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Literature summary for 2.7.1.40 extracted from

  • Suzuki, K.; Ito, S.; Shimizu-Ibuka, A.; Sakai, H.
    Crystal structure of pyruvate kinase from Geobacillus stearothermophilus (2008), J. Biochem., 144, 305-312.
    View publication on PubMed
Search for more literature for 2.7.1.40

Activating Compound

Activating Compound Comment Organism Structure
AMP wild-type, A0.5 value 0.013 mM Geobacillus stearothermophilus
D-ribose 5-phosphate wild-type, A0.5 value 0.0075 mM Geobacillus stearothermophilus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Geobacillus stearothermophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant C9S/C268S, 2.4 A resolution. Crystal belongs to space group P6222. Enzyme is a homotetramer, a sulfate ion is bound in a pocket in the effector-binding C domain Geobacillus stearothermophilus

Protein Variants

Protein Variants Comment Organism
C9S/C268S crystallization data Geobacillus stearothermophilus
H425A the A0.5 values for H425A are increased 8.0- and 60fold for D-ribose 5-phosphate and AMP Geobacillus stearothermophilus
V435E about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical Geobacillus stearothermophilus
V435K about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical Geobacillus stearothermophilus
V435R about fourfold increase in A0.5 values for D-ribose 5-phosphate compared with that of the wild-type enzyme. The A0.5 values for AMP and the S0.5 values are essentially identical Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q02499
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Subunits

Subunits Comment Organism
tetramer crystallization data Geobacillus stearothermophilus