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ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
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ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
active site structure, substrate binding structure involving amino acid residues L11, G34, A35, N38, Y89, Y103, R105, I134, R167, V247, E251, and E287, 2-dehydro-3-deoxy-D-gluconate is recognized as an open chain structure, catalytic mechanism, Arg167 and Asp251 play a role in transferring the gamma-phosphate of ATP to the 5'-hydroxyl group of 2-dehydro-3-deoxy-D-gluconate
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ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
reaction is initiated by the deprotonation of the hydroxyl group of the substrate by the catalytic base Asp280. A nucleophilic attack on the gamma-phosphate of ATP by the negatively charged hydroxyl group generates the transition state intermediate
ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
active site structure, substrate binding structure involving amino acid residues L11, G34, A35, N38, Y89, Y103, R105, I134, R167, V247, E251, and E287, 2-dehydro-3-deoxy-D-gluconate is recognized as an open chain structure, catalytic mechanism, Arg167 and Asp251 play a role in transferring the gamma-phosphate of ATP to the 5'-hydroxyl group of 2-dehydro-3-deoxy-D-gluconate
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ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
ATP + 2-keto-D-gluconate
ADP + 6-phospho-2-keto-D-gluconate
CTP + 2-dehydro-3-deoxy-D-gluconate
CDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
GTP + 2-dehydro-3-deoxy-D-gluconate
GDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
ITP + 2-dehydro-3-deoxy-D-gluconate
IDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
TTP + 2-dehydro-3-deoxy-D-gluconate
TDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
UTP + 2-dehydro-3-deoxy-D-gluconate
UDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
additional information
?
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ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
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r
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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enzyme is induced by galacturonate or glucuronate and is controlled by a single structural gene
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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preferred substrate, binding mechanism and structure, overview
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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preferred substrate, binding mechanism and structure, overview
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?
ATP + 2-keto-D-gluconate
ADP + 6-phospho-2-keto-D-gluconate
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ATP + 2-keto-D-gluconate
ADP + 6-phospho-2-keto-D-gluconate
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ATP + 2-keto-D-gluconate
ADP + 6-phospho-2-keto-D-gluconate
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?
CTP + 2-dehydro-3-deoxy-D-gluconate
CDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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8% of the activity with ATP
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?
CTP + 2-dehydro-3-deoxy-D-gluconate
CDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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8% of the activity with ATP
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?
GTP + 2-dehydro-3-deoxy-D-gluconate
GDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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34% of the activity with ATP
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?
GTP + 2-dehydro-3-deoxy-D-gluconate
GDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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34% of the activity with ATP
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?
GTP + 2-dehydro-3-deoxy-D-gluconate
GDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
94% activity compared to the substrate combination with ATP
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GTP + 2-dehydro-3-deoxy-D-gluconate
GDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
94% of the activity with ATP
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ITP + 2-dehydro-3-deoxy-D-gluconate
IDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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75% of the activity with ATP
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?
ITP + 2-dehydro-3-deoxy-D-gluconate
IDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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75% of the activity with ATP
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?
ITP + 2-dehydro-3-deoxy-D-gluconate
IDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
66% activity compared to the substrate combination with ATP
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?
ITP + 2-dehydro-3-deoxy-D-gluconate
IDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
66% of the activity with ATP
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TTP + 2-dehydro-3-deoxy-D-gluconate
TDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
43% activity compared to the substrate combination with ATP
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TTP + 2-dehydro-3-deoxy-D-gluconate
TDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
43% of the activity with ATP
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?
UTP + 2-dehydro-3-deoxy-D-gluconate
UDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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7% of the activity with ATP
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?
UTP + 2-dehydro-3-deoxy-D-gluconate
UDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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7% of the activity with ATP
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?
additional information
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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
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additional information
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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
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additional information
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no substrate: 2-deoxy-D-ribose, 2-deoxy-D-glucose, D-gluconate, 2-keto-D-gluconate, 2-oxoglutarate, 2-oxo-3-deoxy-6-phosphogluconate
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additional information
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thin-layer chromatography (TLC) and mass spectrometric analyses of reaction products of recombinant FlKin
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additional information
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does not accept ADP or AMP as phosphoryl donors
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additional information
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does not accept ADP or AMP as phosphoryl donors
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additional information
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no substrate: UTP, CTP, ADP, GDP, IDP, UDP, CDP, and AMP, D-glucose, D-fructose, and 2-keto-3-deoxyoctonate
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?
additional information
?
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no substrate: UTP, CTP, ADP, GDP, IDP, UDP, CDP, and AMP, D-glucose, D-fructose, and 2-keto-3-deoxyoctonate
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?
additional information
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D-gluconate, 2-keto-D-gluconate, 5-keto-D-gluconate, N-acetylglucosamine, and D-xylose are no substrates
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additional information
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enzyme shows high substrate specificity, no activity with glucose, fructose, ribose, xylitol, gluconate, and gluconic acid lactone
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additional information
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enzyme shows high substrate specificity, no activity with glucose, fructose, ribose, xylitol, gluconate, and gluconic acid lactone
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evolution
2-keto-3-deoxy-D-gluconate (KDG) kinase and 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase genes, i.e., flkin and flald, are encoded in the assimilating gene cluster in the genome of Flavobacterium sp. strain UMI-01, a member of Bacteroidetes. The amino acid sequences deduced from flkin and flald show low identities with those of corresponding enzymes of Saccharophagus degradans strain 2-40T, a member of Proteobacteria
malfunction
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deletion of the semiphosphorylative Entner-Doudoroff pathway key enzyme 2-keto-3-deoxygluconate kinase in Sulfolobus solfataricus PBL2025 results in a similar growth phenotype on glucose as substrate compared with the wild-type. In contrast, the mutant shows strongly increased concentrations of nonphosphorylative-Entner-Doudoroff intermediates whereas the hexose and pentose phosphates as well as trehalose are decreased. The results indicate (a) that the nonphosphorylative pathway is able to compensate for the missing semiphosphorylative Entner-Doudoroff branch in glucose catabolism, (b) that in addition to its catabolic function the semiphosphorylative Entner-Doudoroff pathway has an additional although not essential role in providing sugar phosphates for anabolism/gluconeogenesis and (c) that glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway
malfunction
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deletion of the semiphosphorylative Entner-Doudoroff pathway key enzyme 2-keto-3-deoxygluconate kinase in Sulfolobus solfataricus PBL2025 results in a similar growth phenotype on glucose as substrate compared with the wild-type. In contrast, the mutant shows strongly increased concentrations of nonphosphorylative-Entner-Doudoroff intermediates whereas the hexose and pentose phosphates as well as trehalose are decreased. The results indicate (a) that the nonphosphorylative pathway is able to compensate for the missing semiphosphorylative Entner-Doudoroff branch in glucose catabolism, (b) that in addition to its catabolic function the semiphosphorylative Entner-Doudoroff pathway has an additional although not essential role in providing sugar phosphates for anabolism/gluconeogenesis and (c) that glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway
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metabolism
the enzyme occupies a central position in the pectin, galacturonate, and xylan catabolic pathways
metabolism
the enzyme is active in alginate degradation. Unsaturated monosaccharide, the end product of alginate lyases, is spontaneously and/or enzymatically converted to an open chain form, DEH, and further converted to 2-keto-3-deoxy-D-gluconate (KDG) by the NAD(P)H-dependent DEH reductase. The KDG is phosphorylated to KDPG by KDG kinase and then split to pyruvate and glyceraldehyde-3-phosphate (GAP) by KDPG aldolase. The alginate-derived pyruvate and GAP are finally metabolized by Kreb's cycle. Alginate-metabolic system of Flavobacterium sp. strain UMI-01, overview
metabolism
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the enzyme occupies a central position in the pectin, galacturonate, and xylan catabolic pathways
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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
physiological function
the enzyme is active in alginate degradation
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Cynkin, M.A.; Ashwell, G.
Uronic acid metabolism in bacteria: IV. Purification and properties of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli
J. Biol. Chem.
235
1576-1579
1969
Klebsiella aerogenes, Escherichia coli, no activity in Azobacter agilis, no activity in Neurospora crassa, no activity in Salmonella typhimurium
brenda
Pouyssegur, J.; Stoeber, F.
Study of the common degradative pathway of hexuronates in Escherichia coli K 12. Purification, properties and individuality of 2-keto-3-deoxy-D-gluconokinase
Biochimie
53
771-781
1971
Escherichia coli
brenda
Inagaki, E.; Ukita, Y.; Kumei, M.; Kajihara, Y.; Tahirov, T.H.
Crystallization and preliminary crystallographic analysis of 2-keto-3-deoxygluconate kinase from Thermus thermophilus
Acta Crystallogr. Sect. D
60
761-763
2004
Thermus thermophilus
brenda
Ohshima, N.; Inagaki, E.; Yasuike, K.; Takio, K.; Tahirov, T.H.
Structure of Thermus thermophilus 2-keto-3-deoxygluconate kinase: evidence for recognition of an open chain substrate
J. Mol. Biol.
340
477-489
2004
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Jung, J.H.; Lee, S.B.
Identification and characterization of Thermoplasma acidophilum 2-keto-3-deoxy-D-gluconate kinase: A new class of sugar kinases
Biotechnol. Bioprocess Eng.
10
535-539
2005
Thermoplasma acidophilum
-
brenda
Ohshima, T.; Kawakami, R.; Kanai, Y.; Goda, S.; Sakuraba, H.
Gene expression and characterization of 2-keto-3-deoxygluconate kinase, a key enzyme in the modified Entner-Doudoroff pathway of the aerobic and acidophilic hyperthermophile Sulfolobus tokodaii
Protein Expr. Purif.
54
73-78
2007
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii (Q96XN9)
brenda
Mathews, I.I.; McMullan, D.; Miller, M.D.; Canaves, J.M.; Elsliger, M.; Floyd, R.; Grzechnik, S.K.; Jaroszewski, L.; Klock, H.E.; Koesema, E.; Kovarik, J.S.; Kreusch, A.; Kuhn, P.; McPhillips, T.M.; Morse, A.T.; Quijano, K.; Rife, C.L.; Schwarzenbacher, R
Crystal structure of 2-keto-3-deoxygluconate kinase (TM0067) from Thermotoga maritima at 2.05 A resolution
Proteins Struct. Funct. Bioinform.
70
603-608
2007
Thermotoga maritima (Q9WXS2)
-
brenda
Pickl, A.; Johnsen, U.; Archer, R.; Schnheit, P.
Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii
FEMS Microbiol. Lett.
361
76-83
2014
Haloferax volcanii (D4GSE6), Haloferax volcanii
brenda
Mathews, I.; McMullan, D.; Miller, M.; Canaves, J.; Elsliger, M.; Floyd, R.; Grzechnik, S.; Jaroszewski, L.; Klock, H.; Koesema, E.; Kovarik, J.; Kreusch, A.; Kuhn, P.; McPhillips, T.; Morse, A.; Quijano, K.; Rife, C.; Schwarzenbacher, R.; Spraggon, G.S.
Crystal structure of 2-keto-3-deoxygluconate kinase (TM0067) from Thermotoga maritima at 2.05 A resolution
Proteins
70
603-608
2008
Thermotoga maritima (Q9WXS2), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WXS2)
brenda
Nishiyama, R.; Inoue, A.; Ojima, T.
Identification of 2-keto-3-deoxy-D-gluconate kinase and 2-keto-3-deoxy-D-phosphogluconate aldolase in an alginate-assimilating bacterium, Flavobacterium sp. strain UMI-01
Mar. Drugs
15
37
2017
Flavobacterium sp. UMI-01 (A0A0B6VMB0)
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