Question 1

An allosteric ______________ stabilizes the T state of the enzyme.

Accepted Answer

inhibitor

Question 2

In many enzyme assays, the natural substrate and product are not used. Why?

Accepted Answer

Many products are difficult to measure accurately. Some are simply difficult to measure, while others are difficult to discern against the background of other molecules present in the reaction. Instead, substrates are chosen that the enzyme can still process but that result in products that can be easily measured. For example, substrates are chosen that result in products that are colored and can be detected spectrophotometrically.

Question 3

______________ is directly dependent on enzyme concentration.

Accepted Answer

Vmax

Question 4

The model describing allosteric regulation that requires all subunits to be in the same state is called the:

Accepted Answer

A)  concerted model. 
B)  syncopated model. 
C)  cooperative model. 
D)  equilibrium model. 
E)  None of the above. 
A)  concerted model. 
B)  syncopated model. 
C)  cooperative model. 
D)  equilibrium model. 
E)  None of the above.

Question 5

When [S] << KM, the enzymatic velocity depends on:

Accepted Answer

A)  the values of kcat/KM, [S], and [E]t. 
B)  the Vmax of the reaction. 
C)  the affinity of the substrate for the catalytic site. 
D)  kcat. 
E)  the formation of the ES complex. 
A)  the values of kcat/KM, [S], and [E]t. 
B)  the Vmax of the reaction. 
C)  the affinity of the substrate for the catalytic site. 
D)  kcat. 
E)  the formation of the ES complex.

Question 6

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-A reaction that is directly proportional to the concentration of reactant is a(n) ______________.

Accepted Answer

A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong 
A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong

Question 7

The ______________ rule states that all subunits in an allosteric enzyme must be in either the T or the R state; there can not be hybrids.

Accepted Answer

The answer of The ______________ rule states that all subunits...

Question 8

Allosteric modifiers alter the equilibria between:

Accepted Answer

A)  the ES state. 
B)  the R and T forms of a protein. 
C)  the forward and reverse reaction rate. 
D)  the formation of a product and its reverse reaction. 
E)  All of the above. 
A)  the ES state. 
B)  the R and T forms of a protein. 
C)  the forward and reverse reaction rate. 
D)  the formation of a product and its reverse reaction. 
E)  All of the above.

Question 9

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-_______________: Enzymes that do not obey Michaelis-Menten kinetics.

Accepted Answer

A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong 
A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong

Question 10

When designing a drug to inhibit the formation of a product which requires several enzymes in a metabolic pathway, what should be the first piece of information a biochemist needs to develop the drug?

Accepted Answer

The biochemist should look for the rate-

Question 11

When a substrate concentration is much greater than KM, the rate of catalysis is almost equal to:

Accepted Answer

A)  KD 
B)  kcat. 
C)  Vmax. 
D)  All of the above. 
E)  None of the above. 
A)  KD 
B)  kcat. 
C)  Vmax. 
D)  All of the above. 
E)  None of the above.

Question 12

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-The kcat is often referred to as the _______________.

Accepted Answer

A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong 
A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong

Question 13

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-An enzyme's affinity for its substrate is measured by the _______________ constant.

Accepted Answer

A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong 
A) first-order reaction 
B) second-order reaction 
C) metabolism 
D) ensemble 
E) biomolecular
F)turnover number
G)Michaelis-Menten
H)equilibrium
I)bsequential
J)kinetics
K)initial velocity
L)allosteric
M)ping-pong

Question 14

What is the turnover number for an enzyme and what does this value tell us about the enzyme?

Accepted Answer

The rate of reaction and dissociation of

Question 15

How does the sequential model differ from the concerted model for allosteric enzymes?

Accepted Answer

The concerted model does not allow for a

Question 16

The type of inhibition by a product of one enzyme on another enzyme in an earlier protein in a metabolic pathway is considered a(an) ______________ inhibitor.

Accepted Answer

The answer of The type of inhibition by a product...

Question 17

Would you expect the order of substrate binding to be critical for enzyme catalysis?

Accepted Answer

Yes, in some cases. For example, in ping

Question 18

An enzyme will be most sensitive to changes in cellular concentration when the concentration is ______________.

Accepted Answer

The answer of An enzyme will be most sensitive to...

Question 19

Which of the following is true under these conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 M.

Accepted Answer

A)  The enzyme is saturated with substrate. 
B)  Most of the enzyme does not have substrate bound. 
C)  There is more enzyme than substrate. 
D)  All of the above. 
E)  None of the above. 
A)  The enzyme is saturated with substrate. 
B)  Most of the enzyme does not have substrate bound. 
C)  There is more enzyme than substrate. 
D)  All of the above. 
E)  None of the above.

Question 20

Allosteric enzymes can be identified because the plot of initial velocity, V0, versus substrate concentration, S, is not hyperbolic but ______________ shaped.

Accepted Answer

The answer of Allosteric enzymes can be identified because the...

Exam 7: Kinetics and Regulation

An allosteric ______________ stabilizes the T state of the enzyme.

In many enzyme assays, the natural substrate and product are not used. Why?

______________ is directly dependent on enzyme concentration.

The model describing allosteric regulation that requires all subunits to be in the same state is called the:

When [S] << KM, the enzymatic velocity depends on:

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -A reaction that is directly proportional to the concentration of reactant is a(n) ______________.

The ______________ rule states that all subunits in an allosteric enzyme must be in either the T or the R state; there can not be hybrids.

Allosteric modifiers alter the equilibria between:

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -_______________: Enzymes that do not obey Michaelis-Menten kinetics.

When designing a drug to inhibit the formation of a product which requires several enzymes in a metabolic pathway, what should be the first piece of information a biochemist needs to develop the drug?

When a substrate concentration is much greater than KM, the rate of catalysis is almost equal to:

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -The kcat is often referred to as the _______________.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -An enzyme's affinity for its substrate is measured by the _______________ constant.

What is the turnover number for an enzyme and what does this value tell us about the enzyme?

How does the sequential model differ from the concerted model for allosteric enzymes?

The type of inhibition by a product of one enzyme on another enzyme in an earlier protein in a metabolic pathway is considered a(an) ______________ inhibitor.

Would you expect the order of substrate binding to be critical for enzyme catalysis?

An enzyme will be most sensitive to changes in cellular concentration when the concentration is ______________.

Which of the following is true under these conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 M.

Allosteric enzymes can be identified because the plot of initial velocity, V0, versus substrate concentration, S, is not hyperbolic but ______________ shaped.

Biochemistry and the Unity of Life

Water, Weak Bonds, and the Generation of Order Out of Chaos

Amino Acids

Protein Three-Dimensional Structure

Techniques in Protein Biochemistry

Basic Concepts of Enzyme Action

Mechanisms and Inhibitors

Hemoglobin: an Allosteric Protein

Carbohydrates

Lipids

Membrane Structure and Function

Signal Transduction Pathways

Digestion: Turning a Meal Into Cellular Biochemicals

Metabolism: Basic Concepts and Design

Glycolysis

Gluconeogenesis

Preparation for the Cycle

Harvesting Electrons From the Cycle

The Electron Transport Chain

The Proton-Motive Force

The Light Reactions

The Calvin Cycle

Glycogen Degradation

Glycogen Synthesis

The Pentose Phosphate Pathway

Fatty Acid Degredation

Fatty Acid Synthesis

Lipid Synthesis

Amino Acid Degradation and the Urea Cycle

Amino Acids Synthesis

Nucleotide Metabolism

The Structure of Informational Macromolecules: Dna and Rna

DNA Replication

DNA Repair and Recombination

RNA Synthesis and Regulation in Prokaryotes

Gene Expression in Eukaryotes

RNA Processing in Eukaryotes

The Genetic Code

The Mechanism of Protein Synthesis

Recombinant Dna Techniques

Filters