SFP7: Enzyme Kinetics Flashcards

1
Q

Does an enzyme affect the kinetics or equilibrium of a reaction?

A

The kinetics of a reaction (NOT the equilibrium)

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2
Q

What is V0?

A

Initial velocity when substrate is added to reaction mixture

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3
Q

Describe the method of analysing the kinetics of enzyme catalysed reactions?

A

Collect data at constant enzyme concentration, several different [S], calculate initial rate (Vo) and plot Vo against [S]

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4
Q

What is the dependence of Vo on [S] known as?

A

Hyperbolic

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5
Q

What is Vmax?

A

Maximum velocity catalysed by a given enzyme concentration

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6
Q

What is Km?

A

The [S] which gives 1/2 Vmax

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7
Q

When [S]=Km, what does V0 equal?

A

V0= Vmax/2

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8
Q

What is the equation that relates Vo to Vmax and Km?

A

Vo= Vmax x ([S] / ([S] + Km))

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9
Q

What is the equation called that relates Vo to Vmax and Km?

A

Michaelis-menten equation

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10
Q

What units does Km have?

A

Concentration units

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11
Q

What information does the michaelis constant give (Km)?

A

The affinity of an enzyme for its substrate

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12
Q

What does high Km mean?

A

Relatively weak substrate binding

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13
Q

Explain the example of alcohol metabolism with importance of Km?

A

most people produce a low Km (high affinity) aldehyde dehydrogenase to break down acetaldehyde efficiently
However some people produce a high Km (low affinity) form of aldehyde dehydrogenase , leads to facial flushing and tachycardia

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14
Q

What is the kCat?

A

A turnover number or molecular activity (molecules of substrate transformed per unit time (usually given as per second))

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15
Q

What value(s) are useful for comparing two enzymes?

A

The enzyme turnover number (KCat), is a good indicator of efficiency

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16
Q

What value(s) are useful to analyse an individual enzyme?

A

Vmax and Km

17
Q

What does KCat equal with relation to Vmax and enzyme concentration

A

KCat= Vmax/[E]