AP BIOLOGY

Detailed explanation-1: -In competitive inhibition, a molecule similar to the substrate but unable to be acted on by the enzyme competes with the substrate for the active site.

Detailed explanation-2: -Examples of competitive inhibition include the inhibition of trypsin by -1-antitrypsin, chymotrypsin by -1-antichymotrypsin, dihydrofolate reductase by the chemotherapeutic agent methotrexate, and the Krebs cycle enzyme succinic dehydrogenase by malonate.

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: -These are called competitive inhibitors. They resemble the substrates in their structure. If they bind before substrates, the substrates cannot bind to enzymes. This results in competitive inhibition leading to blocking of the active site.

Detailed explanation-5: -Competitive inhibition occurs when molecules very similar to the substrate molecules bind to the active site and prevent binding of the actual substrate. Penicillin, for example, is a competitive inhibitor that blocks the active site of an enzyme that many bacteria use to construct their cell…