An allosteric inhibitor is converted to an activator by the enzyme. - increases the rate of substrate binding. - binds and activates the high-affinity state of the enzymes. - is identical to the active site. - binds at the regulatory site.

Question

Chemistry

Micaela Huang

12 February, 00:48

An allosteric inhibitor is converted to an activator by the enzyme. - increases the rate of substrate binding. - binds and activates the high-affinity state of the enzymes. - is identical to the active site. - binds at the regulatory site.

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Yamilet · Answer 1

An allosteric inhibitor binds at the regulatory site of a particular enzyme

Explanation:

An allosteric inhibitor is not converted to an activator. It does not bind the enzyme active site. Active site is different from regulatory site.

An inhibitor that binds the enzyme active site is called competitive inhibitor