The statement which is incorrect with respect to enzyme action is

The correct option is: Addition of a lot of succinates does not reverse the inhibition of succinic dehydrogenase by malonate.

Here is a step-by-step educational breakdown of enzyme inhibition and why this statement is incorrect:

1. Concept of Competitive Inhibition:
In competitive inhibition, an inhibitor structurally resembles the substrate of the enzyme. Because of this similarity, the inhibitor competes directly with the substrate for binding at the active site of the enzyme.

2. The Relationship Between Succinate and Malonate:
Succinic dehydrogenase is an enzyme that catalyzes the conversion of succinate (the substrate) into fumarate. Malonate is a structural analog of succinate, meaning it has a very similar molecular structure. Because of this, malonate acts as a competitive inhibitor of succinic dehydrogenase by binding to its active site. This makes the statement "malonate is a competitive inhibitor of succinic dehydrogenase" biologically correct.

3. Reversal of Competitive Inhibition:
Because competitive inhibitors compete with substrate molecules for the exact same active site, the inhibition can be overcome by increasing the concentration of the substrate. When a large excess of succinate (substrate) is added, the probability of a succinate molecule binding to the active site becomes much higher than that of a malonate molecule. Therefore, adding a lot of succinate successfully reverses the inhibition. This shows that the statement "Addition of a lot of succinates does not reverse the inhibition of succinic dehydrogenase by malonate" is incorrect, making it the correct answer to the question.

4. Verifying the Remaining Options:
- The statement "the substrate binds with the enzyme as its active site" (at its active site) is correct because the active site is the specific pocket on the enzyme designed to bind the substrate.
- The statement "a non-competitive inhibitor binds the enzyme at a site distinct from that which binds the substrate" is correct because non-competitive inhibitors bind to a separate regulatory or allosteric site rather than competing for the active site.