Enzyme Kinetics And Inhibition Flashcards

1
Q

How do enzymes increase the rate of reaction?

A

Lower activation energy of the reaction

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2
Q

Give 6 key features of Enzymes

A
Proteins
Specific 
No effect on equilibrium 
Increase rate of reaction 
Unchanged after reaction 
Cofactors may be required
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3
Q

Define active site

A

Place where substances bind and the chemical reaction occurs
Few aa’s long
Exclude water

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4
Q

What are the two models for enzyme substrate interaction at active site

A

Induced fit

Lock and key

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5
Q

Describe relationship between [S] and rate.

A

Rate increases until enzyme saturated

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6
Q

What effect does increased the concentration of enzyme have on maximal velocity?

A

Increases it

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7
Q

Define enzyme activity

A

Decrease in [s] /unit time

Increase in[p]/ unit time

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8
Q

Define Vmax

A

Maximal rate when all enzymes are saturated with substrate

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9
Q

Define Km

A

Substrate concentration that gives half the maximal velocity

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10
Q

What is the international uni of enzyme activity?

A

The amount of enzyme that converts 1 umole of substance per minute under standard conditions

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11
Q

How do you work out rate from graph?

A

Gradient at time =0 on time vs product graph

only time [S] is known

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12
Q

What is a Km a measure of?

A

Affinity of enzyme for it substrate
Low km= high affinity
High km = low affinity

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13
Q

What does the x intercept of a line weaver Burke plot show?

A

-1/Km

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14
Q

What does the y intercept of a lineweaver Burke plot show?

A

1/Vmax

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15
Q

What is the effect of a competitive inhibitor on Vmax and km?

A

Vmax remains the same

Km increases

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16
Q

What is the effect of a non-competitive inhibitor on km and Vmax?

A

Km the same

Vmax changes