H1 Biology and H2 Biology

What are the effects of competitive inhibitors on enzyme-catalysed reactions?

Notes from the video ‘H2 Biology Tuition | H1 Biology Tuition | Competitive Inhibitors’:


In this Biology tutorial, we would learn about the effects of competitive inhibitor on enzyme-catalysed enzymes.


A competitive inhibitor binds to the enzyme’s active site.


A competitive inhibitor has similar conformation and charge to the substrate molecule. A competitive inhibitor binds reversibly to an enzyme’s active site and competes with the substrate for the active site. This decreases the availability of active sites for substrate binding and leads to a reduction in the rate of formation of enzyme-substrate complexes, and hence, the rate of reaction.

At high substrate concentrations, the effects of the competitive inhibitors can be overcome. The higher portion of substrate molecules would be able to outcompete the competitive inhibitors for the active site to form enzyme-substrate molecules. At high substrate concentrations, the rate of reaction is the same as that when no competitive inhibitors are present.

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