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Biochemistry > Lecture 13, Kinetics (Ford) > Flashcards

Lecture 13, Kinetics (Ford) Flashcards

1
Q

List the 3 kinetic trends that are possible.

A

Linear, hyperbolic, sigmoidal

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2
Q

What is the equation for a linear kinetic trend?

A

v = k[S]

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3
Q

What is the equation for a hyperbolic kinetic trend?

A

v0 = (vmax*[S]) / (Km + [S])

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4
Q

What is the equation for a sigmoidal kinetic trend?

A

v = [S]^n / KD + [S]^n

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5
Q

How do you determine the reaction order based on the graph?

A

Linear line (k is the absolute value of the slope of the line)

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6
Q

Describe the linear graph for first order kinetics.

A

ln[S] vs. time

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7
Q

Describe the linear graph for second order kinetics.

A

1/[S] vs. time

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8
Q

Describe the linear graph for zero order kinetics.

A

[S] vs. time

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9
Q

What are the substrate-independent interpretations of a zero order reaction?

A

Unimolecular reaction and enzyme is saturated

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10
Q

T or F: For a reversible reaction, the substrate is being both used and created.

A

True.

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11
Q

What is the equation for a reversible reaction at equilibrium?

A

k1[S] = k-1[P]

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12
Q

For a reversible reaction, how can the association and dissociation constants be redefined?

A 
KA = k1/k-1
KD = 1/KA
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13
Q

T or F: No matter what, catalysis is a first order reaction.

A

False. Michaelis-Menten enzymes follow first order kinetics, but not matter what, catalysis is not a first order reaction.

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14
Q

How can reaction rate a catalysis be simplified if we make some assumptions?

A

E + S ← → E * S → E + P

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15
Q

When reaction rate is simplified, describe the changes in concentration.

A

Linear

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16
Q

T or F: [E] cannot be measured.

A

True.

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17
Q

Moving toward a Michaelis-Menten equation and assuming that the binding of the substrate is at equilibrium, how can the equilibrium constant be defined?

A

KS = KD; KS = k-1/k1

18
Q

Regarding reaction rate simplification, what is the steady state assumption?

A

[S]&raquo_space; [E]

19
Q

Regarding reaction rate simplification, describe the formation of the E*S complex.

A

Formation occurs at the same rate as its loss

20
Q

What is the rate-determining step when simplifying the reaction rate?

A

k2

21
Q

Since k2 is the rate-determining step, what is the rate of product formation?

A

v0 = kcat * [E*S]

22
Q

Why can’t [E*S] be meaured?

A

Transient and unstable

23
Q

What does it mean when vmax is reached?

A

Enzyme is fully saturated; [E*S] = [E]T

24
Q

Describe the kcat of a good enzyme.

A

kcat&raquo_space; k-1; kcat/Km ~ k1

25
Q

Describe the kcat of a poor enzyme.

A

kcat &laquo_space;k-1; kcat/Km ~ 1/Km

26
Q

T or F: Multiple binding site enzymes can follow Michaelis-Menten kinetics, whether they are cooperative or noncooperative.

A

False. Multiple binding site enzymes can follow Michaelis-Menten kinetics, as long as they are noncooperative.

27
Q

What is the equation for a Lineweaver-Burk plot?

A

1/v0 = Km/vmax * 1/[S]0 + 1/vmax

28
Q

T or F: Inhibitors can be reversible or irreversible.

A

True.

29
Q

What kind of bonds do reversible inhibitors utilize?

A

Noncovalent interactions

30
Q

What are the types of inhibition reversible inhibitors use?

A

Competitive, noncompetitive, uncompetitve

31
Q

Which of the reversible inhibitors are allosteric?

A

Noncompetitive, uncompetitive

32
Q

Describe the vmax and Km of competitive inhibitors.

A 
vmax = constant
Km = variable
33
Q

Describe the vmax and Km of noncompetitive inhibitors.

A 
vmax = variable
Km = constant
34
Q

Describe the vmax and Km of uncompetitive inhibitors.

A 
vmax = variable
Km = variable
35
Q

What does the graph for a competitive inhibitor look like?

A

Chopsticks

36
Q

What does the graph for a noncompetitive inhibitor look like?

A

V

37
Q

What does the graph for a uncompetitive inhibitor look like?

A

Railroad tracks

38
Q

What do irreversible inhibitors do?

A

Inactivate enzymes

39
Q

What do group-specific irreversible inhibitors target?

A

Specific amino acid (low specificity)

40
Q

What do substrate analog irreversible inhibitors target?

A

Substrate mimic, modifies enzyme (high specificity)

41
Q

What do suicide inhibitor irreversible inhibitors target?

A

Substrate mimic, unable to form products (very high specificity)

Biochemistry (10 decks)

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