Phosphofructokinase: structure and control.

摘要: Phosphofructokinase from Bacillus stearothermophilus shows cooperative kinetics with respect to the substrate fructose-6-phosphate (F6P), allosteric activation by ADP, and inhibition phosphoenolpyruvate. The crystal structure of active conformation enzyme has been solved 2.4 A resolution, three ligand-binding sites have located. Two these form site bind substrates F6P ATP. third binds both activator inhibitor. complex ADP partly refined at a model ATP built into using 6 resolution map bound 5'-adenylylimidodiphosphate (AMPPNP). $\gamma$ -phosphate is close 1-hydroxyl F6P, in suitable position for in-line phosphoryl transfer. binding phosphate involves two arginines neighbouring subunit tetramer, which suggests that rearrangement subunits could explain cooperativity binding. also residues subunits.