Gibbs energy profiles have great utility as teaching and learning tools because they present students with a visual representation of the energy changes that occur during enzyme catalysis. Unfortunately, most textbooks divorce discussions of traditional kinetic topics, such as enzyme inhibition, from discussions of these same topics in terms of Gibbs energy profiles. Examination of the changes in the values of the apparent kinetic parameters KS[superscript app], k[subscript cat][superscript app], and (k[subscript cat]/K[subscript M])[superscript app] in response to various modes of inhibition may be informative to students when presented in combination with Gibbs energy profiles. Herein, the symbolism of standard Gibbs energy profiles is utilized to derive expressions for the changes in Gibbs energy associated with the apparent kinetic parameters and to describe their behavior in the presence of either a competitive, uncompetitive, noncompetitive, or linear mixed-type inhibitor under rapid equilibrium conditions. The approach is intuitive and complementary to the traditional derivations of enzyme kinetic equations. (Contains 2 figures.)