Allostery in E.coli phosphofructokinase
Keywords:
Allosteric contnol,
E. coli phosphofructokinase,
Glycolysls,
Ligand binding,
Subunit interface
1987 Volume 27 Issue 1 Pages 1-3
Details
1987 Volume 27 Issue 1 Pages 1-3
Phosphofructokinase from E. coli shows cooperative kinetics with respect to the substrate to fructose-6-phosphate, allosteric activation by ADP and inhibition by phosphoenolpyruvate. The crystal structure of the enzyme with active conformation has been solved, which allows us to discuss the allostery in this enzyme.
