Hinesbiopharma has created a compound called CH 523 that binds to an allosteric

Question

Hinesbiopharma has created a compound called CH 523 that binds to an allosteric site approximately 15A away from the active site of AB Case. 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 in s the substrate, a shift in a helix connecting the active site and the allosteric site displaces the Phe side chain, 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 to the enzyme. What type of kinetics do you think CH523 will exhibit? Explain your answer!

Explanation / Answer

The type of inhibition decribed above is competitive inhibition.

Here the binding of inhibitor prevents any further association which is necessary for the catalysis in the given reaction of the loop.

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