information on EC 2.7.1.13 - dehydrogluconokinase
for references in articles please use BRENDA:EC2.7.1.13
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.13 dehydrogluconokinase
The enzyme appears in viruses and cellular organisms
showSynonyms
ketogluconokinase, 2-ketogluconokinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-ketogluconate kinase
2-ketogluconokinase
-
-
-
-
ketogluconokinase
-
-
-
-
ketogluconokinase (phosphorylating)
-
-
-
-
kinase, ketoglucono-(phosphorylating)
-
-
-
-
2-ketogluconate kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 2-dehydro-D-gluconate = ADP + 6-phospho-2-dehydro-D-gluconate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
glucose degradation (oxidative)
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SYSTEMATIC NAME
IUBMB Comments
ATP:2-dehydro-D-gluconate 6-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9030-56-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-dehydro-D-gulonate
ADP + 6-phospho-2-dehydro-D-gulonate
Substrates: -
Products: -
Products: -
r
ATP + 2-keto-3-deoxy-D-gluconate
ADP + ?
Substrates: -
Products: -
Products: -
?
ATP + 2-keto-3-deoxy-D-gulonate
ADP + ?
Substrates: -
Products: -
Products: -
?
ATP + 2-dehydro-D-gluconate
ADP + 2-dehydro-6-phosphogluconate
-
Substrates: i.e. 2-dehydro-D-gluconate
Products: -
Products: -
?
ATP + 2-dehydro-D-gluconate
ADP + 2-dehydro-6-phosphogluconate
-
Substrates: i.e. 2-dehydro-D-gluconate
Products: i.e. 6-phospho-2-dehydro-D-gluconate
Products: i.e. 6-phospho-2-dehydro-D-gluconate
?
ATP + 2-dehydro-D-gluconate
ADP + 2-dehydro-6-phosphogluconate
-
Substrates: -
Products: -
Products: -
?
ATP + 2-dehydro-D-gluconate
ADP + 2-dehydro-6-phosphogluconate
-
Substrates: part of the 2-ketogluconate utilization operon
Products: -
Products: -
?
ATP + 2-dehydro-D-gluconate
ADP + 6-phospho-2-dehydro-D-gluconate
Substrates: -
Products: -
Products: -
?, r
ATP + 2-dehydro-D-gluconate
ADP + 6-phospho-2-dehydro-D-gluconate
-
Substrates: -
Products: -
Products: -
r
ATP + 2-dehydro-D-gluconate
ADP + 6-phospho-2-dehydro-D-gluconate
Substrates: preferred substrate
Products: -
Products: -
r
additional information
?
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Substrates: the substrate specificity analysis reveals that three ketoacids (2-dehydro-3-deoxy-D-gluconate, 2-dehydro-D-gulonate, and 2-dehydro-3-deoxy-D-gulonate) with structures close to the natural substrate (2-dehydro-D-gluconate) are successfully phosphorylated at an efficiency lower than or comparable to 2-dehydrogluconate, as depicted by the measured kinetic constant values. Assay method optimization, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: the substrate specificity analysis reveals that three ketoacids (2-dehydro-3-deoxy-D-gluconate, 2-dehydro-D-gulonate, and 2-dehydro-3-deoxy-D-gulonate) with structures close to the natural substrate (2-dehydro-D-gluconate) are successfully phosphorylated at an efficiency lower than or comparable to 2-dehydrogluconate, as depicted by the measured kinetic constant values. Assay method optimization, overview
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-dehydro-D-gluconate
ADP + 2-dehydro-6-phosphogluconate
-
Substrates: part of the 2-ketogluconate utilization operon
Products: -
Products: -
?
ATP + 2-dehydro-D-gluconate
ADP + 6-phospho-2-dehydro-D-gluconate
Substrates: -
Products: -
Products: -
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
2-keto-3-deoxy-D-gluconate
pH 8.0, temperature not specified in the publication
25
2-keto-3-deoxy-D-gulonate
pH 8.0, temperature not specified in the publication
-
4
2-keto-D-gulonate
pH 8.0, temperature not specified in the publication
0.35
2-dehydro-D-gluconate
pH 8.0, temperature not specified in the publication
additional information
additional information
steady-state kinetics of the recombinant enzyme
-
additional information
additional information
-
steady-state kinetics of the recombinant enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.8
2-dehydro-D-gluconate
pH 8.0, temperature not specified in the publication
10.2
2-keto-3-deoxy-D-gluconate
pH 8.0, temperature not specified in the publication
2.1
2-keto-3-deoxy-D-gulonate
pH 8.0, temperature not specified in the publication
-
1.1
2-keto-D-gulonate
pH 8.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.77
2-dehydro-D-gluconate
pH 8.0, temperature not specified in the publication
7.37
2-keto-3-deoxy-D-gluconate
pH 8.0, temperature not specified in the publication
0.083
2-keto-3-deoxy-D-gulonate
pH 8.0, temperature not specified in the publication
-
0.246
2-keto-D-gulonate
pH 8.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
H16, also known as Alcaligenes eutrophus, enzyme is induced during growth on 2-ketogluconate
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
2-ketogluconate kinase (KGUK) is involved in the glucose and 2-ketogluconate catabolism of several aerobic bacteria, but relatively few bacterial species are able to utilize 2-ketogluconate as the sole carbon source for growth and energy provision
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A085G079_9ENTR
312
0
33022
TrEMBL
-
F8GQN3_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
314
0
33413
TrEMBL
-
A0A1B7JWG1_9GAMM
326
0
35584
TrEMBL
-
E5AU47_MYCRK
Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
318
0
33966
TrEMBL
-
Q88HH9_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
316
0
33615
TrEMBL
-
A0A085G4K4_9GAMM
318
0
33579
TrEMBL
-
A0A3G7JGR9_9PSED
328
0
35171
TrEMBL
-
A0A198GX28_9ENTR
312
0
32973
TrEMBL
-
Q0K080_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
314
0
33563
TrEMBL
-
H3RIK8_PANSE
317
0
34224
TrEMBL
-
A0A1B7IHL1_9ENTR
312
0
32991
TrEMBL
-
A0A1B7HJQ2_9ENTR
312
0
32958
TrEMBL
-
A0A1B7I0Y2_9ENTR
312
0
32968
TrEMBL
-
A0A3G7BKL3_9PSED
328
0
35260
TrEMBL
-
A0A085A2S5_9ENTR
313
0
33421
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stabilized by storage in an imidazole solution which is removed just before use
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography and desalting gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene kguK, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) pLysS
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Frampton, E.W.; Wood, W.A.
Purification and properties of 2-ketogluconokinase from Aerobacter aerogenes
J. Biol. Chem.
236
2578-2580
1961
Klebsiella aerogenes
brenda
Nandadasa, H.G.; Andreesen, M.; Schlegel, H.G.
The utilization of 2-ketogluconate by Hydrogenomonas eutropha H 16
Arch. Microbiol.
99
15-23
1974
Cupriavidus necator
brenda
Swanson, B.L.; Hager, P.; Phibbs, P.Jr.; Ochsner, U.; Vasil, M.L.; Hamood, A.N.
Characterization of the 2-ketogluconate utilization operon in Pseudomonas aeruginosa PAO1
Mol. Microbiol.
37
561-573
2000
Pseudomonas aeruginosa
brenda
Sanchez-Moreno, I.; Trachtmann, N.; Ilhan, S.; Helaine, V.; Lemaire, M.; Guerard-Helaine, C.; Sprenger, G.A.
2-Ketogluconate kinase from Cupriavidusnecator H16 purification, characterization, and exploration of its substrate specificity
Molecules
24
2393
2019
Cupriavidus necator (Q0K080), Cupriavidus necator
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.13)
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Release 2023.1 (January 2023)
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