Irreversible inhibition: Irreversible inhibitors check the reaction rate by occupying the active sites or destroying the globular structure. They occupy the active sites by forming covalent bonds or they may physically block the active sites.
In reversible inhibition, the inhibitor forms weak linkages with enzyme. Their effect can be neutralized completely or partially by increase in concentration of substrate.
In competitice inhibition, inhibitors resemble the normal substrate molecule and compete for admission into the active site. It reduces the productivity of enzyme by blocking the substrate from entering into active site.
Non-competitive inhibitors obstruct enzymatic reactions by binding to a part of enzyme away from the active site. This interaction causes the enzyme molecule to change its shape, rendering the active site unreceptive to substrate, or leaving the enzyme less effective at catalyzing. Hence this option is correct.
Non-competitive inhibitors obstruct enzymatic reactions by binding to a part of enzyme away from the active site. This interaction causes the enzyme molecule to change its shape, rendering the active site unreceptive to substrate, or leaving the enzyme less effective at catalyzing. Hence this option is correct.