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Inhibition of Succinic dehydrogenase enzyme by malonate is a classical example of:
Malonate closely resembles the substrate succinate in structure and competes for the active site of succinic dehydrogenase -> Classical Competitive Inhibition!
When the inhibitor closely resembles the substrate in its molecular structure and inhibits the activity of the enzyme by competing for the active binding site, it is known as competitive inhibition.
Inhibition of succinic dehydrogenase by malonate is the classic demonstration: malonate closely resembles succinate in chemical structure, binding to the active site and preventing succinate oxidation to fumarate.
Competitive inhibition can be overcome by increasing the concentration of the substrate (succinate).
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Malonate is a structural analog of succinate that competitively occupies the active site of succinic dehydrogenase.
Non-competitive inhibitors bind to an allosteric site distinct from the substrate active site.
Allosteric inhibition involves conformational changes induced by binding at a regulatory site.
Feedback inhibition occurs when the end product of a metabolic pathway inhibits an upstream pathway enzyme.
Assuming malonate destroys the enzyme permanently.
"When the inhibitor closely resembles the substrate in its molecular structure and inhibits the activity of the enzyme, it is known as competitive inhibitor... Inhibition of succinic dehydrogenase by malonate which closely resembles the substrate succinate in structure is an example."
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