Lecture 9 Flashcards

1
Q

How do enzymes work as catalysts?

A

By providing an alternate path of lower activation energy

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2
Q

What is a progress curve?

A

A curve displaying the measures of the appearance of produce (or disappearance of substrate) with time

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3
Q

Where is velocity measured from on a progress curve?

A

From the linear proportion; initial velocity

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4
Q

Why can the parabolic portion of a progress curve not be used to measure velocity?

A

There are too many unknowns

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5
Q

What is the relationship between enzyme and velocity?

A

Linearly proportional

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6
Q

What are the effects of an infinite substrate concentration?

A

Increases in a linear way however as all active sites within the enzyme become occupied, the ROR stops increasing = Vmax

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7
Q

What order of reaction is the linear portion of the progress curve?

A

First order, rate is dependent upon substrate concentration

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8
Q

What order of reaction is the parabolic portion of the progress curve?

A

Zeroth order, rate is not dependent on substrate concentration

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9
Q

How can Vmax be increased?

A

By adding more enzyme and therefore more active sites

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10
Q

What is the Michaelis constant?

A

Km; the substrate concentration required to generate half the Vmax

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11
Q

What is the Michaelis-Menten equation?

A

V = Vmax [S] / Km + [S]

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12
Q

What are the simplifying assumptions of Michaelis-Menten model?

A

Product is not converted back to substrate, Haldane’s steady-state assumption, only measuring initial ROR means that [S] does not change over time ( [S] > [E] )

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13
Q

What is Haldane’s steady-state assumption?

A

The rate of ES complex formation is equal to the rate of its breakdown d[ES] / d t = 0

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14
Q

What is the Lineweaver-Burk plot

A

Plotting the inverse of the Michaelis parabolic plot to get a linear plot

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15
Q

What is the y-intercept of the Lineweaver-Burk plot?

A

1 / Vmax

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16
Q

What is the x-intercept of the Lineweaver-Burk plot?

17
Q

What is the slope of the Lineweaver-Burk plot?

18
Q

What are the units of Km

A

Concentration so; mmol / L

19
Q

What does a low Km relate to?

A

High affinity for bonding to that particular substrate

20
Q

What does a high Km relate to?

A

Low affinity for bonding to that particular substrate

21
Q

In a cell, what is the typical range of [S]?

A

Often around or below the Km value, meaning that rate control is effective and substrates aren’t queuing for active sites

22
Q

What is Kcat?

Definition

A

The turnover number; the number of substrate molecules converted to product, per enzyme, per time

23
Q

What conditions is Kcat measured under?

A

Enzyme is saturated with substrate

24
Q

What is Kcat?

Measure of…

A

The catalytic activity of an individual enzyme molecule

25
What does k2 represent in terms of enzymes?
The rate of production of enzyme and product from ES (enzyme-substrate complex)
26
What value is Kcat equivalent to?
k2
27
What is the relationship between Kcat, Vmax and [E]?
Kcat = Vmax/[E]
28
What are the relative values of Kcat and Km that an enzyme must have to be highly catalytically efficient?
High Kcat, low Km
29
What ratio shows the efficiency of an enzyme?
Kcat/Km
30
If Kcat/Km is high, what is the efficiency of an enzyme?
High efficiency
31
If Kcat/Km is low, what is the efficiency of an enzyme?
Low efficiency