Question 1

How is it possible for an enzyme to lower the required energy of activation for a reaction?

Accepted Answer

Concepts to Consider: Specificity of the

Question 2

At a constant temperature and pH, the rate of an enzymatically catalyzed reaction is inversely proportional to the enzyme concentration. 
__________________

Accepted Answer

A) True 
 B)False

Question 3

Which refers to an organic, nonpolypeptide compound that binds to the apoenzyme and serves as a cofactor?

Accepted Answer

A)  mineral 
B)  catalyst 
C)  substrate 
D)  coenzyme 
E)  allosteric regulator 
A)  mineral 
B)  catalyst 
C)  substrate 
D)  coenzyme 
E)  allosteric regulator

Question 4

Consider the following two chemical equations:
A. glucose + fructose → sucrose + H2O, Δ G = +27kJ/mole (or +6.5 kcal/mole)
B. glucose + fructose + ATP → sucrose + ADP + Pi, Δ G = − 5kJ/mole (or − 1.2 kcal/mole)
What is the overall Δ G ?

Accepted Answer

A)  22 kJ/mole 
B)  32 kJ/mole 
C)  -32 kJ/mole 
D)  -135 kJ/mole 
E)  135 kJ/mole 
A)  22 kJ/mole 
B)  32 kJ/mole 
C)  -32 kJ/mole 
D)  -135 kJ/mole 
E)  135 kJ/mole

Question 5

According to the second law of thermodynamics, energy cannot be created nor destroyed. 
__________________

Accepted Answer

A) True 
 B)False

Question 6

Some enzymes have a receptor site that is other than the active site. This is also referred to as a(n) ____ site.

Accepted Answer

A)  sensitive 
B)  allosteric 
C)  inhibitive 
D)  reversible 
E)  competitive 
A)  sensitive 
B)  allosteric 
C)  inhibitive 
D)  reversible 
E)  competitive

Question 7

It is a fact that enzymes are highly specific and will only catalyze one or a few reactions. Can you think of a benefit that is derived from such specificity? (i.e., What would happen if most biochemical reactions were catalyzed by the same enzyme?)

Accepted Answer

Concepts to Consider: Having specific en

Question 8

In what method do competitive inhibitors inhibit biochemical reactions?

Accepted Answer

A)  Competitive inhibitors denature the enzyme. 
B)  Competitive inhibitors reduce the concentration of enzyme. 
C)  Competitive inhibitors increase the concentration of enzyme. 
D)  Competitive inhibitors reduce the concentration of substrate. 
E)  Competitive inhibitors increase the concentration of substrate. 
A)  Competitive inhibitors denature the enzyme. 
B)  Competitive inhibitors reduce the concentration of enzyme. 
C)  Competitive inhibitors increase the concentration of enzyme. 
D)  Competitive inhibitors reduce the concentration of substrate. 
E)  Competitive inhibitors increase the concentration of substrate.

Question 9

Select the phosphorylation reaction.

Accepted Answer

A)  glucose + fructose → sucrose + H2O 
B)  glucose + ATP → glucose-P + ADP 
C)  glucose-P + fructose → sucrose + Pi 
D)  glucose + glucose → maltose 
E)  sucrose + H2O → glucose + fructose 
A)  glucose + fructose → sucrose + H2O 
B)  glucose + ATP → glucose-P + ADP 
C)  glucose-P + fructose → sucrose + Pi 
D)  glucose + glucose → maltose 
E)  sucrose + H2O → glucose + fructose

Question 10

Why type of energy is represented by a positive change in G ?

Accepted Answer

A)  entropy 
B)  enthalpy 
C)  exergonic 
D)  endergonic 
E)  activation 
A)  entropy 
B)  enthalpy 
C)  exergonic 
D)  endergonic 
E)  activation

Question 11

Figure 7-1   Which conclusion can be accurately derived from the accompanying figure?

Accepted Answer

A)  Δ S is positive. 
B)  Δ H equals zero. 
C)  Δ G is positive. 
D)  Δ G is negative. 
E)  Δ T is negative. 
A)  Δ S is positive. 
B)  Δ H equals zero. 
C)  Δ G is positive. 
D)  Δ G is negative. 
E)  Δ T is negative.

Question 12

What do hydrolases catalyze?

Accepted Answer

A)  splitting water 
B)  oxidation-reduction reactions 
C)  splitting a molecule using water 
D)  the transfer of a phosphate group 
E)  reactions in which double bonds are formed 
A)  splitting water 
B)  oxidation-reduction reactions 
C)  splitting a molecule using water 
D)  the transfer of a phosphate group 
E)  reactions in which double bonds are formed

Question 13

The cell maintains a ratio of ATP to ADP that is at the equilibrium point. 
__________________

Accepted Answer

A) True 
 B)False

Exam 7: Energy and Metabolism

How is it possible for an enzyme to lower the required energy of activation for a reaction?

At a constant temperature and pH, the rate of an enzymatically catalyzed reaction is inversely proportional to the enzyme concentration. __________________

Which refers to an organic, nonpolypeptide compound that binds to the apoenzyme and serves as a cofactor?

Consider the following two chemical equations: A. glucose + fructose → sucrose + H2O, Δ G = +27kJ/mole (or +6.5 kcal/mole) B. glucose + fructose + ATP → sucrose + ADP + Pi, Δ G = − 5kJ/mole (or − 1.2 kcal/mole) What is the overall Δ G ?

According to the second law of thermodynamics, energy cannot be created nor destroyed. __________________

Some enzymes have a receptor site that is other than the active site. This is also referred to as a(n) ____ site.

It is a fact that enzymes are highly specific and will only catalyze one or a few reactions. Can you think of a benefit that is derived from such specificity? (i.e., What would happen if most biochemical reactions were catalyzed by the same enzyme?)

In what method do competitive inhibitors inhibit biochemical reactions?

Select the phosphorylation reaction.

Why type of energy is represented by a positive change in G ?

Figure 7-1 Which conclusion can be accurately derived from the accompanying figure?

What do hydrolases catalyze?

The cell maintains a ratio of ATP to ADP that is at the equilibrium point. __________________

A View of Life

Atoms and Molecules the Chemical Basis of Life

The Chemistry of Life Organic Compounds

Organization of the Cell

Biological Membranes

Cell Communication

How Cells Make Atp Energy-Releasing Pathways

Photosynthesis Capturing Light Energy

Chromosomes, Mitosis, and Meiosis

The Basic Principles of Heredity

Dna the Carrier of Genetic Information

Gene Expression

Gene Regulation

Dna Technology and Genomics

Human Genetics and the Human Genome

Developmental Genetics

Introduction to Darwinian Evolution

Evolutionary Change in Populations

Speciation and Macroevolution

The Origin and Evolutionary History of Life

The Evolution of Primates

Understanding Diversity Systematics

Viruses and Subviral Agents

Bacteria and Archaea

Protists

Seedless Plants

Seed Plants

The Fungi

An Introduction to Animal Diversity

Sponges, Cnidarians, Ctenophores, and Protostomes

The Deuterostomes

Plant Structure Growth and Development

Leaf Structure and Function

Stem Structure and Transport

Roots and Mineral Nutrition

Reproduction in Flowering Plants

Plant Developmental Responses to External and Internal Signals

Animal Structure and Function an Introduction

Protection Support and Movement

Neural Signaling

Neural Regulation

Sensory Systems

Internal Transport

The Immune System Internal Defense

Gas Exchange

Processing Food and Nutrition

Osmoregulation and Disposal of Metabolic Wastes

Endocrine Regulation

Reproduction

Animal Development

Animal Behavior

Introduction to Ecology Population Ecology

Community Ecology

Ecosystems and the Biosphere

Ecology and the Geography of Life

Biological Diversity and Conservation Biology

Filters

Consider the following two chemical equations: A. glucose + fructose → sucrose + H₂O, Δ G = +27kJ/mole (or +6.5 kcal/mole) B. glucose + fructose + ATP → sucrose + ADP + P_i, Δ G = − 5kJ/mole (or − 1.2 kcal/mole) What is the overall Δ G ?