Enzyme Inhibitors Flashcards

1
Q

What are enzyme inhibitors?

A

Substances that bind to the enzyme to reduce enzyme activity.

Enzyme inhibitors can impede the function of enzymes, affecting metabolic processes.

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2
Q

What are the two types of enzyme inhibitors?

A
  • Competitive Inhibitors
  • Non-Competitive Inhibitors

Each type interacts with the enzyme differently.

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3
Q

Where do competitive inhibitors bind?

A

The active site.

Competitive inhibitors compete with the substrate for binding at this site.

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4
Q

What is the shape similarity of competitive inhibitors?

A

They have a similar shape to the substrate.

This allows them to bind to the active site, blocking substrate access.

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5
Q

What is the effect of competitive inhibitors on enzyme-substrate complexes?

A

Fewer enzyme-substrate complexes form.

This results in a reduced rate of reaction.

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6
Q

How can the effects of a competitive inhibitor be mitigated?

A

By adding more substrate.

Increasing substrate concentration can outcompete the inhibitor.

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7
Q

Where do non-competitive inhibitors bind?

A

The allosteric site.

Binding at this site alters the enzyme’s activity without competing with the substrate.

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8
Q

What happens to the active site when a non-competitive inhibitor binds?

A

The tertiary structure of the active site changes.

This change affects the enzyme’s ability to catalyze reactions.

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9
Q

What is the effect of non-competitive inhibitors on enzyme-substrate complexes?

A

Fewer or no enzyme-substrate complexes form.

This leads to a lower rate of reaction.

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10
Q

What is the effect of adding a non-competitive inhibitor?

A

Reduces the rate of reaction and reduces the maximum rate.

Unlike competitive inhibitors, increasing substrate concentration does not alleviate this effect.

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11
Q

What is the allosteric site?

A

The site on an enzyme where a non-substrate molecule can bind, changing the enzyme’s shape.

This binding can enhance or inhibit enzyme activity.

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12
Q

What role do activator molecules play in enzyme activity?

A

They bind to the allosteric site, changing the active site’s shape to be more substrate-like.

This increases the formation of enzyme-substrate complexes.

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