Phosphorylation- and ligand-induced conformational changes of rat liver fructose-1,6-bisphosphatase |
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Authors: | H Vidal B Roux J P Riou |
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Affiliation: | 1. INSERM U.197, Faculté de Médecine Alexis Carrel, rue G. Paradin, F-69372 Lyon Cédex 08, France;1. Laboratoire de Physico-chimie biologique, Université Claude Bernard, F-69622 Villeurbanne, France;1. Catherine & Joseph Aresty Department of Urology, Keck Medicine of USC, University of Southern California, Los Angeles, CA, USA;2. Department of Urology, University of Florida College of Medicine, University of Florida, Gainesville, FL, USA;3. Citrus Memorial Hospital, Inverness, FL, USA |
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Abstract: | The effects of cyclic AMP-dependent phosphorylation on the structural properties of rat liver fructose-1,6-bisphosphatase were investigated by uv difference spectroscopy and circular dichroism. The incorporation of 4 mol of phosphate per mole of fructose-1,6-bisphosphatase induces a significant increase in the alpha-helix content of the enzyme without affecting its spectrophotometric properties. The addition of fructose 1,6-bisphosphate or fructose 2,6-bisphosphate also affects the conformation of the enzyme. However, both the phosphorylated and the nonphosphorylated forms exhibit similar ligand-induced conformational changes. These results show that cyclic AMP-dependent phosphorylation of fructose-1,6-bisphosphatase induces a specific conformational change. They also suggest that this modification does not alter the interaction of the enzyme protein with fructose 1,6-bisphosphate and fructose 2,6-bisphosphate. |
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