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Literature summary extracted from

  • Suzuki, K.; Ito, S.; Shimizu-Ibuka, A.; Sakai, H.
    Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus (2005), Acta Crystallogr. Sect. F, 61, 759-761.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.40 D-ribose 5-phosphate
-
 Geobacillus stearothermophilus
2.7.1.40 additional information not activated by fructose 1,6-bisphosphate Geobacillus stearothermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.40 expressed in Escherichia coli strain PB25 Geobacillus stearothermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.40 hanging and sitting drop vapour diffusion methods Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.40 W416F/V435W high affinity for phosphoenolpyruvate compared to the wild-type enzyme, but its saturation curve is still sigmoidal and hyperbolic in the presence of allosteric activators Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.40 Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.40 Butyl-Toyopearl 650S chromatography and Resource Q column chromatography Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.40 ADP + phosphoenolpyruvate
-
 Geobacillus stearothermophilus ATP + pyruvate
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.40 ADP
-
 Geobacillus stearothermophilus
2.7.1.40 AMP
-
 Geobacillus stearothermophilus