BIOMOLECULES AND ENZYMES

Detailed explanation-1: -In noncompetitive inhibition, the inhibitor doesn’t block the substrate from binding to the active site. Instead, it attaches at another site and blocks the enzyme from doing its job. This inhibition is said to be “noncompetitive” because the inhibitor and substrate can both be bound at the same time.

Detailed explanation-2: -In noncompetitive inhibition, the inhibitor binds at an allosteric site separate from the active site of substrate binding. Thus in noncompetitive inhibition, the inhibitor can bind its target enzyme regardless of the presence of a bound substrate.

Detailed explanation-3: -Correct answer: Noncompetitive inhibitors bind irreversibly to the enzyme and prevent the substrate-enzyme activity. This decreases the efficacy of the enzyme.

Detailed explanation-4: -Remember that non-competitive inhibitors aren’t attaching directly to the active site, but elsewhere on the enzyme. The inhibitor attachs to a side group in the protein chain, and affects the way the protein folds into its tertiary structure. That in turn changes the shape of the active site.

Detailed explanation-5: -Non-competitive inhibition is a type of enzyme inhibition where the inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate.