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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 Preview

    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 ...

    Solution Summary

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