Types of Enzyme Inhibition

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Last updated 9:02 PM on 8/27/26
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5 Terms

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Competitive Inhibition

Definition: Competes with the substrate for binding at the active site.

Effect on V max: No Change.

Effect on Km Apparent: Increases.

binds : enzyme

<p>Definition: Competes with the substrate for binding at the active site.</p><p>Effect on V max: No Change.</p><p>Effect on Km Apparent: Increases.</p><p>binds : enzyme</p>
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Non-Competitive Inhibition

Definition: Inhibitor binds at an allosteric site, not at the active site.

Effect on V max: Decreases.

Effect on Km Apparent: No Change.

binds : enzyme + ES complex with equal affinity (allosteric)

<p>Definition: Inhibitor binds at an allosteric site, not at the active site.</p><p>Effect on V max: Decreases.</p><p>Effect on Km Apparent: No Change.</p><p>binds : enzyme + ES complex with equal affinity (allosteric)</p>
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Uncompetitive Inhibition

Definition: An inhibitor is only able to bind to the enzyme-substrate complex - that is, it cannot bind before the substrate has bound.

Effect on V max: Decreases.

Effect on Km Apparent: Decreases.

binds : ES complex (only allosteric site)

<p>Definition: An inhibitor is only able to bind to the enzyme-substrate complex - that is, it cannot bind before the substrate has bound.</p><p>Effect on V max: Decreases.</p><p>Effect on Km Apparent: Decreases.</p><p>binds : ES complex (only allosteric site)</p>
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Mixed-Type Inhibition

Definition: Occurs when an inhibitor can bind to either the unoccupied enzyme or the enzyme-substrate complex.

Effect on V max: Decreases.

Effect on Km Apparent: Km apparent Increases if the enzyme has greater affinity for the inhibitor in its free form.

Km apparent Decreases if the enzyme-substrate complex has greater affinity for the inhibitor.

binds : E + ES (unequal affinity) allosteric site

<p>Definition: Occurs when an inhibitor can bind to either the unoccupied enzyme or the enzyme-substrate complex.</p><p>Effect on V max: Decreases.</p><p>Effect on Km Apparent: Km apparent <strong>Increases </strong>if the enzyme has greater affinity for the <u>inhibitor in its free form.</u></p><p> Km apparent <strong>Decreases </strong>if the enzyme-substrate complex has greater affinity for the <u>inhibitor</u>.</p><p>binds : E + ES (unequal affinity) allosteric site</p>
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