Enzymes and Kinetics

Question: The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site
[A].

contains modified amino acids

[B].

catalyzes a chemical reaction

[C].

is complementary to a specific ligand

[D].

contains amino acids without side chains

Answer: Option B

Explanation:

No answer description available for this question.

Question: The active site of an enzyme remains
[A].

at the center of globular proteins

[B].

rigid and does not change shape

[C].

complementary to the rest of the molecule

[D].

none of the above

Answer: Option D

Explanation:

No answer description available for this question.

Question: When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about
[A].

0.1 * Vmax

[B].

0.2 * Vmax

[C].

0.5 * Vmax

[D].

0.9 * Vmax

Answer: Option C

Explanation:

No answer description available for this question.

Question: An enzyme and a reactant molecule maintain relationship as
[A].

a temporary association

[B].

an association stabilized by a covalent bond

[C].

one in which the enzyme is changed permanently

[D].

non complementary binding

Answer: Option A

Explanation:

No answer description available for this question.

Question: An enzyme has a Km of 4.7 x 10-5M. If the Vmax of the preparation is 22m moles liter-1 min-1, what velocity would be observed in the presence of 2.0 x 10-4M substrate and 5.0 x 10-5M of a competitive inhibitor?
[A].

13.54μ moles liter-1min-1

[B].

6.68μ moles liter-1min-1

[C].

7.57μ moles liter-1min-1

[D].

17.8μ moles liter-1min-1

Answer: Option A

Explanation:

No answer description available for this question.

Question: Predominantly uncompetitive inhibition may be called when
[A].

competitive inhibition is greater than uncompetitive inhibition

[B].

competitive inhibition is smaller than uncompetitive inhibition

[C].

competitive inhibition is equal to uncompetitive inhibition

[D].

none of the above

Answer: Option A

Explanation:

No answer description available for this question.

Question: The rate equation in non-competitive inhibition based on Michaelis Menten equation is given by
[A].

rmaxS/(Km + S)(1+I/Ki)

[B].

rmaxE/(Km (1+I/Ki)+S))

[C].

VmaxS/(Km + S)(1+I/Ki)

[D].

rmaxS/Km

Answer: Option A

Explanation:

No answer description available for this question.

Question: The rate equation in competitive inhibition based on Michaelis Menten equation is given by
[A].

rmaxS/(Km (1+I/Ki)+S))

[B].

rmaxE/(Km (1+I/Ki)+S))

[C].

rmaxI/(Km (1+I/Ki)+S))

[D].

rmaxS/(Km (1+I/Ki))

Answer: Option A

Explanation:

No answer description available for this question.

Question: The types of inhibition pattern based on Michaelis Menten equation are
[A].

competitive

[B].

non-competitive

[C].

uncompetitive

[D].

all of the above

Answer: Option D

Explanation:

No answer description available for this question.

Question: If a reaction occurs in the absence of inhibitor with rate ν0 and in the presence of inhibitor with rate νi, the degree of inhibition is defined as
[A].

(ν0 – νi)/ν0

[B].

(ν0 + νi)/ν0

[C].

(ν0νi)/ν0

[D].

(ν0-νi)/νi

Answer: Option A

Explanation:

No answer description available for this question.