How do competitive inhibitors affect the Km and Vmax of an enzyme-catalyzed reaction?

An uncompetitive inhibitor is added to an enzyme reaction. What changes would you expect in Km and Vmax?

If a mixed inhibitor has an alpha value greater than alpha prime, what is the expected effect on Km?

Given an enzyme reaction with a competitive inhibitor, if the initial Km is 5 mM and the inhibitor increases Km by a factor of 2, what is the new Km?

Which analogy best describes the mechanism of competitive inhibition?

Predict the outcome of an enzyme reaction when a mixed inhibitor with alpha less than alpha prime is added.

Which inhibitor type is known to decrease Vmax without changing Km?