MUSCLE PHYSIOLOGY

Detailed explanation-1: -A competitive inhibitor competes with substrate for binding to an active site. When the inhibitor occupies the active site, it forms an enzyme-inhibitor complex and the enzyme cannot react (Fig. 4-4) until the inhibitor dissociates.

Detailed explanation-2: -In virtually every case, competitive inhibitors bind in the same binding site (active site) as the substrate, but same-site binding is not a requirement.

Detailed explanation-3: -The competitive inhibitor binds to the active site and prevents the substrate from binding there. The noncompetitive inhibitor binds to a different site on the enzyme; it doesn’t block substrate binding, but it causes other changes in the enzyme so that it can no longer catalyze the reaction efficiently.

Detailed explanation-4: -Explanation: Competitive inhibitors bind to the active site of the enzyme and prevent substrates from binding to enzyme. This prevents the enzyme-substrate reaction from happening, thereby decreasing the activity of enzymes; however, competitive inhibitors can be overcome by increasing the concentration of substrates.

Detailed explanation-5: -A competitive inhibitor is any molecule that can bind to the active site of an enzyme with sufficient affinity such that it can compete with the enzyme’s natural substrate and reduce enzyme activity as a result.