Enzymes and Their Functions Flashcards

(32 cards)

1
Q

What role do catalysts play in chemical reactions?

A

Catalysts accelerate the rate of chemical reactions without changing the equilibrium.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Enzymes are categorized as what type of catalyst?

A

Biological catalysts (biocatalysts).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

How efficient are enzymes compared to typical catalysts?

A

One enzyme molecule can act on ~1000 substrates, making their catalysis extremely rapid.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What happens if an enzyme is missing in a metabolic pathway?

A

It blocks the pathway, halting the associated metabolic process.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the term for the reactant an enzyme acts on?

A

Substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Why are enzymes considered “highly specific”?

A

They typically act on only one substrate (e.g., lactase only breaks down lactose).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

List four key characteristics of enzymes.

A
  1. Mostly proteins.
  2. Water-soluble.
    3.Heat-labile (denature with heat).
    4.Contain 16% nitrogen by weight.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is the name of the site where a substrate binds to an enzyme?

A

Active site (or catalytic site).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What distinguishes a simple protein enzyme from a conjugated enzyme?

A

Simple enzymes are only proteins; conjugated enzymes have a protein (apoenzyme) and a non-protein part (cofactor).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What term describes the complete, functional form of a conjugated enzyme?

A

Holoenzyme (apoenzyme + cofactor)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are coenzymes often derived from?

A

Vitamin B derivatives.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Describe the two steps in the mechanism of enzyme action.

A
  1. Substrate binds to the enzyme’s active site, forming an enzyme-substrate (ES) complex.
  2. ES complex splits into products, releasing the original enzyme.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

List the five steps of an enzymatic reaction.

A
  1. Substrate approaches active site.
  2. ES complex forms.
  3. Substrate → products.
  4. Products released.
  5. Enzyme recycled.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What does the Lock and Key Theory state about enzyme-substrate binding?

A

The active site’s shape exactly fits the substrate, like a key in a lock (proposed by Emil Fischer

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

How does the Induced Fit Theory differ from Lock and Key?

A

The active site changes shape upon substrate binding for a better fit (proposed by Daniel Koshland).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Name the six classes of enzymes.

A
  1. Oxidoreductases
  2. Transferases
  3. Hydrolases
  4. Lyases
  5. Isomerases
  6. Ligases
17
Q

What is the function of hydrolases?

A

Catalyze hydrolysis reactions (break bonds using water).

18
Q

Which enzyme class joins molecules using ATP?

20
Q

Why might babies be lactose intolerant?

A

Temporary deficiency in lactase enzyme after weaning.

21
Q

What is a prosthetic group in enzymes?

A

A tightly bound, non-protein cofactor (e.g., heme in hemoglobin).

22
Q

What are enzymes?

A

Enzymes are proteins that act as biological catalysts, increasing the rate of chemical reactions without being consumed.

23
Q

What is a coenzyme?

A

A coenzyme is a small organic molecule that assists enzymes in facilitating chemical reactions, often derived from vitamins.

24
Q

What are the two main types of enzymes?

A

Simple enzymes (composed only of protein) and complex (conjugated) enzymes (composed of an apoenzyme and a cofactor).

25
What factors affect enzyme activity?
Temperature, pH, substrate concentration, and enzyme concentration.
26
What is enzyme inhibition?
Enzyme inhibition is the process by which a substance slows down or stops the normal catalytic function of an enzyme.
27
What are the types of enzyme inhibition?
1. Reversible Competitive Inhibition 2. Reversible Non-competitive Inhibition 3. Irreversible Inhibition
28
What is the difference between a cofactor and a coenzyme?
A cofactor is an inorganic ion (e.g., metal ions like Zn²⁺), while a coenzyme is an organic molecule (often derived from vitamins) that assists enzyme activity.
29
What is the significance of enzyme specificity?
Enzyme specificity refers to the ability of an enzyme to catalyze a reaction for only one substrate or a group of similar substrates, ensuring precise biochemical reactions.
30
What is the "Lock and Key" model of enzyme action?
The "Lock and Key" model suggests that the active site of the enzyme is a rigid structure that fits only a specific substrate, like a key fits into a lock.
31
What is the role of allosteric enzymes?
Allosteric enzymes have multiple binding sites and can be regulated by molecules that enhance or inhibit their activity, affecting the enzyme's overall function.
32
What are isoenzymes?
Isoenzymes are different forms of an enzyme that catalyze the same reaction but are found in different tissues, allowing for tissue-specific regulation.