W28 L2 - Enzyme Regulation and Inhibition

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Flashcards on enzyme regulation, effectors, and inhibitors based on lecture notes.

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12 Terms

1
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What are effectors in the context of enzyme regulation?

Substances that have an effect on enzymes, influencing their regulation.

2
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What defines a homotropic effector?

The effector is identical or very similar to the substrate.

  • A homotropic effector is a molecule that binds to an enzyme at the active site, facilitating the enzyme's activity in a manner similar to the substrate.

3
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How does substrate concentration affect reaction rate in Michaelis-Menten kinetics involving a homotropic effector?

The concentration of substrate directly influences the rate of the reaction; less substrate, slower rate; more substrate, faster rate up to Vmax.

4
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What is positive cooperativity in enzyme kinetics?

When a substrate binds to one subunit of an enzyme, it makes it easier for subsequent substrate molecules to bind to other subunits.

5
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What is substrate inhibition?

Too much substrate can decrease the reaction rate.

  • This is because the active site or regulatory sites of the enzyme become saturated

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What are heterotropic effectors?

Compounds that affect the enzyme but are not substrates.

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What is a competitive inhibitor?

An inhibitor that interacts exclusively with the free enzyme, preventing substrate binding.

8
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Why is it called a competitive inhibitor?

The inhibitor and substrate compete for the same binding site on the enzyme.

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What is product inhibition?

The product of the reaction acts as an inhibitor.

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What is an uncompetitive inhibitor?

An inhibitor that binds to the enzyme-substrate complex.

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What is a mixed inhibitor?

An inhibitor that can bind to either the free enzyme or the enzyme-substrate complex.

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What is a non-competitive inhibitor?

A mixed inhibitor with equal affinity for both the free enzyme and the enzyme-substrate complex, though likely doesn't exist in a true form