Interaction of DnaK with ATP: Binding, hydrolysis and Ca+2-stimulated autophosphorylation

The autophosphorylation of DnaK from Escherichia coli using ATP as phosphate donor is markedly stimulated by Ca+2 and to a lesser degree by Mn+2. Mg+2 and other divalent ions are without effect in this reaction. Lanthanum, an agonist/antagonist of Ca+2, is also effective in stimulating the autophosp...

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Veröffentlicht in:	Biochemical and biophysical research communications 1990-02, Vol.166 (3), p.1284-1292
Hauptverfasser:	Dalie, Barbara L., Skaleris, Diane A., Köhle, Kathrin, Weissbach, Herbert, Brot, Nathan
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acids - analysis Bacterial Proteins - metabolism Biological and medical sciences Calcium - pharmacology Cations, Divalent Cell Membrane - metabolism Egtazic Acid - pharmacology Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins Hydrolysis Interactions. Associations Intermolecular phenomena Kinetics Lanthanum - pharmacology Molecular biophysics Phosphorylation Protein Binding
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