Graphical analyses on binding of ligands to a two-sited system. Theoretical treatments exemplified on yeast phosphoglycerate kinase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference23 articles.
1. Kinetic studies on the reaction catalyzed by phosphoglycerate kinase
2. The Phosphoglycerate Kinase Reaction and its Metal Ion Specificity
3. Inhibition of Phosphoglycerate Kinase by Products and Product Homologues
4. The Binding of Organic Ions by Proteins1
5. THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
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1. Role of Phosphate Chain Mobility of MgATP in Completing the 3-Phosphoglycerate Kinase Catalytic Site: Binding, Kinetic, and Crystallographic Studies with ATP and MgATP;Biochemistry;2004-03-01
2. Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer;Quarterly Reviews of Biophysics;1999-02
3. Anion Activation of 3-Phosphoglycerate Kinase Requires Domain Closure;Biochemistry;1998-05-22
4. Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium dialysis binding and enzyme kinetic data;Biochemical Journal;1993-07-15
5. Estimation of the intracellular free ADP concentration by fluorine-19 NMR studies of fluorine-labeled yeast phosphoglycerate kinase in vivo;Biochemistry;1993-05-11
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