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Literature summary extracted from

  • Tjaden, B.; Plagens, A.; Doerr, C.; Siebers, B.; Hensel, R.
    Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase of Thermoproteus tenax: key pieces in the puzzle of archaeal carbohydrate metabolism (2006), Mol. Microbiol., 60, 287-298.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.9.1 additional information neither inhibition nor activation of anabolic PPDK activity observed, kinetics of catabolic pathway Thermoproteus tenax

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.9.1 Escherichia coli, strains DH5alpha and BL21-CodonPLUS(DE3)-RIL Thermoproteus tenax
2.7.9.2 expressed in Escherichia coli strains DH5alpha and BL21-CodonPlus(DE3)-RIL Thermoproteus tenax

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.9.1 ATP concentration 1 mM, 55°C, AMP-competitive inhibition as deduced from AMP saturation kinetics by using various ATP concentration ranging between 50-200 micromol Thermoproteus tenax
2.7.9.1 D-glucose 1-phosphate 72% activity sustained, effector concentration 5 mM, 55°C Thermoproteus tenax
2.7.9.1 additional information inhibition by UDP and D-glucose 1-phosphate at rather high and unphysiological concentrations, no inhibitory effects by alpha-ketoglutarate (1 mM), potassium phosphate (5 mM), glyceraldehyde 3-phosphate (5 mM), 3-phosphoglycerate (5 mM), dihydroxyacetone phosphate (5 mM) Thermoproteus tenax
2.7.9.1 UDP 55% activity of PPDK, effector concentration 5 mM, 55°C Thermoproteus tenax
2.7.9.2 2-oxoglutarate strong inhibition at 1 mM Thermoproteus tenax
2.7.9.2 ADP strong inhibition at 1 mM Thermoproteus tenax
2.7.9.2 AMP strong inhibition at 1 mM Thermoproteus tenax

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.9.1 additional information
-
 additional information reactions follow classical Michaelis Menten kinetics for pyruvate and phosphate, sigmoidal saturation curve observed with ATP, neither inhibition nor activation of the anabolic PPDK activity observed Thermoproteus tenax
2.7.9.1 0.02
-
 AMP 55°C Thermoproteus tenax
2.7.9.1 0.08
-
 diphosphate 55°C Thermoproteus tenax
2.7.9.1 0.5
-
 phosphoenolpyruvate 55°C Thermoproteus tenax
2.7.9.1 0.8
-
 pyruvate 70°C Thermoproteus tenax
2.7.9.1 3.5
-
 diphosphate 70°C Thermoproteus tenax
2.7.9.1 8
-
 ATP KM/S50-value, 70°C Thermoproteus tenax
2.7.9.2 0.4
-
 pyruvate in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70°C Thermoproteus tenax
2.7.9.2 1
-
 ATP in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70°C Thermoproteus tenax

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.9.1 Mg2+
-
 Thermoproteus tenax
2.7.9.1 additional information not depending on monovalent cations such as K+, Na+, NH4+ Thermoproteus tenax
2.7.9.2 Mg2+ 10 mM, required Thermoproteus tenax
2.7.9.2 additional information activity of PEPS does not depend on monovalent cations such as K+ and NH4+ Thermoproteus tenax

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.9.1 100000
-
 x * 100000, SDS-PAGE, homomeric dimer, calculated from theoretical weight and chromatography, more similar to bacterial PPDKs (dimer) than protists or plants (tetramer) Thermoproteus tenax
2.7.9.1 102300
-
 theoretical weight calculated from sequence Thermoproteus tenax
2.7.9.1 250000
-
 native protein, gelfiltration Thermoproteus tenax
2.7.9.2 88000
-
 SDS-PAGE, recombinant enzyme, phosphoenzyme intermediate form Thermoproteus tenax
2.7.9.2 90500
-
 calculated from amino acid sequence Thermoproteus tenax
2.7.9.2 94000
-
 SDS-PAGE, recombinant enzyme, nonphosphorylated form Thermoproteus tenax
2.7.9.2 600000
-
 above 600000, gel filtration Thermoproteus tenax

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.1 Methanosarcina acetivorans Q8TT31 Euryarchaea, Archaeabacteria
-
2.7.9.1 Pyrobaculum aerophilum Q8ZT84 Crenarchaea, Archaeabacteria
-
2.7.9.1 Thermoproteus tenax Q70WQ6 the entire gene consists of 2748 bp, GC content of 52.6%, protein of 915 amino acids corresponding to a theoretical molecular mass of 102.3 kDa, sequence signatures compared to other PPDK genes; hyperthermophilic crenarchaeote, Archaeabacteria, mass culture of Thermoproteus strain DSM 2078
-
2.7.9.2 Thermoproteus tenax Q70WQ8
-
-
2.7.9.2 Thermoproteus tenax Kra1 Q70WQ8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.9.1 recombinant protein, heat precipitation at 90°C for 20 min, ion exchange chromatography Thermoproteus tenax
2.7.9.2 Q-sepharose chromatography Thermoproteus tenax

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.9.1 additional information
-
 the maximal specific activity of the catabolic reaction is approximately 2fold higher if compared to the anabolic reaction, indicated by lower Km-values for reaction compounds of the catabolic reaction, kinetics at 55°C and 70°C shown, neither inhibition nor activation of anabolic PPDK activity observed Thermoproteus tenax

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.9.1 ATP + pyruvate + phosphate bidirectional activity, preference for catabolic reaction, DELTA G +9.9 kJ/mole Thermoproteus tenax AMP + phosphoenolpyruvate + diphosphate
-
 r
2.7.9.2 ATP + pyruvate + H2O
-
 Thermoproteus tenax AMP + phosphoenolpyruvate + phosphate
-
 ir
2.7.9.2 ATP + pyruvate + H2O
-
 Thermoproteus tenax Kra1 AMP + phosphoenolpyruvate + phosphate
-
 ir
2.7.9.2 additional information neither GTP, CTP, ITP nor UTP is active as phosphoryl donor Thermoproteus tenax ?
-
 ?
2.7.9.2 additional information neither GTP, CTP, ITP nor UTP is active as phosphoryl donor Thermoproteus tenax Kra1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.9.1 homodimer x * 100000, SDS-PAGE, homomeric dimer, calculated from theoretical weight and chromatography, more similar to bacterial PPDKs (dimer) than protists or plants (tetramer) Thermoproteus tenax
2.7.9.2 multimer native enzyme, gel filtration Thermoproteus tenax

Synonyms

EC Number Synonyms Comment Organism
2.7.9.1 PPDK
-
 Thermoproteus tenax
2.7.9.1 pyruvate, phoshphate dikinase
-
 Thermoproteus tenax
2.7.9.2 PEP synthetase
-
 Thermoproteus tenax
2.7.9.2 PEPS
-
 Thermoproteus tenax
2.7.9.2 phosphoenolpyruvate synthetase
-
 Thermoproteus tenax

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.9.1 additional information
-
 additional information assay overview, kinetics at 55°C and 70°C, anabolic and catabolic direction Thermoproteus tenax
2.7.9.2 0.683
-
 pyruvate in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70°C Thermoproteus tenax

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.9.2 ATP
-
 Thermoproteus tenax

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.9.1 0.07
-
 ATP 55°C, AMP saturation kinetics with ATP concentration of 50-200 micromol Thermoproteus tenax
2.7.9.2 0.5
-
 AMP in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70°C Thermoproteus tenax
2.7.9.2 0.6
-
 2-oxoglutarate in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70°C Thermoproteus tenax
2.7.9.2 2.6
-
 ADP in 100 mM Tris/HCl, pH 7.0, in the presence of 20 mM beta-mercaptoethanol, 6 mM pyruvate, 10 mM ATP and 10 mM MgCl2, at 70°C Thermoproteus tenax