Session 6: Enzymes Flashcards

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1
Q

What is a transition state?

A

High energy intermediate the lies between substrate and product.

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2
Q

What is meant by the ‘induced fit’ active site hypothesis?

A

The active site of an enzyme only forms a complementary shape after binding of the substrate

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3
Q

What is V0?

A

Initial rate of reaction

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4
Q

What equation predicts that a reaction rate as a function of substrate concentration will have the shape of a rectangular hyperbola?

A

Michaelis-Menten

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5
Q

Define Vmax

A

Maximal rate when all enzyme active sites are saturated with substrate.

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6
Q

Define Km

A

Substrate concentration that gives half the maximal velocity/ affinity of enzyme to the substrate.

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7
Q

What is the affinity for a substrate when Km is low?

A

High affinity

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8
Q

What is the affinity for a substrate when Km is high?

A

Low affinity

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9
Q

What plot is used to allow for an easy estimation of Km and Vmax

A

Lineweaver-Burk plot

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10
Q

How does an irreversible enzyme inhibitor bind?

A

Covalently bonded

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11
Q

Give an example of an irreversible inhibitor.

A

Nerve gases e.g. Sarin

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12
Q

How do reversible inhibitors bind to enzymes?

A

Non-Coventry therefore they can freely dissociate.

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13
Q

What do competitive inhibitors affect?

A

Km increases

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14
Q

What do non-competitive inhibitors affect?

A

Vmax decreases

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