An Introduction to

Metabolism
Rawan Qassrawi
An organism’s metabolism transforms matter
and energy
• Metabolism is the totality of an organism’s chemical reactions.
• In a metabolic pathway, a specific molecule is altered in a series of
defined steps, resulting in a certain product.
• Each step of the pathway is catalyzed by a specific enzyme.
 Enzyme 1 Enzyme 2 Enzyme 3
A B C D
Reaction 1 Reaction 2 Reaction 3
Starting Product
molecule

Enzymes speed up each reaction in a series of reactions

to in order to obtain the product at a much quicker rate.
Metabolic Pathways
Chapter 8
• Metabolism as a whole manages the material and energy resources
Ancell.Introduction to Metabolism
of the
• Catabolic pathways release energy by breaking down complex
molecules into simpler compounds
• A major pathway of catabolism is cellular respiration, the breakdown
of glucose in the presence of oxygen to carbon dioxide and water,
which is an example of a catabolism pathway.
Metabolic Pathways
• Anabolic pathways consume energy to build complex molecules from
simpler ones
• The synthesis of protein from amino acids is an example of anabolism
• Bioenergetics is the study of how organisms manage their energy
resources
Forms of Energy
• Energy is the capacity to cause change or the ability to rearrange
matter.
• Energy exists in various forms, some of which can perform work.
• Kinetic energy is energy associated with motion of objects. Ex)playing
pool.
• Heat (thermal energy) is kinetic energy associated with random
movement of atoms or molecules harnessed to do work. Also in light
which powers (photosynthesis).
Forms of Energy
• Potential energy is energy that matter possesses because of its
location or structure
• Chemical energy is potential energy available for release in a chemical
reaction
• Energy can be converted from one form to another
A diver has more potential Diving converts
energy on the platform potential energy to
than in the water. kinetic energy.

Climbing up converts the kinetic A diver has less potential

energy of muscle movement energy in the water
to potential energy. than on the platform.
The Laws of Energy Transformation
• Thermodynamics is the study of energy transformations
• A isolated system, such as that approximated by liquid in a thermos, is
isolated and is unable to exchange either energy or matter with its
surroundings
• In an open system, energy and matter can be transferred between the
system and its surroundings
• Organisms are open systems – absorb energy in the form of organic
molecules, but release energy in the form of heat and waste, carbon
dioxide and water.
The First Law of Thermodynamics
• According to the first law of thermodynamics, the energy of the
universe is constant
• Energy can be transferred and transformed, but it cannot be
created or destroyed

• The first law is also called the principle of conservation of energy

• Electric company does not make energy, converts it into a form we
can use.
The Second Law of Thermodynamics
• During every energy transfer or transformation, some energy is
unusable, and is often lost as heat or waste (carbon dioxide)

• According to the second law of thermodynamics

• Every energy transfer or transformation increases the entropy
(disorder or randomness) of the universe.
A brown bear converts chemical energy from organic molecules
in its food into kinetic and other forms of energy to carry out
biological processes.

Heat

Chemical
energy

(a) First law of thermodynamics (b) Second law of thermodynamics

The Second Law of Thermodynamics
• Living cells unavoidably convert organized forms of energy to heat.
• Spontaneous processes occur without energy input; they can happen
quickly or slowly.
• For a process to occur without energy input, it must increase the
entropy of the universe.
Biological Order and Disorder
• Cells create ordered structures from less ordered materials
• Organisms also replace ordered forms of matter and energy with less
ordered forms
• Energy flows into an ecosystem in the form of light and exits in the
form of heat
The free-energy change of a reaction tells us
whether or not the reaction occurs spontaneously
• Biologists want to know which reactions occur spontaneously and
which require input of energy
• To do so, they need to determine energy changes that occur in
chemical reactions
Free-Energy Change, G
• A living system’s free energy is energy that can do work when
temperature and pressure are uniform, as in a living cell

• The change in free energy (∆G) during a process is related to the

change in enthalpy, or change in total energy (∆H), change in entropy
(∆S), and temperature in Kelvin (T)
∆G = ∆H – T∆S
• Only processes with a negative ∆G are spontaneous
• Spontaneous processes can be harnessed to perform work
Free Energy, Stability, and Equilibrium
• Free energy is a measure of a system’s instability, its tendency to
change to a more stable state
• During a spontaneous change, free energy decreases and the stability
of a system increases
• Equilibrium is a state of maximum stability
• A process is spontaneous and can perform work only when it is
moving toward equilibrium
 • More free energy (higher G)
• Less stable
• Greater work capacity

In a spontaneous change
• The free energy of the system
decreases (G  0)
• The system becomes more
stable
• The released free energy can
be harnessed to do work

• Less free energy (lower G)

• More stable
• Less work capacity

(a) Gravitational motion (b) Diffusion (c) Chemical reaction

Exergonic and Endergonic Reactions in
Metabolism
• The concept of free energy can be applied to the chemistry of life’s
processes
• An exergonic reaction proceeds with a net release of free energy and
is spontaneous
• An endergonic reaction absorbs free energy from its surroundings
and is nonspontaneous
 (a) Exergonic reaction: energy released, spontaneous

Reactants

Amount of
energy
released

Free energy
(G  0)
Energy
Products

Progress of the reaction

(b) Endergonic reaction: energy required, nonspontaneous

Products

Amount of
energy
required
Free energy

(G  0)
Energy
Reactants

Progress of the reaction

Equilibrium and Metabolism
• Reactions in a closed system eventually reach equilibrium and then
do no work
• Cells are not in equilibrium; they are open systems experiencing a
constant flow of materials
• A defining feature of life is that metabolism is never at equilibrium
• A catabolic pathway in a cell releases free energy in a series of
reactions
• Closed and open hydroelectric systems can serve as analogies
 G  0 G = 0

(a) An isolated hydroelectric system

(b) An open hydro-

electric system G  0

G  0
G  0
G  0

(c) A multistep open hydroelectric system

ATP powers cellular work by coupling
exergonic reactions to endergonic reactions
• A cell does three main kinds of work
• Chemical
• Transport
• Mechanical
• To do work, cells manage energy resources by energy coupling, the
use of an exergonic process to drive an endergonic one
• Most energy coupling in cells is mediated by ATP
The Structure and Hydrolysis of ATP
• ATP (adenosine triphosphate) is the cell’s energy shuttle
• ATP is composed of ribose (a sugar), adenine (a nitrogenous base),
and three phosphate groups
• The bonds between the phosphate groups of ATP’s tail can be broken
by hydrolysis
• Energy is released from ATP when the terminal phosphate bond is
broken
• This release of energy comes from the chemical change to a state of
lower free energy, not from the phosphate bonds themselves
 Adenine

Phosphate groups
Ribose

(a) The structure of ATP

Adenosine triphosphate (ATP)

Energy

Inorganic
Adenosine diphosphate (ADP)
phosphate

(b) The hydrolysis of ATP

How the Hydrolysis of ATP Performs Work
• The three types of cellular work (mechanical, transport, and chemical)
are powered by the hydrolysis of ATP
• In the cell, the energy from the exergonic reaction of ATP hydrolysis
can be used to drive an endergonic reaction
• Overall, the coupled reactions are exergonic
• ATP drives endergonic reactions by phosphorylation, transferring a
phosphate group to some other molecule, such as a reactant
• The recipient molecule is now called a phosphorylated intermediate
The Regeneration of ATP
• ATP is a renewable resource that is regenerated by addition of a
phosphate group to adenosine diphosphate (ADP)
• The energy to phosphorylate ADP comes from catabolic reactions in
the cell
• The ATP cycle is a revolving door through which energy passes during
its transfer from catabolic to anabolic pathways
 ATP H2O

Energy from Energy for cellular

catabolism (exergonic, work (endergonic,
energy-releasing ADP Pi energy-consuming
processes) processes)
Enzymes speed up metabolic reactions by
lowering energy barriers
• A catalyst is a chemical agent that speeds up a reaction without being
consumed by the reaction
• An enzyme is a catalytic protein
• Hydrolysis of sucrose by the enzyme sucrase is an example of an
enzyme-catalyzed reaction
 Sucrase

Sucrose Glucose Fructose

(C12H22O11) (C6H12O6) (C6H12O6)
The Activation Energy Barrier
• Every chemical reaction between molecules involves bond breaking
and bond forming
• The initial energy needed to start a chemical reaction is called the
free energy of activation, or activation energy (EA)
• Activation energy is often supplied in the form of thermal energy that
the reactant molecules absorb from their surroundings
 A B

C D
Transition state

A B
Free energy
EA
C D

Reactants
A B
G  O
C D

Products

Progress of the reaction

How Enzymes Lower the EA Barrier
• Enzymes catalyze reactions by lowering the EA barrier
• Enzymes do not affect the change in free energy (∆G); instead, they
hasten reactions that would occur eventually
 Course of
reaction EA
without without
enzyme enzyme EA with
enzyme
Free energy is lower
Reactants

Course of G is unaffected
reaction by enzyme
with enzyme

Products

Progress of the reaction

Substrate Specificity of Enzymes
• The reactant that an enzyme acts on is called the enzyme’s substrate
• The enzyme binds to its substrate, forming an enzyme-substrate
complex
• The active site is the region on the enzyme where the substrate binds
• Induced fit of a substrate brings chemical groups of the active site
into positions that enhance their ability to catalyze the reaction
 Substrate

Active site

Enzyme Enzyme-substrate
complex
(a) (b)
Catalysis in the Enzyme’s Active Site
• In an enzymatic reaction, the substrate binds to the active site of the
enzyme
• The active site can lower an EA barrier by
• Orienting substrates correctly
• Straining substrate bonds
• Providing a favorable microenvironment
• Covalently bonding to the substrate
 1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.

Substrates
Enzyme-substrate
complex

Active
site

Enzyme
 1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.

Substrates
Enzyme-substrate
complex 3 Active site can
lower EA and speed
up a reaction.

Active
site

Enzyme

4 Substrates are
converted to
products.
 1 Substrates enter active site.
2 Substrates are held
in active site by weak
interactions.

Substrates
Enzyme-substrate
complex 3 Active site can
lower EA and speed
up a reaction.

6 Active
site is
available
for two new
substrate
molecules.
Enzyme

5 Products are 4 Substrates are

released. converted to
products.
Products
Effects of Local Conditions on Enzyme Activity
• An enzyme’s activity can be affected by
• General environmental factors, such as temperature and pH
• Chemicals that specifically influence the enzyme
Effects of Temperature and pH
• Each enzyme has an optimal temperature in which it can function
• Each enzyme has an optimal pH in which it can function
• Optimal conditions favor the most active shape for the enzyme
molecule
 Optimal temperature for Optimal temperature for
typical human enzyme (37°C) enzyme of thermophilic
(heat-tolerant)

Rate of reaction
bacteria (77°C)

0 60
20 80 40 100 120
Temperature (°C)
(a) Optimal temperature for two enzymes

Optimal pH for pepsin Optimal pH for trypsin

(stomach (intestinal
enzyme) enzyme)
Rate of reaction

0 1 5 2 3 4 6 7 8 9 10
pH
(b) Optimal pH for two enzymes
Cofactors
• Cofactors are nonprotein enzyme helpers
• Cofactors may be inorganic (such as a metal in ionic form) or organic
• An organic cofactor is called a coenzyme
• Coenzymes include vitamins
Enzyme Inhibitors
• Competitive inhibitors bind to the active site of an enzyme,
competing with the substrate
• Noncompetitive inhibitors bind to another part of an enzyme,
causing the enzyme to change shape and making the active site less
effective
• Examples of inhibitors include toxins, poisons, pesticides, and
antibiotics
(a) Normal binding (b) Competitive inhibition (c) Noncompetitive
inhibition
Substrate

Active
site
Competitive
inhibitor

Enzyme

Noncompetitive
inhibitor
Feedback Inhibition
• In feedback inhibition, the end product of a metabolic pathway shuts
down the pathway
• Feedback inhibition prevents a cell from wasting chemical resources
by synthesizing more product than is needed
 Initial
substrate
Active site (threonine)
available Threonine
in active site

Enzyme 1
(threonine
Isoleucine
deaminase)
used up by
cell
Intermediate A
Active site of Feedback
enzyme 1 is inhibition Enzyme 2
no longer able
to catalyze the
Intermediate B
conversion
of threonine to Enzyme 3
intermediate A;
pathway is Intermediate C
switched off. Isoleucine
binds to Enzyme 4
allosteric
site. Intermediate D

Enzyme 5

End product
(isoleucine)