L10- Enzymes as Catalysts Flashcards

1
Q

What enzyme catalyzes the hydrolysis of peptides on the C-terminal side of phenylalanine, tyrosine and tryptophan?

A

Chymotrypsin.

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2
Q

What amino acids make up the catalytic triad in a serine protease?

A

Aspartate, histidine and serine.

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3
Q

Do enzymes change their structure after catalysis?

A

No. At the end of the reaction cycle they are the same as when they started.

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4
Q

When the Gibbs free energy (G) of a reaction is negative, that reaction is ______.

A

Spontaneous.

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5
Q

When the Gibbs free energy (G) of a reaction is positive, that reaction is ______.

A

Non-spontaneous.

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6
Q

When the Gibbs free energy (G) of a reaction is zero, that reaction is ______.

A

At equilibrium.

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7
Q

True or False. All exothermic reactions are spontaneous.

A

False. Delta G can be negative (indicating a spontaneous reaction) even when delta H is positive. This occurs when delta S (the change in entropy) is positive.

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8
Q

True or False. Reactions in the body are in equilibrium.

A

False.

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9
Q

How do enzymes affect the energy of reactions?

A

Enzymes lower the activation energy. They accelerate the rate of reactions, but do not change the potential energy of the substrates or products.

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10
Q

How does the activation energy affect the speed of a reaction?

A

In general, the larger the activation energy the slower the reaction.

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11
Q

Define catabolism.

A

Burning fuel to make ATP.

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12
Q

Define anabolism.

A

Burning energy (usually ATP) for biosynthetic processes, active transport and/or mechanical work.

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13
Q

How can one determine reaction velocity?

A

By measuring the amount of product formed per unit time.

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14
Q

What kinetic parameters can be extracted from a Michaelis-Menten kinetics graph?

A

Vmax, the maximum velocity of the catalyzed reaction, and Km, the substrate concentration required to achieve half the maximum velocity.

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15
Q

When is Km equal to the substrate concentration in a Michaelis-Menten Kinetics graph?

A

When the substrate concentration is at half of Vmax.

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16
Q

Delta G for ATP hydrolysis (ATP + H2O -> ADP + Pi) is -7.3 kcal/mole. How much energy is required to perform the reverse reaction?

A

+7.3 kcal/mole.

17
Q

What is a cofactor?

A

Cofactors are typically small molecules that help promote catalysis. Many vitamins act as cofactors.

18
Q

Which enzyme is deficient in individuals with methylmalonic acidemia?

A

Methylmalonyl mutase.

19
Q

What is the cofactor for methylmalonyl mutase?

A

Vitamin B12.

20
Q

What are the substrates and products of methylmalonyl mutase?

A

The enzyme converts methylmalonyl CoA to succinyl CoA.

21
Q

True or False. Generally, the atoms in an enzyme that bind to a substrate are different than the atoms that participate in the catalysis of a reaction.

A

True.

22
Q

What are the four steps, in order, of a reaction catalyzed by serine proteases?

A
  1. Binding of substrate, 2. attack by serine, 3. stabilization of transition state, and 4. release of products.
23
Q

What is an oxyanion hole and what is its function?

A

It is a structural pocket in an enzyme that stabilizes an oxyanion (i.e. stabilizes the transition state).

24
Q

The initial enzyme velocity proportional to what?

A

The amount of substrate.

25
Q

The y-intercept in Lineweaver-Burk plots corresponds to what kinetic parameter?

A

NAME?

26
Q

The x-intercept in Lineweaver-Burk plots corresponds to what kinetic parameter?

A

NAME?

27
Q

The slope in Lineweaver-Burk plots corresponds to what kinetic parameter?

A

Km/Vmax.