ENZYMES

Chapter 10 Lecture
General, Organic, and Biological

Chemistry: An Integrated Approach
LauraFrost,ToddDealandKarenTimberlake
byRichardTriplett
Chapter 10
EnzymesNatures Chemists
Chapter Outline
10.1 Enzymes and Their Substrates
10.2 Thermodynamics of Chemical Reactions
10.3 Enzymes and Catalysis
10.4 Factors That Affect Enzyme Activity
2011 Pearson Education, Inc.
Chapter 10
Introduction
Enzymes are biologically active proteins that
accelerate the breakdown of food that is eaten.
Enzymes are biological catalysts. They
accelerate reactions, but are not consumed or
changed in reactions.
Discussions on the production or consumption of
energy, specifically heat, during chemical
reactions is called thermodynamics.
Chapter 10

Enzymes are large proteins with complex, threedimensional structures.
Enzymes work in an aqueous environment in our
body so that the protein chain folds such that the
polar amino acids are on the surface.
Consider hexokinase, an enzyme whose job is to
transfer a phosphate group from the high energy
molecule, adenosine triphosphate,
ATP, to D-glucose.
Chapter 10
10.1 Enzymes and Their Substrates, Continued
In this equation, the enzyme name is written

above or below the reaction arrow.
The phosphate group is represented by a P in a
circle.
Chapter 10

The Active Site
The folded structure for hexokinase is shown here.
Chapter 10

When in its proper three-dimensional shape,
hexokinase has an indentation on one side of the
structure.
This indentation is known as the active site, and
it is lined with amino acid side chains.
The active site is the functional part of an
enzyme where catalysis occurs.
Chapter 10

Glucose, the reactant for hexokinase, fits snugly
in the active site. In an enzyme reaction, the
reactant is called the substrate.
Enzymes have specific substrates, a property
known as substrate specificity. For example,
the active site of hexokinase reacts with
D-glucose, but will not react with L-glucose.
Enzymes are specific for one enantiomer of the
substrate.
Chapter 10
Chapter 10

Some enzymes, like hexokinase, have nonprotein helpers. Two categories of helpers are
as follows:
1. Cofactors are inorganic substances like
magnesium ions.
2. Coenzymes are small organic molecules derived
from vitamins. Riboflavin found in the coenzyme
flavin adenine dinucleotide (FAD) is a coenzyme.
Chapter 10
10

EnzymeSubstrate Models
A substrate is drawn into the active site by
intermolecular attractions like hydrogen bonding.
Hydrogen bonding orients the substrate properly
within the active site.
The initial interaction of the enzyme with the
substrate is called the enzymesubstrate
complex (ES). This complex forms prior to
catalysis.
Chapter 10
11

There are two enzymesubstrate models:
1. In the Lock-and-key model, the active site
is thought to be a rigid, inflexible shape that
is an exact complement to the shape of the
substrate. The substrate fits in the active site
much like a key fits in a lock.
2. In the induced-fit model, the active site is
flexible, has a shape roughly complementary
to the shape of its substrate, and undergoes
a conformational change, adjusting to the
shape of the substrate when the substrate
interacts with the enzyme.
Chapter 10
12
Chapter 10
13

A good example of an induced-fit model is when
hexokinase and glucose form an enzyme
substrate complex as shown.
Chapter 10
14

As chemical reactions occur, some bonds are
formed and some are broken, and in the
process, the amount of energy changes.
Some reactions release energy as heat
(exothermic reactions), and some absorb
energy as heat (endothermic reactions).
A collision of reactant molecules must occur for a
chemical reaction to occur.
Chapter 10
15
10.2 Thermodynamics of Chemical Reactions,

Continued
Energy is required to cause reactant molecules
to collide.
Reactant molecules must be aligned properly in
order for a reaction to occur.
Activation energy is required to properly align
reactant molecules and to cause them to collide
to produce products.
Chapter 10
16

Continued
If the energy that is available is lower than the
activation energy, the molecules will not collide
with enough force to form products.
Chapter 10
17

Continued
The activation energy that must be overcome
before products are formed is shown as:
The heat of reaction is the difference between the

energy of reactants and the energy of products.
Chapter 10
18

Continued
In an exothermic reaction, the energy of
reactants is higher than the energy of products,
so heat is released.
In an endothermic reaction, the energy of
products is higher than the energy of reactants,
so heat is absorbed.
The height of the activation energy peak gives an
indication of how fast the reaction proceeds.
Chapter 10
19

Continued
Reactions with a low activation energy will
proceed at a faster rate than reactions with a
high activation energy.
Activation energy can be lowered with a catalyst,
which will cause the reaction to proceed at a
faster rate.
A catalyst will not affect the energy of products or
reactants.
Chapter 10
20

Continued
An enzyme-catalyzed reaction increases the rate
of a reaction by forming ES before forming a
product.
Chapter 10
21

Continued
Consider the addition of hydrogen peroxide to a
cut. The area bubbles considerably because
oxygen is produced by the enzyme catalase
found in blood.
A high concentration of oxygen is produced at

the wound site that kills germs.
Without catalase, this reaction occurs very
slowly.
Chapter 10
22

Enzymes lower the activation energy by forming
ES complex.
ES is formed through the interactions between the
enzyme and substrate. Each interaction releases a
small amount of energy to stabilize the complex.
These interactions combine to lower the activation
energy of the reaction.
Some interactions that help lower the activation
energy are discussed in the next several slides .
Chapter 10
23
10.3 Enzymes and Catalysis, Continued

Proximity
The active site of enzymes has a small volume.
When ES forms, the active site is filled with
substrate.
The reacting molecules are in close proximity to
each other, and the closer they are the more likely
a reaction will occur.
Amino acid side chains in the active site are used
to facilitate the reaction.
Chapter 10
24

Orientation
In the active site, substrate molecules are held at
the appropriate distance and in correct alignment
to each other for the reaction to occur.
Amino acid side chains in the active site create
interactions that orient the substrates.
This lowers the activation energy needed for the
reaction to occur.
Chapter 10
25

Proper orientation is shown as:
Chapter 10
26

Bond Energy
When an enzyme interacts with substrate to
form ES, the bonds of the substrate molecule
are weakened (strained).
Strained bonds in the substrate means that the
reaction will proceed more rapidly because the
activation energy is lowered by this effect.
Chapter 10
27

Consider the hexokinase reaction that catalyzes
glucose to glucose-6-phosphate.
Mg2+ (a coenzyme) holds ATP in one area of the
active site and glucose interacts with another
area.
Amino acid side chains in the active site form
multiple hydrogen bonds with glucose, which
stabilizes ES and lowers the activation energy.
Chapter 10
28

A conformational change in the enzyme occurs
when glucose enters the active site.
ATP is in close proximity to the glucose and is in
proper orientation for the reaction.
Glucose-6-phosphate is formed along with ADP.
The enzyme is less attracted to the products, so
the lobes of the enzyme move apart and the
products are released.
Chapter 10
29

This figure shows the formation of
glucose-6-phosphate by hexokinase.
Chapter 10
30

If allowed to sit untouched, the flesh of sliced
apples will turn brown by a process known as
oxidation, caused by an enzyme.
If lemon juice is sprinkled on the sliced apple, the
vitamin C in the lemon juice will inhibit the
formation of this brown color by changing the pH
of the environment of the enzyme.
Enzyme reactions are affected by reaction
conditions such as substrate concentration, pH,
temperature, and the presence of inhibitors.
Chapter 10
31
10.4 Factors That Affect Enzyme Activity,

Continued
Substrate Concentration
Recall that the first step in an enzyme-catalyzed
reaction is the formation of ES.
At a constant concentration of enzyme, an
increase in substrate concentration will cause an
increase in the enzyme activity up to the point
where the enzyme becomes saturated with
substrate.
Chapter 10
32

Continued
Increasing substrate concentration will not affect
the rate of the reaction.
A condition known as steady state is when an
enzyme is operating under maximum activity.
Chapter 10
33

Continued
pH
When the enzyme environment is changed by
pH, its tertiary structure is disrupted, altering the
active site and causing the enzymes activity to
decrease.
Enzymes are most active at a pH known as their
optimum pH.
At optimum pH, the enzyme maintains its tertiary
structure and its active site.
Chapter 10
34

Continued
Changes in pH will also affect the nature of the
amino acid side chains in the active site.
The optimum pH for enzymes is based on the
location of the enzymes as shown:
Chapter 10
35

Continued
Temperature
Enzymes have an optimum temperature at
which they are most active.
The optimum temperature for most human
enzymes is normal body temperature, 37 oC.
Above optimum temperature, enzymes lose
activity due to disruption of intermolecular forces
stabilizing the tertiary structure.
Chapter 10
36

Continued
At high temperatures, enzymes denature, which
modifies the active site.
At low temperatures, enzyme activity is low due
to a lack of energy for the reaction to occur.
Food is stored in a refrigerator or freezer to slow
spoilage brought on by enzymes.
Boiling contaminated water will destroy enzymes
in bacteria that are present in the water.
Chapter 10
37

Continued
Inhibitors
Inhibitors are types of molecules that will cause
enzymes to lose activity.
Enzyme inhibitors prevent the active site from
interacting with substrate to form ES.
Some inhibitors cause temporary loss of activity,
while others cause permanent loss of activity.
Chapter 10
38

Continued
Reversible inhibition occurs when the inhibitor
causes a temporary loss of activity. However,
activity is regained if the inhibitor is removed.
Reversible inhibitors can be competitive or
noncompetitive.
Competitive inhibitors are molecules that
compete with a substrate for the active site, and
have a structure similar to the substrate.
Chapter 10
39

Continued
As long as an inhibitor remains in the active site,
the enzyme cannot react with the substrate to form
product.
Chapter 10
40

Continued
An example of a medical therapy that involves a
competitive inhibitor involves liver alcohol
dehydrogenase (LAD). This enzyme oxidizes
ethanol, the alcohol found in alcoholic
beverages.
This enzyme will also react with ethylene glycol
and methanol, which are found in antifreeze, and
will compete with ethanol for the active site.
If a pet is poisoned by drinking antifreeze, a slow
intravenous infusion of ethanol is administrated.
Chapter 10
41

Continued
Administration of ethanol slows the production of
the toxic metabolites of ethylene glycol and
methanol, giving the kidneys time to eliminate
these two substrates.
Noncompetitive inhibitors do not resemble the
substrate. They do not compete for the enzymes
active site.
Noncompetitive inhibitors bind at a site on the
enzyme that is usually remote to the active site.
Chapter 10
42

Continued
When a noncompetitive inhibitor binds to an
enzyme, it causes a conformational change in
the enzyme. This change in shape causes the
active site to no longer interact with the
substrate.
As long as this type of inhibitor is bound to the
enzyme, it will no longer function effectively.
Chapter 10
43

Continued
This figure diagrams how a noncompetitive inhibitor
functions.
Chapter 10
44

Continued
Inhibitions caused by competitive and
noncompetitive inhibitors can be reversed.
Inhibition by competitive inhibitors can be
reversed by adding more substrate. The higher
the concentration of substrate, the more likely it
will overcome the competition for the active site.
Adding more substrate with noncompetitive
inhibitors has no effect on overcoming inhibition.
Chapter 10
45

Continued
Reversing a noncompetitive inhibitor requires a
special chemical reagent to remove the inhibitor
and restore catalytic activity.
An irreversible inhibitor forms a covalent bond
with an amino acid side chain in the enzymes
active site.
Irreversible inhibition causes the substrate to be
excluded from the active site.
Irreversible inhibition is a permanent inhibition.
Chapter 10
46

Continued
Irreversible inhibition is demonstrated in this
figure.
Heavy metals like silver, mercury, and lead are

examples of irreversible inhibitors.
Chapter 10
47

Continued
Antibiotics Inhibit Bacterial Enzymes
Enzyme inhibitors are used to fight bacterial
infections.
Penicillin is an example of an irreversible inhibitor.
It binds to the enzyme that bacteria use to
synthesize cell walls, and slows the growth of cell
walls.
Without a cell wall, bacteria cannot survive and the
infection stops.
Chapter 10
48
Chapter Summary
Enzymes are large, globular proteins that serve
as biological catalysts.
The functional part of an enzyme is the active
site.
Substrates are the reactants for an enzyme
reaction, and they bind to the active site to form
ES.
Chapter 10
49
Chapter Summary, Continued

Enzymes are specific for one substrate that will
bind to the active site and react.
Two theories, lock-and-key and induced-fit,
explain how an enzyme interacts with its
substrate to form ES.
Chapter 10
50

Thermodynamics is a study of the energy changes
that occur during a chemical reaction.
Activation energy is the energy required to start a
reaction, and plays a role in the rate of reaction.
The lower the activation energy, the faster the rate of
reaction.
Heat of reaction is a measure of the production or
consumption of energy in a reaction.
Chapter 10
51

Continued
An exothermic reaction releases heat to its environment.
An endothermic reaction absorbs heat from its
environment.
Catalysts lower the activation energy causing an increase
in the rate of reaction.
Enzymes form ES before catalysis, which causes a
lowering of the activation energy.
Chapter 10
52

Formation of the ES complex lowers the
activation energy for a catalyzed reaction.
In the active site, atoms are brought close
together and aligned with amino acid side
chains.
Chapter 10
53

The active site also aligns the reactants with the
optimal orientation for a reaction to occur.
The interaction of substrate with the active site
weakens bonds between atoms in the substrate
so the reaction can form products easier.
Chapter 10
54

Factors such as pH, temperature, substrate
concentration, and the presence of inhibitors can
affect the activity of an enzyme.
An increase in substrate concentration increases
the rate of an enzyme-catalyzed reaction. When
substrate concentration is increased, the active
site becomes saturated with substrate.
Chapter 10
55

Continued
When the active site is saturated, the enzyme is
operating at steady state.
Enzymes have an optimum pH and temperature at
which they function best.
Inhibitors decrease or eliminate an enzymes
catalytic abilities.
Chapter 10
56

Continued
The effect of inhibitors can be reversible or
irreversible.
Reversible inhibitors can be competitive inhibitors,
which compete with the substrate for the active site.
Reversible inhibitors can also be noncompetitive,
which bind to a site on the enzyme other than the
active site, and causes a conformational change in the
enzyme.
Chapter 10
57

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Chapter 10 Lecture

General, Organic, and Biological

2011 Pearson Education, Inc.

10.1 Enzymes and Their Substrates

10.1 Enzymes and Their Substrates, Continued

In this equation, the enzyme name is written

2011 Pearson Education, Inc.

10.1 Enzymes and Their Substrates, Continued

2011 Pearson Education, Inc.

10.1 Enzymes and Their Substrates, Continued

2011 Pearson Education, Inc.

10.1 Enzymes and Their Substrates, Continued

10.1 Enzymes and Their Substrates, Continued

2011 Pearson Education, Inc.

10.1 Enzymes and Their Substrates, Continued

2011 Pearson Education, Inc.

10.1 Enzymes and Their Substrates, Continued

10.1 Enzymes and Their Substrates, Continued

10.1 Enzymes and Their Substrates, Continued

2011 Pearson Education, Inc.

10.1 Enzymes and Their Substrates, Continued

2011 Pearson Education, Inc.

10.2 Thermodynamics of Chemical Reactions

10.2 Thermodynamics of Chemical Reactions,

2011 Pearson Education, Inc.

10.2 Thermodynamics of Chemical Reactions,

2011 Pearson Education, Inc.

10.2 Thermodynamics of Chemical Reactions,

The heat of reaction is the difference between the

10.2 Thermodynamics of Chemical Reactions,

10.2 Thermodynamics of Chemical Reactions,

10.2 Thermodynamics of Chemical Reactions,

2011 Pearson Education, Inc.

10.2 Thermodynamics of Chemical Reactions,

A high concentration of oxygen is produced at

10.3 Enzymes and Catalysis

10.3 Enzymes and Catalysis, Continued

10.3 Enzymes and Catalysis, Continued

10.3 Enzymes and Catalysis, Continued

2011 Pearson Education, Inc.

10.3 Enzymes and Catalysis, Continued

2011 Pearson Education, Inc.

10.3 Enzymes and Catalysis, Continued

10.3 Enzymes and Catalysis, Continued

10.3 Enzymes and Catalysis, Continued

2011 Pearson Education, Inc.

10.4 Factors That Affect Enzyme Activity

10.4 Factors That Affect Enzyme Activity,

10.4 Factors That Affect Enzyme Activity,

2011 Pearson Education, Inc.

10.4 Factors That Affect Enzyme Activity,

10.4 Factors That Affect Enzyme Activity,

2011 Pearson Education, Inc.

10.4 Factors That Affect Enzyme Activity,

10.4 Factors That Affect Enzyme Activity,

10.4 Factors That Affect Enzyme Activity,

10.4 Factors That Affect Enzyme Activity,

10.4 Factors That Affect Enzyme Activity,

2011 Pearson Education, Inc.

10.4 Factors That Affect Enzyme Activity,

2011 Pearson Education, Inc.

10.4 Factors That Affect Enzyme Activity,

10.4 Factors That Affect Enzyme Activity,

2011 Pearson Education, Inc.