Information on EC 2.7.1.178 - 2-dehydro-3-deoxyglucono/galactono-kinase

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The expected taxonomic range for this enzyme is: Sulfolobus solfataricus

EC NUMBER
COMMENTARY hide
2.7.1.178
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RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxyglucono/galactono-kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
show the reaction diagram
ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3,6-anhydro-alpha-L-galactopyranose degradation
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4-deoxy-L-threo-hex-4-enopyranuronate degradation
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alginate degradation
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D-fructuronate degradation
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D-galactonate degradation
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D-galacturonate degradation I
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Entner-Doudoroff pathway III (semi-phosphorylative)
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L-glucose degradation
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degradation of sugar acids
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Entner Doudoroff pathway
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Pentose phosphate pathway
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Galactose metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
ATP:2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase
The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with similar catalytic efficiency. cf. EC 2.7.1.45, 2-dehydro-3-deoxygluconokinase and EC 2.7.1.58, 2-dehydro-3-deoxygalactonokinase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-D-galactonate 6-phosphate
show the reaction diagram
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-D-galactonate 6-phosphate
show the reaction diagram
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?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.1
2-dehydro-3-deoxy-D-galactonate
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pH 7.5, 60°C
0.14 - 3.6
2-dehydro-3-deoxy-D-gluconate
2.8
ATP
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pH 7.5, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.4
2-dehydro-3-deoxy-D-galactonate
Sulfolobus solfataricus
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pH 7.5, 60°C
5 - 60.8
2-dehydro-3-deoxy-D-gluconate
3.8
ATP
Sulfolobus solfataricus
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pH 7.5, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
2-dehydro-3-deoxy-D-galactonate
Sulfolobus solfataricus
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pH 7.5, 60°C
3965
1.4 - 434
2-dehydro-3-deoxy-D-gluconate
1172
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
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calculated from sequence
PDB
SCOP
CATH
ORGANISM
UNIPROT
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 34875, calculated from sequence; x * 37513, mass spectrometric analysis
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method, crystallized in 0.1 M sodium acetate pH 4.1 and 1.4 M NaCl. The crystal structure of apoenzyme is solved by molecular replacement to a resolution of 2.0 A and a ternary complex with 2-dehydro-3-deoxygluconate and an ATP analogue is resolved at 2.1 A. The complex suggests that the structural basis for the enzyme’s ability to phosphorylate 2-oxo-3-deoxygluconate and 2-dehydro-3-deoxygalactonate is derived from a subtle repositioning of residues that are conserved in homologous nonpromiscuous kinases
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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deactivated above
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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produced as inclusion bodies in Escherichia coli when polyhistidine is used as a fusion tag. To reduce inclusion body formation in Escherichia coli, the enzyme is fused with three partners, thioredoxin, glutathione-S-transferase, and N-utilization substance A. With the use of fusion-partners, the solubility of the archaeal protein is remarkably enhanced, and the soluble fraction of the recombinant protein is increased in this order: thioredoxin > glutathione-S-transferase > N-utilization substance A. In the case of recombinant enzyme, the enzyme activity of the Trx-fused protein is 200-fold higher than that of the polyhistidine-fusion protein
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