Bio201 Lecture 12 Enzymes - Energy & Metabolism

8 Energy, Enzymes, and
Metabolism
8 Energy, Enzymes, and Metabolism
• 8.1 What Physical Principles Underlie

Biological Energy Transformations?
• 8.2 What Is the Role of ATP in
Biochemical Energetics?
• 8.3 What Are Enzymes?
• 8.4 How Do Enzymes Work?
• 8.5 How Are Enzyme Activities Regulated?
8.1 What Physical Principles Underlie Biological Energy
Transformations?
Energy: is the capacity to do work.
Transformation of energy is required by

living things.
The first of thermodynamics

A fundamental law is that energy can be
transformed fom one form to another but
cannot be created or destroyed.
Transformations?
All forms of energy can be placed in two

categories:
• Potential energy is stored energy—such

as concentration gradient,
• Kinetic energy is the energy of

movement
Figure 8.1 Energy Conversions and Work
Transformations?
Metabolism: Sum total of all chemical

reactions in an organism.
1) Anabolic reactions: synthesis (building)

of complex molecules from simple
molecules; energy input is required.
2) Catabolic reactions: breaking down of

complex molecules into to simpler ones;
energy is released. (ex. DIGESTION)
Transformations?
Change in energy can be measured in calories or joules.
Change in free energy (ΔG) in a reaction is the difference in

free energy of the products and the reactants.
ΔGreaction = Gproducts - Greactants
• If ΔG is negative, free energy is released-exergonic

reaction.
• If ΔG is positive, free energy is consumed-endergonic reaction
If free energy is not available, the reaction does not occur.

Transformations?
Exergonic reactions release free energy (–ΔG):

Catabolism (breakdown)
Transformations?
Endergonic reactions consume free energy

(+ΔG): Anabolism (creation)
Transformations?
In principle, chemical reactions can run in

both directions.
Forward and reverse reactions are

balanced.
A B
The concentrations of A and B determine
which direction will be favored.
At chemical equilibrium, ΔG = 0
Recap
• What is the difference between potential energy and

kinetic energy
• What is the difference between anabolism and
catabolism?
• What is the difference between endergonic and exergonic
reactions and the importance of ΔG?
8.2 What Is the Role of ATP in Biochemical Energetics?
Currency of biological energy is ATP

• ATP (adenosine
triphosphate) captures
and transfers free
energy.
• ATP releases a large
amount of energy when
hydrolyzed.
• ATP can phosphorylate,
or donate phosphate
groups to other
molecules.
Figure 8.6 Coupling of Reactions
Exergonic and endergonic reactions are coupled.

8.3 What Are Enzymes?
Catalysts speed up the rate of a reaction.
The catalyst is not altered by the reactions.
Most biological catalysts are enzymes

(proteins) that act as a framework in which
reactions can take place.
Activation energy:
Some reactions require energy to start the

reaction - activation energy (Ea).
• Changes the reactants into unstable forms

(higher free energy)—transition state
intermediates.
• Enzymes lower the energy barrier by bringing

the reactants together.
Figure 8.8 Activation Energy Initiates Reactions (Part 1)
Figure 8.8 Activation Energy Initiates Reactions (Part 2)
Enzymes:
•Biological catalysts and are
highly specific.
•Reactants are called substrates.
•Substrate molecules bind to the

active site of the enzyme.
•The three-dimensional shape of

the enzyme determines the
specificity.
Binding of a substrate to the active site of an
enzyme produces an enzyme-substrate
complex (ES)
E + S → ES → E + P
E = Enzyme, S = Substrate, P = Product
The enzyme may change when bound to the

substrate, but returns to its original form.
Figure 8.9 Enzyme and Substrate
• Enzymes lower the energy barrier for reactions.
• The final equilibrium does not change, and ΔG does

not change.
Recap
• Explain how the structure of an enzyme

makes that enzyme specific.
• What is the relationship between an

enzyme and the equilibrium point of a
reaction?
8.4 How Do Enzymes Work?
Enzymes can speed up reactions by several

mechanisms:
1. Orient substrates
2. Induce strain in the
substrate
3. Temporarily add chemical
groups to substrates
Figure 8.11 Life at the Active Site (A)
Enzymes orient substrate molecules, bringing

together the atoms that will bind.
Figure 8.11 Life at the Active Site (B)
Enzymes can stretch the bonds in substrate

molecules, making them unstable.
Figure 8.11 Life at the Active Site (C)
Enzymes can temporarily add chemical

groups to substrates.
Enzyme adds charges to the substrate.

Figure 8.12 Some Enzymes Change Shape When Substrate Binds to Them
Many enzymes change shape when they bind

to the substrate—induced fit.
Figure 8.13 Catalyzed Reactions Reach a Maximum Rate
The rate of a catalyzed reaction depends on

substrate concentration.
At saturation, all enzymes are bound to substrate
—maximum rate.
8.5 How Are Enzyme Activities Regulated?
Thousands of chemical
reactions are
occurring in cells
simultaneously.
The reactions are
organized in metabolic
pathways. Each
reaction is catalyzed
by a specific enzyme.
Enzymes are regulated by inhibitors:

Molecules that bind to the enzyme and
slow reaction rates.
Two kinds:
1. Irreversible inhibition
2. Reversible inhibition
a. Competitive
b. Non-competitive
Irreversible inhibition: Inhibitor covalently

binds to side chains in the active site—
permanently inactivates the enzyme.
Reversible inhibition:
a) Competitive inhibitors compete with
the natural substrate for binding sites.
When concentration of competitive
inhibitor is reduced, it detaches from the
active site.
b) Noncompetitive inhibitors: Bind to the
enzyme at a different site (not the active
site).
The enzyme changes shape and alters the
active site.
Figure 8.16 Reversible Inhibition (A)
Effect of pH & temperature on enzyme activity:

• pH influences the ionization of functional
groups.
• Every enzyme has an optimal temperature. At high
temperatures, non-covalent bonds begin to break.
Enzyme can lose its tertiary structure and become
denatured.

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8 Energy, Enzymes, and

• 8.1 What Physical Principles Underlie

Energy: is the capacity to do work.

Transformation of energy is required by

The first of thermodynamics

All forms of energy can be placed in two

• Potential energy is stored energy—such

• Kinetic energy is the energy of

Metabolism: Sum total of all chemical

1) Anabolic reactions: synthesis (building)

2) Catabolic reactions: breaking down of

Change in free energy (ΔG) in a reaction is the difference in

ΔGreaction = Gproducts - Greactants

• If ΔG is negative, free energy is released-exergonic

• If ΔG is positive, free energy is consumed-endergonic reaction

If free energy is not available, the reaction does not occur.

Exergonic reactions release free energy (–ΔG):

Endergonic reactions consume free energy

In principle, chemical reactions can run in

Forward and reverse reactions are

• What is the difference between potential energy and

Currency of biological energy is ATP

Exergonic and endergonic reactions are coupled.

Catalysts speed up the rate of a reaction.

The catalyst is not altered by the reactions.

Most biological catalysts are enzymes

Some reactions require energy to start the

• Changes the reactants into unstable forms

• Enzymes lower the energy barrier by bringing

•Reactants are called substrates.

•Substrate molecules bind to the

•The three-dimensional shape of

The enzyme may change when bound to the

• The final equilibrium does not change, and ΔG does

• Explain how the structure of an enzyme

• What is the relationship between an

Enzymes can speed up reactions by several

Enzymes orient substrate molecules, bringing

Enzymes can stretch the bonds in substrate

Enzymes can temporarily add chemical

Enzyme adds charges to the substrate.

Many enzymes change shape when they bind

The rate of a catalyzed reaction depends on

Enzymes are regulated by inhibitors:

Irreversible inhibition: Inhibitor covalently

Effect of pH & temperature on enzyme activity:

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