Enzyme Kinetics Flashcards

1
Q

Vo

A

The number of moles of product formed per second when the reaction is just beginning

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2
Q

Preconditions:

A
  1. At Vo [P]=0

2. [S]»[E]

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3
Q

Vo=

A

Vmax x [S] / [S] + KM

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4
Q

The Michaelis constant

A

KM is a measure of the affinity of the enzyme for its substrate

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5
Q

A low KM means

A

A high affinity of enzyme for substrate

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6
Q

Vmax is not

A

A constant

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7
Q

Catalytic constant =

A

kcat= Vmax/[Eo]

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8
Q

Kcat is a

A

turnover number

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9
Q

The specificity constant

A

kcat/KM -> describes catalytic efficiency of enzymes

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10
Q

High specificity constant

A

Better substrate for an enzyme

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11
Q

The Line-Weaver Burk Plot

A

1/Vo = KM/Vmax x 1/[S] + 1/Vmax

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12
Q

Reversible inhibition can be

A

Competitive or non-competitive

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13
Q

Irreversible inhibition can be

A

Non-competitive or uncompetitive

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14
Q

In competitive inhibition

A

KM increased, Vmax unaffected

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15
Q

In uncompetitive inhibition

A

KM reduced, Vmax reduced

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16
Q

In non-competitive inhibition

A

KM unaffected, Vmax reduced

17
Q

Slope in Line-Weaver

A

KM/Vmax

18
Q

Line-Weaver Burk Plot crosses Y axis at

A

1/Vmax

19
Q

Line-Weaver Burk Plot crosses X axis at

A

-1/KM

20
Q

How does excess substrate affect competitive inhibition?

A

Inhibition relieved

21
Q

Differences between significance of competitive and non-competitive inhibition?

A

Competitive - drug action

Non-competitive - toxicological