Enzymes Flashcards

1
Q

What is thermodynamics?

A

The study of energy and its transformations.

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2
Q

What are exergonic reactions?

A

Energy-releasing reactions.

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3
Q

What are endergonic reactions?

A

Energy-requiring reactions.

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4
Q

What does thermodynamics tell us about a reaction?

A

Whether a reaction can occur, but not how fast it will happen.

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5
Q

What is activation energy (Ea)?

A

The energy needed to start a reaction

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6
Q

Why don’t spontaneous reactions always happen quickly?

A

Because reaching the activation energy is rare.

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7
Q

How do enzymes affect activation energy?

A

Enzymes lower the activation energy needed for reactions.

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8
Q

What role do enzymes play in biological systems?

A

They act as catalysts to speed up reactions without being consumed.

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9
Q

Do enzymes change the overall free energy change (ΔG) of a reaction?

A

No, enzymes do not change the overall free energy change of a reaction.

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10
Q

What is enzyme specificity?

A

The concept that each enzyme catalyzes only particular reactions.

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11
Q

What is the induced-fit hypothesis?

A

The idea that enzymes adjust their shape to bind substrates more precisely.

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12
Q

What happens to enzymes after the reaction?

A

They are released unchanged and ready to catalyze more reactions.

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13
Q

What are cofactors?

A

Non-protein molecules essential for enzyme activity.

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14
Q

How do enzymes bring reactants together?

A

By binding reactants in the right orientation for the reaction.

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15
Q

How do enzymes strain reactant bonds?

A

By putting stress on bonds, making them easier to break.

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16
Q

What favorable microenvironments do enzymes create?

A

Enzymes provide an environment conducive to the reaction.

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17
Q

What is ATP’s role in reactions?

A

ATP typically provides the energy in coupled reactions.

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18
Q

What are some factors that influence enzyme activity?

A

Substrate concentration, molecule interactions, temperature, and pH.

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19
Q

How does enzyme concentration affect the reaction rate?

A

With excess substrate, the reaction rate is proportional to enzyme concentration.

20
Q

What happens to the reaction rate as substrate concentration increases?

A

The reaction rate increases until enzymes become saturated.

21
Q

What are competitive inhibitors?

A

Molecules that resemble the substrate and bind to the enzyme’s active site, reducing the reaction rate.

22
Q

Can competitive inhibition be overcome?

A

Yes, by increasing substrate concentration (if the inhibition is reversible).

23
Q

What are noncompetitive inhibitors?

A

Molecules that bind to an allosteric site on the enzyme, altering its function without competing with the substrate.

24
Q

How do noncompetitive inhibitors affect enzyme activity?
.

A

They can either increase or decrease enzyme activity

25
What is feedback inhibition?
A regulatory mechanism where the product of a reaction inhibits the enzyme that produces it.
26
Give an example of feedback inhibition.
The synthesis of isoleucine from threonine, where isoleucine inhibits the first enzyme in the pathway.
27
What is the optimal temperature for enzyme activity?
The temperature at which an enzyme functions most efficiently.
28
What happens to enzyme activity at temperatures above the optimal range?
Enzyme activity declines rapidly as enzymes can denature.
29
How does pH affect enzyme activity?
Each enzyme has an optimal pH, and deviation from this pH can reduce its activity.
30
What can extreme changes in pH do to an enzyme?
They can alter the enzyme's structure and function, reducing its activity.
31
Why is understanding enzyme regulation important?
It is crucial for controlling enzyme activity in biological and industrial processes.
32
What is activation energy?
The minimum amount of energy required for a chemical reaction to occur.
33
What is the active site of an enzyme?
The specific region where substrate molecules bind and undergo a chemical reaction.
34
How do enzymes affect activation energy?
Enzymes lower the activation energy, increasing the reaction rate.
35
What is allosteric regulation?
The regulation of an enzyme's activity through the binding of a regulatory molecule at a site other than the active site, known as the allosteric site.
36
What is an allosteric site?
A specific site on an enzyme, distinct from the active site, where a regulatory molecule can bind, inducing a conformational change in the enzyme.
37
What is a catalyst?
A substance that increases the rate of a chemical reaction without being consumed or permanently altered.
38
What is a coenzyme?
A non-protein organic molecule that binds to an enzyme and is essential for its activity, often acting as a carrier during the enzymatic reaction.
39
What is a cofactor?
A non-protein chemical compound or metallic ion required for an enzyme's activity, assisting in the proper functioning of the enzyme.
40
What is competitive inhibition?
When a molecule similar to the substrate competes for binding at the enzyme's active site, reducing the enzyme's activity.
41
Can competitive inhibition be overcome?
Yes, by increasing the concentration of the substrate.
42
What is an enzyme?
A protein that acts as a biological catalyst, speeding up the rate of a chemical reaction without being consumed.
43
What is feedback inhibition?
A regulatory mechanism where the end product of a metabolic pathway inhibits an enzyme involved in its synthesis, preventing overproduction.
44
What is a substrate?
The specific reactant molecule that an enzyme acts upon during a biochemical reaction.
45
How do enzymes function as catalysts?
By lowering the activation energy required for the reaction to occur.
46
What happens at the enzyme's active site?
The substrate binds, forming an enzyme-substrate complex, and is converted into products.
47