Lecture 11 - measuring and comparing the activity of enzymes Flashcards

1
Q

what does a progress curve measure

A

it measures the appearance of product or the disappearance of substrate

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2
Q

what velocity must you always use on a progress curve

A

initial reaction velocity

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3
Q

what will happen when there is a fixed amount of enzyme, as the substrate increases the reaction rate will

A

increase in a linear way at first

but as all active sites become occupied = rate of reaction stops increasing

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4
Q

what is the Vmax

A

maximum velocity possible, when substrate is in excess

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5
Q

what is the Km

A

the substrate concentration at which V = Vmax / 2

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6
Q

what does a small Km mean

A

it needs very little substrate to reach half velocity

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7
Q

what are the Michaelis Menten assumptions

A
  • product is not converted back to substrate
  • by measuring the initial rate, (S) does not change
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8
Q

on the Lineweaver-Burk plot what is the Y intercept

A

1/Vmax

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9
Q

on the Lineweaver-Burk plot what is the X intercept

A

-1/Km

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10
Q

on the Lineweaver-Burk plot what is the slope curve

A

Km/Vmax

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11
Q

what are the units of Km

A

same as concentration e.g mmol/L

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12
Q

if an enzyme can act on different substrates will the Km for each be the same or different

A

each substrate that it acts on will have a different Km

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13
Q

what does a high Km mean

A

low affinity for substrate

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14
Q

what does a low Km mean

A

high affinity for substrate

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15
Q

what is the Kcat (turnover number)

A

the number of substrate molecules converted to product, per enzyme, per unit time, when E is saturated with substrate

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16
Q

what does Kcat help to define

A

the activity of one enzyme molecule measure of catalytic activity

17
Q

what is Kcat equal to

A

Vmax/E

18
Q

peak enzyme should have

A

a high Kcat = ability to turnover a lot of substrate into product per second

a low Km = low substrate concentration required to get up to speed, high affinity for the substrate