Enzymes Flashcards

1
Q

What is the active site formed from?

A

Different parts of the primary sequence - doesn’t have to be adjacent

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2
Q

Why are active sites in clefts?

A

To exclude H2O molecules

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3
Q

What type of bond is there between enzymes and substrates?
Give an example
Why?

A

Weak bonds - they are not covalent
H
Allows the products to be released

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4
Q

What does the Vmax mean?

A

Reaction rate when the enzyme is fully saturated by substrate

(The maximum rate)

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5
Q

What does Km mean?

A

Concentration of the substrate at which half of the active sites of the enzyme are occupied by the substrate

(Conc of enzymes at half Vmax)

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6
Q

What is 1 unit?

A

The amount of enzyme to produce 1umol of product per min under standard conditions

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7
Q

What is the rate of an enzyme catalysed reaction proportional to?

A

Concentration of enzymes

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8
Q

How would a competitive inhibitor effect the graph?

A

Km increases and Vmax unaffected
Adding enough substrate will overcome the effect of the inhibitor

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9
Q

How would a non-competitive inhibitor effect the graph?

A

Km unaffected and Vmax decreases
Lowers conc of effective enzymes

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10
Q

How is the kM related to affinity?

A

Lower the kM
Higher the affinity of an enzyme to the substrate

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11
Q

What affects the Vmax?

A

The enzyme conc - positively

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12
Q

What does a high level of creatine kinase suggest?

A

Muscle damage - cardiac or cellular

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13
Q

What is an irreversible inhibitor?

A

A substance that permanently blocks the action of an enzyme

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14
Q

On the special graph what axis is the Vmax and Km?
Which inhibitor affects them?

A

Vmax - y non-competitive
Km - x competitive

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