NEET BIOLOGY

Detailed explanation-1: -If an inhibitor is noncompetitive, the enzyme-catalyzed reaction will never reach its normal maximum rate even with a lot of substrate. This is because the enzyme molecules with the noncompetitive inhibitor bound are “poisoned” and can’t do their job, regardless of how much substrate is available.

Detailed explanation-2: -Enzyme inhibitors are compounds which modify the catalytic properties of the enzyme and, therefore, slow down the reaction rate, or in some cases, even stop the catalysis. Such inhibitors work by blocking or distorting the active site.

Detailed explanation-3: -A denatured enzyme refers to an enzyme that has lost its normal three-dimensional, or tertiary, structure. Once an enzyme loses this structure and is denatured, it is no longer able to function.

Detailed explanation-4: -Competitive enzyme inhibitors possess a similar shape to that of the substrate molecule and compete with the substrate for the active site of the enzyme. This prevents the formation of enzyme-substrate complexes. Therefore, fewer substrate molecules can bind to the enzymes so the reaction rate is decreased.

Detailed explanation-5: -Types of Enzyme Inhibition Enzyme inhibitors can block the binding site, preventing the substrate from attaching to the active site, and decreasing the enzyme’s catalytic activity. Reversible inhibitors attach to enzymes via non-covalent interactions like hydrogen bonds, hydrophobic contacts, and ionic bonds.