Almost no metabolic reaction is able to occur without the help of an enzyme. Explain how the structure of an allosteric enzyme and substrate function to control a metabolic pathway. Include a specific example in your answer.
In noncompetitive inhibition (also known as allosteric inhibition), an inhibitor binds to an allosteric site; the substrate can still bind to the enzyme, but the enzyme is no longer in optimal position to catalyze the reaction.
Allosteric inhibitors induce a conformational change that changes the shape of the active site and reduces the affinity of the enzyme’s active site for its substrate.