Enzyme inhibitors can alter the \(K_m\) value. Competitive inhibitors increase \(K_m\) without affecting \(Vmax\), as they compete with the substrate for the active site of the enzyme. On the other hand, non-competitive inhibitors do not change \(K_m\) but decrease \(Vmax\), as they bind to a different site on the enzyme and alter its activity. Understanding these effects is essential for developing effective inhibitors in pharmaceutical applications.
