Question

Which of the following statements about inhibitors of enzyme-catalyzed reactions is TRUE? Reversible inhibitors bind to either free enzyme or the enzyme-substrate complex but not both. An uncompetitive inhibitor will always bind at the active site. An uncompetitive inhibitor typically affects KM but not k cat. A competitive inhibitor does not affect V max. All of the following are properties of a coenzyme EXCEPT: They tend to be stable to heat. They are protein components. They can serve as intermediate carriers of functional groups. They are usually actively involved in the catalytic reaction of the enzyme.

My answers were incorrect. Could I get the answer and explanations please?

Answer 1

Solution.

Q-5. A competative inhibitor doesnot affect Vmax.

      In competitive inhibition, the substrate and inhibitor cannot bind to the enzyme at the same time, This usually results from the inhibitor having an affinity for the active site of an enzyme where the substrate also binds; the substrate and inhibitor compete for access to the enzyme's active site. This type of inhibition can be overcome by sufficiently high concentrations of substrate (V_max remains constant), i.e., by out-competing the inhibitor.

Q- 6.They can serve as intermediate carriers of functional groups.