Enzymes Flashcards

0
Q

What is the binding curve of haemoglobin?

A

Sigmoidal

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1
Q

What curve does myoglobin binding show?

A

Hyperbolic

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2
Q

What is Vmax?

A

Maximal rate when all enzyme active sites are saturated with substrate

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3
Q

What is Km?

A

Substrate concentration that gives half maximal velocity

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4
Q

What is the significance of Km?

A

Km values gives a measure of the affinity of an enzyme for its substrate

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5
Q

What does high Km mean?

A

Low affinity

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6
Q

Why do you see cooperative binding with Hb?

A

Hb has 4 subunits- binding of oxygen increases R state making it easier for oxygen to bind to subsequent subunits

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7
Q

What are the two states of Hb and their affinities

A

T state- low affinity

R state- high affinity

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8
Q

Why is the cooperative binding of Hb important?

A

Sigmoidal binding curve means that oxygen can be efficiently carried from the lungs to the tissue

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9
Q

Does binding of more oxygen to haemoglobin increase or decrease affinity?

A

Increases affinity

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10
Q

What effect does 2,3-BPG have on Hb?

A

Increased BPG decreases affinity and shifts curve to the right (stabilises T state)

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11
Q

What is the Bohr effect?

A

Binding of H+ and CO2 to Hb lowers its affinity for oxygen- shifts curve to the right

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12
Q

Why is the Bohr effect important?

A

Metabolically active tissues produce large amounts of H+ and CO2- the Bohr effect ensures the delivery of O2 is coupled to demand

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13
Q

Explain CO poisoning

A

CO binds to Hb 250x more readily than O2
Fatal when COHb is >50%
It also acts to increase affinity of unaffected subunits

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14
Q

What is the structure of Hb?

A

2 alpha and 2 beta chains

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