MDG S2 Flashcards

1
Q

Define Allosterism

A

The binding of a substrate to at one site of a multisubunit protein that influences the subsequent binding of other substrates to other subunits

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2
Q

Give an example of Allosterism

A

Haemoglobin - when oxygen binds to one subunit, it increases the oxygen affinity of the next subunit

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3
Q

What is competitive inhibition?

A

Where the inhibitor non-permanently binds to the enzyme at the substrate binding site to lower enzyme activity

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4
Q

How does competitive inhibition affect Vmax and Km?

A

Vmax is unaffected but Km increases

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5
Q

What is non-competitive inhibition?

A

Where the inhibitor molecule permanently binds to the enzyme NOT at the substrate binding site to lower enzyme activity

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6
Q

How does non-competitive inhibition affect Km and Vmax?

A

Km is unaffected but Vmax is reduced

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7
Q

Define Vmax

A

The maximum velocity of an enzyme catalysed reaction

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8
Q

Define Km

A

The substrate concentration that will give half Vmax

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9
Q

How does increased concentration of 2,3-BPG affect the oxygen affinity of haemoglobin?

A

Decreased affinity for oxygen, dissociation curve shifts to the right

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10
Q

How does an increased pH affect the oxygen affinity of haemoglobin?

A

Increased pH=Decreased [H+] so increased oxygen affinity so the dissociation curve shifts to the left

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11
Q

What are the differences between alpha and beta thalassaemia?

A

Alpha thalassaemia is fatal and symptoms occur before birth. Beta thalassaemia’s symptoms appear after birth

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12
Q

Why is alpha thalassaemia diagnosed before birth but beta thalassaemia can only be diagnosed after birth?

A

Foetal haemoglobin is made up of alpha and gamma subunits so beta subunits aren’t produced until after birth, so the defective gene isn’t yet being expressed.

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