Question

Malonate is a competitive inhibitor of an enzyme…………...

Answer 1

Hint: The binding of succinic dehydrogenase to the substrate, succinate, is competitively inhibited. This happens because its chemistry is similar to succinate. It happens with the ability to inhibit the binding of the enzyme and substrate. It binds to the active site of succinic dehydrogenase so that succinate cannot. Thus, it inhibits the reaction.

Complete answer:
Competitive inhibition may be a sort of enzyme inhibition where binding of the inhibitor to the site on the enzyme prevents binding of the substrate and the other way around. Malonate is a competitive inhibitor of the compound ‘succinate dehydrogenase’: malonate attaches to the dynamic site of the enzyme without responding, thus rivals succinate, the typical substrate of the enzyme.
Competitive inhibitors are commonly used to make pharmaceuticals. For example, methotrexate is a chemotherapy drug that acts as a competitive inhibitor. It is structurally almost like the coenzyme, folate, which binds to the enzyme dihydrofolate reductase. This chemical is important for the formation of DNA and RNA, and when methotrexate ties the protein, it renders it latent, so it can't blend DNA and RNA. Another example: prostaglandin is made in large amounts as a response to pain and may cause inflammation. Essential fatty acids form the prostaglandins; when this was discovered, it clothed that these were actually excellent inhibitors to prostaglandins. These unsaturated fats inhibitors have been utilized as medications to alleviate torment since they can go about as the substrate, and tie to the chemical, and block prostaglandins.

So the correct answer is ‘Succinate dehydrogenase’.

Note:
Most competitive inhibitors function by binding reversibly to the active site of the enzyme. As a result, many sources state that this is often the defining feature of competitive inhibitors. This, notwithstanding, might be a deceptive distortion, as there are numerous potential components by which an enzyme may bind either the inhibitor or the substrate however never both at an identical time. For instance, allosteric inhibitors may show competitive, non-competitive, or uncompetitive inhibition.