Enzyme inhibitions

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Last updated 10:51 AM on 7/29/26
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20 Terms

1
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What is competitive inhibition?

Inhibitor competes with substrates for binding to the active site.

2
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How does an inhibitor affect Vmax in competitive inhibition?

Vmax remains the same; the slope of the Lineweaver-Burk plot increases.

3
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What happens to Km in competitive inhibition?

Km increases; the inhibitor is similar in structure to the substrate.

4
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What is uncompetitive inhibition?

Inhibitor binds only to the ES complex, not the free enzyme.

5
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How does uncompetitive inhibition affect Vmax?

Vmax decreases as the concentration of inhibitor increases.

6
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What is the effect of uncompetitive inhibition on Km?

Km decreases; the inhibitor distorts the active site.

7
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What is mixed inhibition?

Inhibitor can bind to either the enzyme (E) or the enzyme-substrate complex (ES).

8
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How does mixed inhibition affect Vmax?

Vmax decreases as the concentration of inhibitor increases.

9
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What happens to Km in mixed inhibition?

Km increases; the ratio of Km/Vmax changes.

10
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What is allosteric inhibition?

Inhibition that occurs when an inhibitor binds to a site other than the active site.

11
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What is the role of end product inhibition?

End products control their own rate of production through negative feedback.

12
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What are isoenzymes?

Different forms of an enzyme that catalyze the same reaction in different tissues.

13
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How do isoenzymes differ?

They have slight variations in the amino acid sequences of their quaternary structure.

14
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What is the significance of maintaining high inhibitor concentration in competitive inhibition?

It ensures effective inhibition by reducing the availability of free enzyme for substrate binding.

15
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What is the effect of increasing inhibitor concentration on Vmax in uncompetitive inhibition?

Vmax is lowered, and the y-intercept of the Lineweaver-Burk plot increases.

16
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What is the relationship between Km and Vmax in uncompetitive inhibition?

The ratio of Km/Vmax remains the same despite changes in both values.

17
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Identify the type of inhibitor: 'Inhibition is not reversed with substrate.'

Noncompetitive inhibitor.

18
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Identify the type of inhibitor: 'Increasing substrate reverses inhibition.'

Competitive inhibitor.

19
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Identify the type of inhibitor: 'Binds to enzyme, not active site.'

Noncompetitive inhibitor.

20
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Identify the type of inhibitor: 'Structure is similar to substrate.'

Competitive inhibitor.