Information on EC 4.2.1.140 - gluconate/galactonate dehydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.140
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RECOMMENDED NAME
GeneOntology No.
gluconate/galactonate dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O
show the reaction diagram
D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactonate degradation
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Entner-Doudoroff pathway II (non-phosphorylative)
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Entner-Doudoroff pathway III (semi-phosphorylative)
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Galactose metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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Pentose phosphate pathway
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degradation of sugar acids
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Entner Doudoroff pathway
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SYSTEMATIC NAME
IUBMB Comments
D-gluconate/D-galactonate hydro-lyase
The enzyme is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway in Picrophilus torridus [3] and via the branched variant of the Entner-Doudoroff pathway in Sulfolobus solfataricus [1,2]. In vitro it utilizes D-gluconate with 6-10 fold higher catalytic efficiency than D-galactonate [1,3]. It requires Mg2+ for activity [1,2]. cf. EC 4.2.1.6, galactonate dehydratase, and EC 4.2.1.39, gluconate dehydratase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-galactonate
2-dehydro-3-deoxy-D-galactonate + H2O
show the reaction diagram
D-gluconate
2-dehydro-3-deoxy-D-gluconate + H2O
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
D-galactonate
2-dehydro-3-deoxy-D-galactonate + H2O
show the reaction diagram
D-gluconate
2-dehydro-3-deoxy-D-gluconate + H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EGTA
enzyme activity is reduced to 24% after dialysis in buffer containing EGTA. Activity is completely recovered in the presence of 10 mM MgCl2 and recovered to 39% and 62% in the presence of MnCl2 and CoCl2, respectively
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.81 - 2
D-galactonate
1.57 - 2.5
D-gluconate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.08
D-galactonate
Sulfolobus solfataricus
Q97U27
pH 6.0, 70°C
10.4
D-gluconate
Sulfolobus solfataricus
Q97U27
pH 6.0, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.33
D-galactonate
Sulfolobus solfataricus
Q97U27
pH 6.0, 70°C
3335
6.65
D-gluconate
Sulfolobus solfataricus
Q97U27
pH 6.0, 70°C
698
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
substrate: D-gluconate, pH 6.2, 60°C
additional information
13.4 U/mg, pH 6.0, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.1
pH 4.5: 50% of maximal activity, pH 8.1: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
8 * 44000, SDS-PAGE
44729
1 * 44729, calculated from sequence
45000
1 * 45000, SDS-PAGE
48000
gel filtration
340000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
8 * 44000, SDS-PAGE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
half-life: 15 min
95
half-life: 41 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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