PMID:10903924

Citation	Bolesch, DG and Keasling, JD (2000) The effect of monovalent ions on polyphosphate binding to Escherichia coli exopolyphosphatase. Biochem. Biophys. Res. Commun. 274:236-41
Abstract	The thermodynamic driving force for the interaction of Escherichia coli exopolyphosphatase (PPX) with polyphosphate was investigated by varying salt choice and concentration. This interaction was found to be cation concentration independent but weakly dependent on the concentration of certain anions. Both of these traits are very uncommon for nonspecific protein-polyelectrolyte interactions. Interpretation of these results based on theory indicated that binding was not entropy driven due to release of polyelectrolyte-condensed counterions, as is the case for nearly all protein-polyelectrolyte interactions. The thermodynamics of the PPX-polyphosphate interaction showed similarity only to the interaction of polynucleotides with single stranded binding proteins.
Links	PubMed Online version:10.1006/bbrc.2000.3128
Keywords	Acid Anhydride Hydrolases/antagonists & inhibitors; Acid Anhydride Hydrolases/chemistry; Acid Anhydride Hydrolases/metabolism; Cations/metabolism; Dose-Response Relationship, Drug; Entropy; Escherichia coli/enzymology; Fluorides/pharmacology; Polyphosphates/metabolism; Potassium Chloride/pharmacology; Potassium Compounds/pharmacology; Protein Binding; Protein Structure, Tertiary; Thermodynamics
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