Ch 6 Enzymes Flashcards

1
Q

What significant discovery did NASA announce on Jan. 29, 2025?

A

NASA discovered amino acids on asteroid Bennu

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

What are the ways to increase the rate of chemical reactions?

A
  • Increasing the temperature
  • Increasing the concentrations of the reacting substances
  • Adding a catalyst
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is a catalyst?

A

A substance that participates in the reaction yet returns to its original form

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

What are enzymes?

A

Catalysts used by living systems to increase the rates of chemical reactions

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

What is the active site of an enzyme?

A

A specific fraction of the structure where reactions take place

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

Most enzymes work under what conditions?

A

Mild conditions

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

True or False: Enzymes can operate under extreme temperatures and pressures.

A

False

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is activation energy (ΔG‡)?

A

Energy input needed to start the reaction

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

How do enzymes affect activation energy?

A

Enzymes lower the activation energy

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

What does a negative ΔG° indicate?

A

The reaction is spontaneous

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

What are the seven major classifications of enzymes?

A
  • Oxidoreductases
  • Transferases
  • Hydrolases
  • Lyases
  • Isomerases
  • Ligases
  • Translocases
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the difference between kinetics and thermodynamics?

A

Kinetics refers to the speed of a reaction, while thermodynamics refers to the direction and likelihood of a reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is stereospecificity in enzymes?

A

Most enzymes are very specific with respect to the stereochemistry of substrates

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is the lock-and-key model?

A

A model where the substrate binds to a portion of the enzyme with a complementary shape

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

What is the induced fit model?

A

Binding of the substrate induces a change in the conformation of the enzyme for a complementary fit

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

What are cofactors?

A

Substances that aid in catalysis, including metal ions and organic molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What are coenzymes?

A

Organic molecules that act as cofactors, often derived from vitamins

18
Q

What is acid-base catalysis?

A

A mechanism where a proton is transferred between the enzyme and the substrate

19
Q

What is covalent catalysis?

A

A mechanism where a covalent bond forms between the catalyst and the substrate during the transition state

20
Q

What is metal ion catalysis?

A

A mechanism where metal ions mediate oxidation-reduction reactions or promote reactivity

21
Q

What is the catalytic triad?

A

The hydrogen-bonded arrangement of Asp, His, and Ser residues in enzymes like chymotrypsin

22
Q

In the context of enzyme kinetics, what does [S] represent?

A

Substrate concentration

23
Q

What analogy is used to describe enzyme activity and velocity?

A

A monkey is like an enzyme and a peanut is like a substrate

24
Q

Fill in the blank: Enzymes often use _______ to aid in catalysis.

25
Q

What is enzyme kinetics?

A

How fast an enzyme catalyzes a reaction under a given set of conditions.

26
Q

How are rates of enzyme reactions measured?

A

In units of product produced or substrate consumed per time period, e.g., moles/unit time.

27
Q

What does Chymotrypsin catalyze?

A

The selective hydrolysis of peptide bonds, particularly at Phe and Tyr residues.

28
Q

What is the significance of color change in measuring chymotrypsin activity?

A

It indicates the rate of colored product formation.

29
Q

What is Vmax?

A

The maximum processing speed of the enzyme when it is saturated with substrate.

30
Q

Is Vmax a constant value?

A

No, it is dependent on the amount and type of enzyme.

31
Q

What describes the relationship between initial rate of an enzyme-catalyzed reaction and substrate concentration?

A

Many enzymes obey Michaelis–Menten kinetics.

32
Q

What characterizes a unimolecular reaction?

A

It has a velocity dependent on the concentration of only one substrate.

33
Q

What is the rate equation for a unimolecular reaction?

A

𝜈 = k [A], where k has units of sec–1.

34
Q

What characterizes a bimolecular reaction?

A

It has a velocity dependent on two substrate concentrations.

35
Q

What is the rate equation for a bimolecular reaction?

A

𝜈 = k [A] [B] or k [A]² or k [B]², where k has units of M–1 ⋅ sec–1.

36
Q

What does ‘steady state’ mean in enzyme kinetics?

A

It refers to a constant value of the enzyme-substrate complex (E∙S).

37
Q

Who developed enzyme kinetics?

A

Maud Menten, MD/PhD, around 1913 in Berlin.

38
Q

What does KM represent in enzyme kinetics?

A

The concentration of substrate at which half of the enzyme’s active sites are bound to substrate (½ Vmax).

39
Q

What does a high KM value indicate?

A

A low substrate affinity.

40
Q

What does a low KM value indicate?

A

A high substrate affinity.

41
Q

Fill in the blank: The maximum rate when the enzyme is saturated with substrate is called _______.

42
Q

If two enzymes have the same Vmax, how is the enzyme with a higher affinity for substrate determined?

A

The enzyme with the lower KM value has the higher affinity.