cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase

The cooperative binding of the allosteric activator fructose-1,6-bisphosphate [Fru(1,6)P2] to yeast pyruvate kinase was investigated by equilibrium dialysis and fluorescence quench titration. The results show that yeast pyruvate kinase binds four molecules of Fru(1,6)P2 per tetramer and the observed...

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Veröffentlicht in:	The EMBO journal 1992-11, Vol.11 (11), p.3811-3814
Hauptverfasser:	Murcott, T.H.L, Gutfreund, H, Muirhead, H
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric Regulation Allosteric Site Analytical, structural and metabolic biochemistry binding binding sites Biological and medical sciences cooperative Dialysis enzyme activity Enzymes and enzyme inhibitors fructose fructose-1,6-bisphosphate Fructosediphosphates - metabolism Fundamental and applied biological sciences. Psychology Kinetics Models, Molecular molecular conformation Protein Binding Protein Conformation pyruvate kinase Pyruvate Kinase - metabolism Regression Analysis Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Spectrometry, Fluorescence sugar phosphates Transferases
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