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Literature summary for 2.7.1.45 extracted from

  • Ahmed, H.; Ettema, T.J.; Tjaden, B.; Geerling, A.C.; van der Oost, J.; Siebers, B.
    The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation (2005), Biochem. J., 390, 529-540.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.45

Cloned(Commentary)

Cloned (Comment) Organism
gene kdgK as part of the ED gene cluster, expresssion in Escherichia coli Saccharolobus solfataricus
gene kdgK as part of the ED gene cluster, expresssion in Escherichia coli as soluble proein at low rate Thermoproteus tenax

Protein Variants

Protein Variants Comment Organism
additional information reconstruction of the Entner-Doudoroff pathway with recombinantly produced enzymes of Thermoproteus tenax and Solfolobus solfataricus, overview Saccharolobus solfataricus
additional information reconstruction of the Entner-Doudoroff pathway with recombinantly produced enzymes of Thermoproteus tenax and Solfolobus solfataricus, overview Thermoproteus tenax

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.178
-
 2-dehydro-3-deoxy-D-gluconate pH 7.0, 70°C, recombinant enzyme Thermoproteus tenax

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ absolutely dependent on Saccharolobus solfataricus
Mg2+ absolutely dependent on Thermoproteus tenax

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
 x * 32000, recombinant enzyme, SDS-PAGE, x * 33308, sequence calculation Thermoproteus tenax
33308
-
 x * 32000, recombinant enzyme, SDS-PAGE, x * 33308, sequence calculation Thermoproteus tenax

Organism

Organism UniProt Comment Textmining

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli, by heat precipitation and gel filtration Thermoproteus tenax

Source Tissue

Source Tissue Comment Organism Textmining
additional information the archaeon grows optimally at 80-85°C and pH 2-4 Saccharolobus solfataricus
-
additional information the archaeon grows optimally at about 90°C and pH 5.0 Thermoproteus tenax
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Saccharolobus solfataricus
additional information
-
-
 Thermoproteus tenax
0.104
-
 recombinant cell extract after heat precipitation step Saccharolobus solfataricus
41.3
-
 purified recombinant enzyme Thermoproteus tenax

Subunits

Subunits Comment Organism
? x * 32000, recombinant enzyme, SDS-PAGE, x * 33308, sequence calculation Thermoproteus tenax

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 the archaeon grows optimally at 80-85°C and pH 2-4 Saccharolobus solfataricus
additional information
-
 the archaeon grows optimally at about 90°C and pH 5.0 Thermoproteus tenax
60
-
 assay at Saccharolobus solfataricus
70
-
 assay at Thermoproteus tenax

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 the archaeon grows optimally at 80-85°C and pH 2-4 Saccharolobus solfataricus
additional information
-
 the archaeon grows optimally at about 90°C and pH 5.0 Thermoproteus tenax
7
-
 assay at Saccharolobus solfataricus
7
-
 assay at Thermoproteus tenax

Cofactor

Cofactor Comment Organism Structure
ATP absolutely dependent on Saccharolobus solfataricus
ATP absolutely dependent on Thermoproteus tenax