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Biochemistry I Module of the MCAT Self Prep eCourse_ Lesson 3_ Enzyme Kinetics (Pro)

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Biochemistry I Module of the MCAT Self Prep eCourse_ Lesson 3_ Enzyme Kinetics (Pro)Biochemistry I Module of the MCAT Self Prep eCourse_ Lesson 3_ Enzyme Kinetics (Pro)

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Biochemistry I Module Of The MCAT Self Prep ECours
Course
Biochemistry I Module of the MCAT Self Prep eCours

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Biochemistry I Module of the MCAT Self Prep
eCourse: Lesson 3: Enzyme Kinetics (Pro)

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Lesson 3: Enzyme Kinetics Lesson 3: Enzyme Kinetics


Rate= k [A][B]



Rate is the change in concentration per unit time.

k is the rate constant (depends on the reaction).

[A] and [B] are the concentrations of reactants A and B.
Write the rate law for the

following reaction: A+B -> AB
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In Michaelis-Menten Kinetics (B) III Only

experiments, which of the

following is assumed to be true? In Michaelis-Menten Kinetics

experiments:

I. Substrate concentration is

constant. - ENZYME concentration is held

II. Increasing the Enzyme constant as we increase the substrate

concentration will not change concentration.

Vmax. - If you were to increase the enzyme

III. The enzymes are saturated at concentration, the Vmax would

Vmax. increase.

- The enzymes are saturated at Vmax.

(A) I Only

(B) III Only

(C) I and II Only

(D) I, II, and III

,In Michaelis-Menten Kinetics (C) I and II Only

experiments, which of the

following is assumed to be true? In Michaelis-Menten Kinetics experiments, we assume that:



I. Our Solutions are behaving - Our Solutions are behaving ideally.

ideally. - Our constants ([E] and k) are not changing during the

II. Our constants ([E] and k) are experiment.

not changing during the - Substrate CANNOT be converted into product without the

experiment. enzyme.

III. Substrate can be converted

into product with or without the

enzyme.



(A) I Only

(B) III Only

(C) I and II Only

(D) I, II, and III


How can we increase the rate of (B) I and II Only

a reaction assuming the rate

constant (k) is constant? We can increase the rate of reaction

by increasing the substrate or enzyme

I. Increase Substrate concentration.

Concentration

II. Increase Enzyme Adding any type of inhibitor will not

Concentration increase the rate of a reaction.

III. Increase Mixed Inhibitor

Concentration



(A) I Only

(B) I and II Only

(C) II and III Only

(D) I, II, and III


False. Adding more catalyst after a catalytic amount has already
True or false? Adding more
been added will NOT AFFECT the rate of reaction.
catalyst after a catalytic amount

has already been added will
You only need a small amount ("a catalytic amount") of catalyst
increase the rate of reaction.
for it to do its job. Adding more will not do anything.


What does it mean if the rate of (D) The enzymes no longer have

reaction has reached maximum available active sites.

velocity (Vmax)?

When the rate of reaction reaches

(A) There are more products Vmax, it means that the enzymes are

than reactants. saturated and will not be able to react

(B) The substrates are no longer any more quickly since all active sites

able to get any closer to the are filled up with substrates.

enzymes.

(C) The substrates are no longer

able to get in any better of an

orientation.

(D) The enzymes no longer have

available active sites.

, If a reaction has reached Vmax, (B) It would remain the same

what would happen to the rate

of reaction if we increase the Increasing the substrate concentration

substrate concentration? would have no effect on the rate of the

reaction because all active sites are

(A) It would increase already occupied at Vmax.

(B) It would remain the same

(C) It would decrease

(D) It would stop


What is the one way to increase (B) Increase Enzyme Concentration

the Vmax of a reaction?

The only way to increase Vmax is by increasing the enzyme

(A) Increase Substrate concentration.

Concentration

(B) Increase Enzyme

Concentration

(C) Increase Inhibitor

Concentration

(D) Increase Product

Concentration


E + S => ES => E + P



Rate1 = k1 [E][S]

These are the two steps of

enzyme catalysis: Rate2 = k2 [ES]



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What is the steady-state (A) [ES] is constant

assumption when talking about

enzyme kinetics? The steady state assumption means that the concentration of the

enzyme-substrate complex (ES) is constant, which means that the

(A) [ES] is constant formation of ES is equal to the dissociation of ES.

(B) [S] is constant

(C) [P] is constant

(D) [I] is constant

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Biochemistry I Module of the MCAT Self Prep eCours

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