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Enzymes, Inhibition and Allosteric Control

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An enzyme and its substrate are combined in a test tube but no product is formed. Another molecule is added to the tube, and now the product is formed at the normal rate. Give 2 reasons.

This has to do with inhibition, but how do I know what kind of inhibition is working on the substrate?

If an allosteric control was added to the tube, it could turn on the enzyme and make it produce a product.

Is it true that another thing that could make the product start forming is if a Reversible competitive inhibitor was added, because the inhibition will drop off.

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Solution Summary

This response discusses the effect of adding allosteric control to a tube of an enzyme and its substrate.

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Allosteric control is the most common scenario in this case.

When an allosteric activator is not bound to the regulatory site of an enzyme, the ...

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