You discover a new inhibitor to an enzyme and a crystal structure clearly shows that it binds in the active site at the same location as the substrate. What do you think that this means about the likelihood that this inhibitor will show competitive inhibition? How would you know if this inhibitor was competitive or not? Hines biopharma has created a compound called CH523 that binds to an allosteric site approximately 15A away from the active site of ABCase. Crystal structures reveal that this allosteric site is blocked in the absence of substrate; a Phe residue blocks the ligand binding pocket. When the enzyme binds the substrate, a shift in a helix connecting the active site and the allosteric site displaces the sidechain, clearing the pocket and allowing the inhibitor to bind. When the inhibitor is bound, it prevents a nearby loop from moving to associate with the remainder of the active site The association of this loop with the active site is necessary for catalysis to occur. Binding studies have confirmed predictions made by the crystal structures: in the absence of substrate, the inhibitor does not bind lo the enzyme. What type of kinetics do you think CHS23 will exhibit? Explain your answer!