It was found that a reversible inhibitor and a substrate bind an enzyme, but at different sites. The inhibitor was quite potent at reducing enzyme activity, but an analysis indicated it could not actually bind the enzyme unless the substrate was bound first. These results led to what conclusion?

Question

Kyan Grimes

Biology

10 February, 20:55

It was found that a reversible inhibitor and a substrate bind an enzyme, but at different sites. The inhibitor was quite potent at reducing enzyme activity, but an analysis indicated it could not actually bind the enzyme unless the substrate was bound first. These results led to what conclusion?

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Answers (1)

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Romeo · Answer 1

Uncompetitive inhibitor

Explanation:

There are two types of inhibitors: reversible (can detach enzyme) and irreversible (can't detach enzyme).

Exist three types of reversible inhibitors: competitive inhibitors (inhibitor binds free enzyme, usually has the same shape as the substrate, and substrate cant binds enzyme), non-competitive inhibitors (inhibitors bind the enzyme at a different site of substrate and change the enzyme conformation) and uncompetitive inhibitor (inhibitors bind the complex enzyme-substrate).

In this case, is an uncompetitive inhibitor, because we know that inhibitor is reversible, and the substrate must be bind with the enzyme so the uncompetitive inhibitor bind to the complex and stop the enzymatic activity. If the enzyme and the substrate are not together, the inhbitor can't bind the enzyme.