Enzyme Kinetics Flashcards

1
Q

Describe the term V

A

rate of the catalysed reaction

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2
Q

Describe the term Vmax

A

Vmax is the maximum velocity or rate at which the enzyme catalyzed a reaction. It happens when all enzyme active sites are saturated with substrate

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3
Q

Describe the term k

A

rate constant of the reacion

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4
Q

Describe the term k1

A

the forward rate constant for enzyme association with the substrate

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5
Q

Describe the term k-1

A

the backward rate constant for enzyme dissociation from the substrate

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6
Q

Describe the term k2

A

the forward rate constant of enzyme conversion of substrate to product

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7
Q

Give the equation for the term Km, Michaelis constant

A

k-1+k2/k1

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8
Q

What is the Michaelis constant Km equivalent to?

A

Km is equivalent to the substrate concentration where the initial reaction rate is half-maximal ([S] = 0.5 Vmax)

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9
Q

What is Km roughly a measure of?

A

The inverse measure of the affinity or strength of binding between the enzyme and its substrate

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10
Q

What units is Km measured in?

A

mol l-1

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11
Q

What does a low Km indicate?

A

A greater affinity for substrate to bind to enzyme - needs little substrate to work at half maximal velocity

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12
Q

Why are hyperbolic graphs not a good way of measuring Km and Vmax?

A

as they are not linear, reaction velocity will never quite reach true Vmax!!

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13
Q

What is the most widely used and most precise method of linearising the data of the equation?

A

Lineweaver-Burk plot

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14
Q

What does a high Km indicate?

A

Low affinity for substrate to bind to enzyme - enzyme needs a lot of substrate to work at half maximal velocity

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15
Q

What is the Michaelis-Menten Equation?

A

V0 = Vmax [S] / Km + [S]

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16
Q

What happens to the Km and Vmax on a Lineweaver-Burk Plot during COMPETITIVE inhibition?

A

INCREASED Km, NO CHANGE Vmax

17
Q

What happens to the Km and Vmax on a Lineweaver-Burk Plot during NON-COMPETITIVE (mixed) inhibition?

A

NO CHANGE Km, DECREASED Vmax

18
Q

What is inhibition of rate limiting enzymes by end products and common mechanism of?

A

Allosteric Control

19
Q

What do allosteric enzymes not follow?

A

Michaelis-Menten kinetics

20
Q

What is an important example of allosteric regulation?

A

Binding of oxygen to haemoglobin