Biochemistry Questions Biochemistry Questions / Explain the concept of competitive inhibition using the Michaelis-Menten curve. How does this type of inhibitor affect binding efficiency and the maximal rate of the reaction? Discuss the necessity of mutational analysis in identifying non-competitive inhibitors.

Competitive inhibition of an enzyme occurs at the orthosteric site. The inhibitor blocks the active site, preventing the endogenous substrate from binding and thus reducing the maximal rate (Vmax) of the reaction.

The binding efficiency of the substrate is not changed by the presence of a competitive inhibitor, however the number of enzymes available is impacted, as the inhibitor will prevent some / all from being available.

Mutational analysis is necessary to identify some types of inhibitors. This involves mutating residues within the active site of the enzyme, preventing the inhibitor from binding while still allowing substrate to bind and undergo the reaction.