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?

A

-1 / Km

17
Q

What is the slope of the Lineweaver-Burk plot?

A

Km / Vmax

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
Q

What does k2 represent in terms of enzymes?

A

The rate of production of enzyme and product from ES (enzyme-substrate complex)

26
Q

What value is Kcat equivalent to?

A

k2

27
Q

What is the relationship between Kcat, Vmax and [E]?

A

Kcat = Vmax/[E]

28
Q

What are the relative values of Kcat and Km that an enzyme must have to be highly catalytically efficient?

A

High Kcat, low Km

29
Q

What ratio shows the efficiency of an enzyme?

A

Kcat/Km

30
Q

If Kcat/Km is high, what is the efficiency of an enzyme?

A

High efficiency

31
Q

If Kcat/Km is low, what is the efficiency of an enzyme?

A

Low efficiency