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Literature summary for 2.7.1.40 extracted from

  • De la Vega-Ruíz, G.; Domínguez-Ramírez, L.; Riveros-Rosas, H.; Guerrero-Mendiola, C.; Torres-Larios, A.; Hernández-Alcántara, G.; García-Trejo, J.J.; Ramírez-Silva, L.
    New insights on the mechanism of the K+-independent activity of crenarchaeota pyruvate kinases (2015), PLoS One, 10, e0119233.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.40

Cloned(Commentary)

Cloned (Comment) Organism
-
 Thermofilum pendens

Inhibitors

Inhibitors Comment Organism Structure
AMP dead-end inhibitor Thermofilum pendens
oxalate dead-end inhibitor Thermofilum pendens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information the kinetic mechanism is random order with a rapid equilibrium Thermofilum pendens
0.092
-
 ADP pH 6.0, 45°C, recombinant enzyme with His6 tag Thermofilum pendens
0.14
-
 ADP pH 6.0, 45°C, recombinant enzyme without His6 tag Thermofilum pendens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean Thermofilum pendens
Mn2+ although the maximum activity is 3.8-fold higher with Mg2+ than with Mn2+, the K0.5 for Mn2+ is 250fold lower than the K0.5 for Mg2+, with no significant change in the constants for the substrates. This finding shows that Mn2+ is the preferred divalent cation, consistent with the geochemistry of the Archaean ocean Thermofilum pendens
additional information the enzyme from Thermofilum pendens is K+-independent. Eukarya pyruvate kinases have glutamate at position 117 (numbered according to the rabbit muscle enzyme), whereas in Bacteria have either glutamate or lysine and in Archaea have other residues. Glutamate at this position makes pyruvate kinases K+-dependent, whereas lysine confers K+-independence because the positively charged residue substitutes for the monovalent cation charge. The enzyme from Thermofilum pendens has Val70 at the corresponding position Thermofilum pendens

Organism

Organism UniProt Comment Textmining
Thermofilum pendens A1RX09
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermofilum pendens

Reaction

Reaction Comment Organism Reaction ID
ATP + pyruvate = ADP + phosphoenolpyruvate the kinetic mechanism is random order with a rapid equilibrium Thermofilum pendens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate the substrate binding order of the Thermofilum pendens enzyme is independent despite lacking an internal positive charge Thermofilum pendens ATP + pyruvate
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 assay at Thermofilum pendens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
99
-
 thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of the hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability Thermofilum pendens
105
-
 thermal stability studies of this enzyme show two calorimetric transitions, one attributable to the A and C domains (Tm of 99.2°C), and the other (Tm of 105.2°C) associated with the B domain. The calorimetric and kinetic data indicate that the B domain of this hyperthermophilic enzyme is more stable than the rest of the protein with a conformation that induces the catalytic readiness of the enzyme. Intra- and interdomain interactions of the crenarchaeota enzymes may account for their higher B domain stability Thermofilum pendens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information the kinetic mechanism is random order with a rapid equilibrium Thermofilum pendens
0.16
-
 ADP pH 6.0, 45°C, in presence of Mg2+ Thermofilum pendens
0.2
-
 ADP pH 6.0, 45°C, in presence of Mn2+ Thermofilum pendens
0.38
-
 phosphoenolpyruvate pH 6.0, 45°C, in presence of Mg2+ Thermofilum pendens
1
-
 phosphoenolpyruvate pH 6.0, 45°C, in presence of Mn2+ Thermofilum pendens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Thermofilum pendens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
35
-
 AMP pH 6.0, 45°C Thermofilum pendens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information the kinetic mechanism is random order with a rapid equilibrium Thermofilum pendens