Transplanting allosteric control of enzyme activity by protein-protein interactions: Coupling a regulatory site to the conserved catalytic core

摘要

Glycerol kinase from Escherichia coli, but not Haemophilus influ- enzae, is inhibited allosterically by phosphotransferase system protein IIA~Glc. The primary structures of these related kinases contain 501 amino acids, differing at 117. IIA~Glc inhibition is trans- planted from E. coli glycerol kinase into H. influenzae glycerol kinase by interconverting only 11 of the differences: 8 residues that interact with IIA~Glc at the allosteric binding site and 3 residues in the conserved ATPase catalytic core that do not interact with IIA~Glc but the solvent accessible surface of which decreases when it binds.