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BIOL 204 > Enzymes > Flashcards

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
Q

What is feedback inhibition?

A

A regulatory mechanism where the product of a reaction inhibits the enzyme that produces it.

26
Q

Give an example of feedback inhibition.

A

The synthesis of isoleucine from threonine, where isoleucine inhibits the first enzyme in the pathway.

27
Q

What is the optimal temperature for enzyme activity?

A

The temperature at which an enzyme functions most efficiently.

28
Q

What happens to enzyme activity at temperatures above the optimal range?

A

Enzyme activity declines rapidly as enzymes can denature.

29
Q

How does pH affect enzyme activity?

A

Each enzyme has an optimal pH, and deviation from this pH can reduce its activity.

30
Q

What can extreme changes in pH do to an enzyme?

A

They can alter the enzyme’s structure and function, reducing its activity.

31
Q

Why is understanding enzyme regulation important?

A

It is crucial for controlling enzyme activity in biological and industrial processes.

32
Q

What is activation energy?

A

The minimum amount of energy required for a chemical reaction to occur.

33
Q

What is the active site of an enzyme?

A

The specific region where substrate molecules bind and undergo a chemical reaction.

34
Q

How do enzymes affect activation energy?

A

Enzymes lower the activation energy, increasing the reaction rate.

35
Q

What is allosteric regulation?

A

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
Q

What is an allosteric site?

A

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
Q

What is a catalyst?

A

A substance that increases the rate of a chemical reaction without being consumed or permanently altered.

38
Q

What is a coenzyme?

A

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
Q

What is a cofactor?

A

A non-protein chemical compound or metallic ion required for an enzyme’s activity, assisting in the proper functioning of the enzyme.

40
Q

What is competitive inhibition?

A

When a molecule similar to the substrate competes for binding at the enzyme’s active site, reducing the enzyme’s activity.

41
Q

Can competitive inhibition be overcome?

A

Yes, by increasing the concentration of the substrate.

42
Q

What is an enzyme?

A

A protein that acts as a biological catalyst, speeding up the rate of a chemical reaction without being consumed.

43
Q

What is feedback inhibition?

A

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

44
Q

What is a substrate?

A

The specific reactant molecule that an enzyme acts upon during a biochemical reaction.

45
Q

How do enzymes function as catalysts?

A

By lowering the activation energy required for the reaction to occur.

46
Q

What happens at the enzyme’s active site?

A

The substrate binds, forming an enzyme-substrate complex, and is converted into products.

47
Q
A

BIOL 204 (6 decks)

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