430-530-Lec 9-Enzyme Regulation 2025

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14 Terms

1
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What factors affect the rate of enzymatic reactions?

Enzyme concentration, cofactor concentration, substrate concentration, effectors/inhibitors, temperature, and pH.

2
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What happens to enzyme activity at different pH levels?

Changes in pH can alter active site chemistry and disrupt enzyme structure, potentially leading to denaturation.

3
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What is the optimal temperature for most human metabolic enzymes?

37 degrees Celsius.

4
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What is competitive inhibition?

A type of reversible inhibition where an inhibitor competes with the substrate for the active site, increasing apparent KM.

5
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How does non-competitive inhibition affect enzyme kinetics?

It decreases Vmax without affecting KM, as the inhibitor binds to a different site on the enzyme.

6
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What characterizes irreversible inhibitors?

They covalently bind to enzymes, permanently inactivating them.

7
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What is the significance of the Michaelis Constant (KM)?

It is the substrate concentration at which the reaction velocity is half of Vmax and indicates the enzyme’s affinity for a substrate.

8
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Define allosteric regulation of enzymes.

Allosteric regulation involves an effector molecule binding to a site other than the active site, modifying enzyme activity.

9
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What is feedback inhibition?

A regulatory mechanism where the end product of a metabolic pathway inhibits an enzyme involved in its synthesis.

10
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How can enzymes be regulated by covalent modifications?

Through modifications such as phosphorylation, which can activate, inhibit, or modulate enzyme activity.

11
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What happens during the activation of zymogens?

Inactive precursors are converted to active enzymes by proteolytic cleavage.

12
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What is a common characteristic of allosteric enzymes?

They often have multiple binding sites and do not follow Michaelis-Menten kinetics, exhibiting sigmoidal behavior.

13
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What is the role of cooperativity in allosteric enzymes?

Binding of a ligand to one site increases the affinity of other binding sites, a phenomenon known as positive cooperativity.

14
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Describe the actions of suicide inhibitors.

They are converted by the enzyme into a reactive form that then binds irreversibly to the enzyme, effectively inhibiting it.