Question 1

The relationship between ∆G°′ and ∆G is best described as:

Accepted Answer

A)  determined by the temperature. 
B)  described by changes in Keq. 
C)  differing from standard state to physiological or actual concentrations of reactants and products. 
D)  dependent on the reaction mechanism of the reaction. 
E)  differing only in terms of the types of reactions used for each value. 
A)  determined by the temperature. 
B)  described by changes in Keq. 
C)  differing from standard state to physiological or actual concentrations of reactants and products. 
D)  dependent on the reaction mechanism of the reaction. 
E)  differing only in terms of the types of reactions used for each value.

Question 2

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-Which model is most appropriate to explain an enzyme binding to its substrate?

Accepted Answer

A) apoenzymes 
B) hydrolyases 
C) active site 
D) transition state 
E) spontaneous
F)induced fit
G)energy
H)prosthetic group
I)lock and key
J)substrate(s)
K)oxidoreductases
L)equilibria 
A) apoenzymes 
B) hydrolyases 
C) active site 
D) transition state 
E) spontaneous
F)induced fit
G)energy
H)prosthetic group
I)lock and key
J)substrate(s)
K)oxidoreductases
L)equilibria

Question 3

Riboflavin is a water-soluble organic substance that is not synthesized by humans. Metabolically, it is chemically converted into a substance called flavin adenine dinucleotide, which is required by succinate dehydrogenase. Which of the following statements is most correct?

Accepted Answer

A)  Riboflavin is a coenzyme. 
B)  Flavin adenine dinucleotide is a vitamin. 
C)  Succiniate dehydrogenase is a coenzyme. 
D)  Flavin adenine dinucleotide is a coenzyme. 
A)  Riboflavin is a coenzyme. 
B)  Flavin adenine dinucleotide is a vitamin. 
C)  Succiniate dehydrogenase is a coenzyme. 
D)  Flavin adenine dinucleotide is a coenzyme.

Question 4

How does a rigid, lock-and key-model for substrate binding not fit with the formation of the transition state?

Accepted Answer

The amino acids in the active site must

Question 5

A cofactor is best defined as:

Accepted Answer

A)  another protein. 
B)  a covalently bound inorganic molecule. 
C)  a small molecule that holds the substrate in the active site. 
D)  a molecule responsible for most of the catalytic activity of the enzyme. 
E)  None of the above 
A)  another protein. 
B)  a covalently bound inorganic molecule. 
C)  a small molecule that holds the substrate in the active site. 
D)  a molecule responsible for most of the catalytic activity of the enzyme. 
E)  None of the above

Question 6

A mutation of a proteolytic enzyme described in Section 6.1 results in a stable covalent bond between one of the catalytic amino acids of the protease with its protein substrate. What would be the most likely outcome of enzyme function?

Accepted Answer

The enzyme, after one round of reaction,

Question 7

The free energy of activation is:

Accepted Answer

A)  the amount of chemical energy available in the transition state. 
B)  the difference in free energy between the substrate and the product. 
C)  the free energy gained by adding a catalyst. 
D)  the difference in free energy between the transition state and the substrate. 
E)  All of the above. 
A)  the amount of chemical energy available in the transition state. 
B)  the difference in free energy between the substrate and the product. 
C)  the free energy gained by adding a catalyst. 
D)  the difference in free energy between the transition state and the substrate. 
E)  All of the above.

Question 8

The free-energy change (ΔG°′) for the oxidation of the sugar molecules in a sheet of paper into CO2 and H2O is large and negative (ΔG°′ - 2833 kJ/mol). Explain why paper is stable at room temperature in the presence of oxygen (O2).

Accepted Answer

Activation energy! While the r

Question 9

A reaction can occur spontaneously only if ΔG is __________________.

Accepted Answer

The answer of A reaction can occur spontaneously only if...

Question 10

How do enzymes facilitate the formation of the transition state?

Accepted Answer

When enzymes bind substrate, free energy

Exam 6: Basic Concepts of Enzyme Action

The relationship between ∆G°′ and ∆G is best described as:

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -Which model is most appropriate to explain an enzyme binding to its substrate?

Riboflavin is a water-soluble organic substance that is not synthesized by humans. Metabolically, it is chemically converted into a substance called flavin adenine dinucleotide, which is required by succinate dehydrogenase. Which of the following statements is most correct?

How does a rigid, lock-and key-model for substrate binding not fit with the formation of the transition state?

A cofactor is best defined as:

A mutation of a proteolytic enzyme described in Section 6.1 results in a stable covalent bond between one of the catalytic amino acids of the protease with its protein substrate. What would be the most likely outcome of enzyme function?

The free energy of activation is:

The free-energy change (ΔG°′) for the oxidation of the sugar molecules in a sheet of paper into CO2 and H2O is large and negative (ΔG°′ - 2833 kJ/mol). Explain why paper is stable at room temperature in the presence of oxygen (O2).

A reaction can occur spontaneously only if ΔG is __________________.

How do enzymes facilitate the formation of the transition state?

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

Kinetics and Regulation

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