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Literature summary for 2.7.1.40 extracted from

  • Ramirez-Silva, L.; Oria-Hernandez, J.
    Selectivity of pyruvate kinase for Na+ and K+ in water/dimethylsulfoxide mixtures (2003), Eur. J. Biochem., 270, 2377-2385.
    View publication on PubMed
Search for more literature for 2.7.1.40

Metals/Ions

Metals/Ions Comment Organism Structure
K+ in aqueous media, muscle pyruvate kinase is highly selective for K+ over Na+. Dimethylsulfoxide favors the partition of K+ and Na+ into the monovalent and divalent cation binding sites of the enzyme. The kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affnities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20. The data suggest that K+ induces conformational changes that prevent the binding of Mg2+ to the monovalent cation binding site Oryctolagus cuniculus
Mg2+ kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affinities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20 Oryctolagus cuniculus
Na+ in aqueous media, muscle pyruvate kinase is highly selective for K+ over Na+. Dimethylsulfoxide favors the partition of K+ and Na+ into the monovalent and divalent cation binding sites of the enzyme. The kinetics of the enzyme at subsaturating concentrations of activators show that K+ and Mg2+ exhibit high selectivity for their respective cation binding sites, whereas when Na+ substitutes K+, Na+ and Mg2+ bind with high affinity to their incorrect sites. The ratio of the affnities of Mg2+ and K+ for the monovalent cation binding site is close to 200. For Na+ and Mg2+ this ratio is approximately 20. The data suggest that K+ induces conformational hanges that prevent the binding of Mg2+ to the monovalent cation binding site Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
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 Oryctolagus cuniculus
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