BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Allosteric inhibitors block the active site. Allosteric inhibitors change the shape of the enzyme. Adding a competitive inhibitor will increase the number of products in the reaction. Competitive inhibitors bind to the substrates.

Detailed explanation-2: -The allosteric inhibitor binds to an enzyme at a site other than the active site. The shape of the active site is altered so that the enzyme can no longer bind to its substrate.

Detailed explanation-3: -The allosteric site is the site, which is not the active site, where some drugs bind to an enzyme. Due to this, the shape of the enzyme changes, it becomes difficult for the substrate to recognize the active site of the enzyme.

Detailed explanation-4: -Answer and Explanation: The correct answer is (B) Allosteric inhibition involves conformational changes in the protein. In allosteric inhibition, a molecule known as an allosteric inhibitor binds to an enzyme at a site that is different from the active site of the enzyme, which is where the reaction takes place.

Detailed explanation-5: -Which of the following is not true for allosteric enzyme? Explanation: “Each of two or more enzymes with identical function but a different structure.” This statement is not true for allosteric enzymes as it is defining isoenzyme.