Lecture 13 - Enzyme Kinetics Flashcards

1
Q

Reaction order when ln[S] is linear.

A

First order kinetics

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2
Q

Reaction order when 1/[S] is linear.

A

Second order kinetics

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3
Q

Reaction order when [S] is linear.

A

Zero order kinetics

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4
Q

Why would substrate be independent of enzyme (i.e. what explains zero order kinetics)?

A

Unimolecular reaction or enzyme is saturated

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5
Q

Variable, [S] where reaction rate is half maximal OR half of the active sites are full

A

Km, Michaelis Constant

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6
Q

Variable, maximum rate possible for a given concentration of enzyme.

A

Vman, Maximum velocity

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7
Q

Variable, number of substrate molecules converted per active site pet time (first order rate constant).

A

kcat, Turnover number

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8
Q

Variable, a dissociation constant for substrate binding.

A

KS

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9
Q

Variable, measure of enzyme performance by predicting the fate of E*S.

A

kcat/Km, Specificity constant

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10
Q

Assumptions of Michaelis-Menten equation.

A

Binding of substrate is at equilibrium allowing us to define an equilibrium constant and steady state (i.e. [S] >> [E], change in S = 0)

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11
Q

Equation, Michaelis-Menten

A
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12
Q

Lab conditions where…

A

[S] < Km

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13
Q

Lab conditions where…

A

[S] = Km

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14
Q

Lab conditions where…

A

[S] >> Km

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15
Q

Enzyme is […] when kcat >> k-1 and kcat/Km ~ k1

A

Good

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16
Q

Enzyme is […] when kcat << k-1 and kcat/Km ~ 1/Km

A

Poor

17
Q

Multiple binding site enzymes can follow Michaelis-Mentin kinetics, as long as they are […].

A

Noncooperative

18
Q

Slope of Linewaever-Burk plot.

A

KM/Vmax

19
Q

Y-intercept of Lineweaver-Burk plot.

A

1/Vmax

20
Q

X-intercept of Lineweaver-Burk plot.

A

-1/KM

21
Q

Competitive inhibition: vmax = […] and Km = […].

A

Constant; Variable

22
Q

Noncompetitive inhibition: vmax = […] and Km = […].

A

Variable; Constant

23
Q

Uncompetitive inhibition: vmax = […] and Km = […].

A

Variable; Variable

24
Q

Inhibition depicted

A

Noncompetitive inhibition

25
Q

Inhibition depicted.

A

Uncompetitive inhibition

26
Q

Irreversible inhibitor, targets a specific amino acid.

A

Group-specific

27
Q

Irreversible inhibitor, substrate mimic, modifies enzymes.

A

Substrate analogs

28
Q

Irreversible inhibitor, modified substrate so is unable to form products.

A

Suicide inhibitors

29
Q

Group-specific irreversible inhibition has […] affinity.

A

Low

30
Q

Substrate analogs irreversible inhibition has […] affinity.

A

High

31
Q

Suicide inhibitors irreversible inhibition has […] affinity.

A

Very high